Updated on 2024/02/02

写真a

 
TERAHARA Naoya
 
Organization
Faculty of Science and Engineering Research Associate
Contact information
The inquiry by e-mail is 《here
External link

Degree

  • 博士(生命科学) ( 東洋大学 )

  • 修士(生命科学) ( 東洋大学 )

Education

  • 2009.3
     

    Toyo University   doctor course   completed

  • 2006.3
     

    Toyo University   master course   completed

  • 2005.3
     

    Toyo University   graduated

  • 2001.3
     

    埼玉県立越ヶ谷高等学校普通科   graduated

Research History

  • 2019.4 - Now

    Chuo University   Assistant Professor

  • 2019.4 -  

    中央大学理工学部助教

  • 2016.4 - 2019.3

    大阪大学大学院   生命機能研究科   特任助教

  • 2013.4 - 2016.3

    大阪大学大学院   生命機能研究科   特任研究員

  • 2010.4 - 2013.3

    日本学術振興会特別研究員(PD)   大阪大学

  • 2009.4 - 2010.3

    Toyo University

  • 2007.4 - 2009.3

    日本学術振興会特別研究員(DC2)   東洋大学

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Professional Memberships

  • 日本農芸化学会

  • 極限環境微生物学会

  • THE BIOPHYSICAL SOCIETY OF JAPAN

Research Interests

  • 1分子計測

  • 分子モーター

  • 細菌べん毛

  • 膜タンパク質

  • イオンチャネル

Research Areas

  • Life Science / Biophysics

Papers

  • Below 3 Å structure of apoferritin using a multipurpose TEM with a side entry cryoholder Reviewed International journal

    Yoko Kayama, Raymond N Burton-Smith, Chihong Song, Naoya Terahara, Takayuki Kato, Kazuyoshi Murata

    Scientific Reports   11   8395   2021.4

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    Recently, the structural analysis of protein complexes by cryo-electron microscopy (cryo-EM) single particle analysis (SPA) has had great impact as a biophysical method. Many results of cryo-EM SPA are based on data acquired on state-of-the-art cryo-electron microscopes customized for SPA. These are currently only available in limited locations around the world, where securing machine time is highly competitive. One potential solution for this time-competitive situation is to reuse existing multi-purpose equipment, although this comes with performance limitations. Here, a multi-purpose TEM with a side entry cryo-holder was used to evaluate the potential of high-resolution SPA, resulting in a 3 Å resolution map of apoferritin with local resolution extending to 2.6 Å. This map clearly showed two positions of an aromatic side chain. Further, examination of optimal imaging conditions depending on two different multi-purpose electron microscope and camera combinations was carried out, demonstrating that higher magnifications are not always necessary or desirable. Since automation is effectively a requirement for large-scale data collection, and augmenting the multi-purpose equipment is possible, we expanded testing by acquiring data with SerialEM using a β-galactosidase test sample. This study demonstrates the possibilities of more widely available and established electron microscopes, and their applications for cryo-EM SPA.

    DOI: 10.1038/s41598-021-87183-1

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  • Dynamic exchange of two types of stator units in Bacillus subtilis flagellar motor in response to environmental changes Reviewed International journal

    Naoya Terahara, Keiichi Namba, Tohru Minamino

    Computational and Structural Biotechnology Journal   18   2897 - 2907   2020.10

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    Bacteria can migrate towards more suitable environments by rotating flagella that are under the control of sensory signal transduction networks. The bacterial flagellum is composed of the long helical filament functioning as a propeller, the flexible hook as a universal joint and the basal body as a rotary motor powered by ion motive force across the cell membrane. The flagellar motor consists of a rotor and multiple stator units, each of which couples the ion flow through its ion channel with force generation. The flagellar building blocks and motor proteins are highly conserved among bacterial species, but structural and functional diversity of flagella has also been revealed. It has been reported that the structure and function of the flagellar motor of a Gram-positive bacterium, Bacillus subtilis, differ from those of Escherichia coli and Salmonella. The flagellar motor of the B. subtilis BR151MA strain possesses two distinct types of stator complexes, H+-type MotAB and Na+-type MotPS, around the rotor. These two types of stator units dynamically assemble to and disassemble from the rotor in response to environmental changes such as viscosity and external Na+ concentrations. In this mini-review article, we describe our recent understanding of the structure and dynamics of the B. subtilis flagellar motor.

    DOI: 10.1016/j.csbj.2020.10.009

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  • Coupling ion specificity of the flagellar stator proteins MotA1/MotB1 of Paenibacillus sp. TCA20 Reviewed International journal

    Sakura Onoe, Myu Yoshida, Naoya Terahara, Yoshiyuki Sowa

    Biomolecules   10 ( 7 )   1078   2020.7

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    The bacterial flagellar motor is a reversible rotary molecular nanomachine, which couples ion flux across the cytoplasmic membrane to torque generation. It comprises a rotor and multiple stator complexes, and each stator complex functions as an ion channel and determines the ion specificity of the motor. Although coupling ions for the motor rotation were presumed to be only monovalent cations, such as H+ and Na+, the stator complex MotA1/MotB1 of Paenibacillus sp. TCA20 (MotA1TCA/MotB1TCA) was reported to use divalent cations as coupling ions, such as Ca2+ and Mg2+. In this study, we initially aimed to measure the motor torque generated by MotA1TCA/MotB1TCA under the control of divalent cation motive force; however, we identified that the coupling ion of MotA1TCAMotB1TCA is very likely to be a monovalent ion. We engineered a series of functional chimeric stator proteins between MotB1TCA and Escherichia coli MotB. E. coli ΔmotAB cells expressing MotA1TCA and the chimeric MotB presented significant motility in the absence of divalent cations. Moreover, we confirmed that MotA1TCA/MotB1TCA in Bacillus subtilis ΔmotABΔmotPS cells generates torque without divalent cations. Based on two independent experimental results, we conclude that the MotA1TCA/MotB1TCA complex directly converts the energy released from monovalent cation flux to motor rotation.

    DOI: 10.3390/biom10071078

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  • Structural and functional comparison of Salmonella flagellar filaments composed of FljB and FliC Reviewed International journal

    Tomoko Yamaguchi, Shoko Toma, Naoya Terahara, Tomoko Miyata, Masamichi Ashihara, Tohru Minamino, Keiichi Namba, Takayuki Kato

    Biomolecules   10 ( 2 )   246   2020.2

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    The bacterial flagellum is a motility organelle consisting of a long helical filament as a propeller and a rotary motor that drives rapid filament rotation to produce thrust. Salmonellaenterica serovar Typhimurium has two genes of flagellin, fljB and fliC, for flagellar filament formation and autonomously switches their expression at a frequency of 10-3-10-4 per cell per generation. We report here differences in their structures and motility functions under high-viscosity conditions. A Salmonella strain expressing FljB showed a higher motility than one expressing FliC under high viscosity. To examine the reasons for this motility difference, we carried out structural analyses of the FljB filament by electron cryomicroscopy and found that the structure was nearly identical to that of the FliC filament except for the position and orientation of the outermost domain D3 of flagellin. The density of domain D3 was much lower in FljB than FliC, suggesting that domain D3 of FljB is more flexible and mobile than that of FliC. These differences suggest that domain D3 plays an important role not only in changing antigenicity of the filament but also in optimizing motility function of the filament as a propeller under different conditions.

    DOI: 10.3390/biom10020246

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  • CryoTEM with a cold emission gun that moves structural biology into a new stage Reviewed

    Takayuki Kato, Fumiaki Makino, Takanori Nakane, Naoya Terahara, Takeshi Kaneko, Yuko Shimizu, Sohei Motoki, Isamu Ishikawa, Koji Yonekura, Keiichi Namba

    Microscopy and Microanalysis   25 ( 2 )   998 - 999   2019.8

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    Language:English   Publishing type:Research paper (international conference proceedings)   Publisher:Cambridge University Press (CUP)  

    DOI: 10.1017/s1431927619005725

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  • Structural insights into the substrate specificity switch mechanism of the type III protein export apparatus. Reviewed International journal

    Yumi Inoue, Yuya Ogawa, Miki Kinoshita, Naoya Terahara, Masafumi Shimada, Noriyuki Kodera, Toshio Ando, Keiichi Namba, Akio Kitao, Katsumi Imada, Tohru Minamino

    Structure   27 ( 6 )   965 - 976   2019.6

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    Bacteria use a type III protein export apparatus for construction of the flagellum, which consists of the basal body, the hook, and the filament. FlhA forms a homo-nonamer through its C-terminal cytoplasmic domains (FlhAC) and ensures the strict order of flagellar assembly. FlhAC goes through dynamic domain motions during protein export, but it remains unknown how it occurs. Here, we report that the FlhA(G368C) mutation biases FlhAC toward a closed form, thereby reducing the binding affinity of FlhAC for flagellar export chaperones in complex with their cognate filament-type substrates. The G368C mutations also restrict the conformational flexibility of a linker region of FlhA (FlhAL), suppressing FlhAC ring formation. We propose that interactions of FlhAL with its neighboring subunit converts FlhAC in the ring from a closed conformation to an open one, allowing the chaperon/substrate complexes to bind to the FlhAC ring to form the filament at the hook tip.

    DOI: 10.1016/j.str.2019.03.017

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  • Novel insights into conformational rearrangements of the bacterial flagellar switch complex Reviewed International journal

    Tomofumi Sakai, Tomoko Miyata, Naoya Terahara, Koichiro Mori, Yumi Inoue, Yusuke V Morimoto, Takayuki Kato, Keiichi Namba, Tohru Minamino

    mBio   10 ( 2 )   e00079-19   2019.4

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    The flagellar motor can spin in both counterclockwise (CCW) and clockwise (CW) directions. The flagellar motor consists of a rotor and multiple stator units, which act as a proton channel. The rotor is composed of the transmembrane MS ring made of FliF and the cytoplasmic C ring consisting of FliG, FliM, and FliN. The C ring is directly involved in rotation and directional switching. The Salmonella FliF-FliG deletion fusion motor missing 56 residues from the C terminus of FliF and 94 residues from the N terminus of FliG keeps a domain responsible for the interaction with the stator intact, but its motor function is reduced significantly. Here, we report the structure and function of the FliF-FliG deletion fusion motor. The FliF-FliG deletion fusion not only resulted in a strong CW switch bias but also affected rotor-stator interactions coupled with proton translocation through the proton channel of the stator unit. The energy coupling efficiency of the deletion fusion motor was the same as that of the wild-type motor. Extragenic suppressor mutations in FliG, FliM, or FliN not only relieved the strong CW switch bias but also increased the motor speed at low load. The FliF-FliG deletion fusion made intersubunit interactions between C ring proteins tighter compared to the wild-type motor, whereas the suppressor mutations affect such tighter intersubunit interactions. We propose that a change of intersubunit interactions between the C ring proteins may be required for high-speed motor rotation as well as direction switching.IMPORTANCE The bacterial flagellar motor is a bidirectional rotary motor for motility and chemotaxis, which often plays an important role in infection. The motor is a large transmembrane protein complex composed of a rotor and multiple stator units, which also act as a proton channel. Motor torque is generated through their cyclic association and dissociation coupled with proton translocation through the proton channel. A large cytoplasmic ring of the motor, called C ring, is responsible for rotation and switching by interacting with the stator, but the mechanism remains unknown. By analyzing the structure and function of the wild-type motor and a mutant motor missing part of the C ring connecting itself with the transmembrane rotor ring while keeping a stator-interacting domain for bidirectional torque generation intact, we found interesting clues to the change in the C ring conformation for the switching and rotation involving loose and tight intersubunit interactions.

    DOI: 10.1128/mBio.00079-19

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  • Autonomous control mechanism of stator assembly in the bacterial flagellar motor in response to changes in the environment Reviewed International journal

    Tohru Minamino, Naoya Terahara, Seiji Kojima, Keiichi Namba

    Molecular Microbiology   109 ( 6 )   723 - 734   2018.8

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    The bacterial flagellar motor is composed of a rotor and a transmembrane ion channel complex that acts as a stator unit. The ion channel complex consists of at least three structural parts: a cytoplasmic domain responsible for the interaction with the rotor, a transmembrane ion channel that forms a pathway for the transit of ions across the cytoplasmic membrane, and a peptidoglycan-binding (PGB) domain that anchors the stator unit to the peptidoglycan (PG) layer. A flexible linker connecting the ion channel and the PGB domain not only coordinates stator assembly with its ion channel activity but also controls the assembly of stator units to the motor in response to changes in the environment. When the ion channel complex encounters the rotor, the N-terminal portion of the PGB domain adopts a partially stretched conformation, allowing the PGB domain to reach and bind to the PG layer. The binding affinity of the PGB domain for the PG layer is affected by the force applied to its anchoring point and to the type of ionic energy source. In this review article, we will present current understanding of autonomous control mechanism of stator assembly in the bacterial flagellar motor.

    DOI: 10.1111/mmi.14092

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  • Insight into structural remodeling of the FlhA ring responsible for bacterial flagellar type III protein export Reviewed

    Naoya Terahara, Yumi Inoue, Noriyuki Kodera, Yusuke V Morimoto, Takayuki Uchihashi, Katsumi Imada, Toshio Ando, Keiichi Namba, Tohru Minamino

    Science Advances   4 ( 4 )   eaao7054   2018.4

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    The bacterial flagellum is a supramolecular motility machine. Flagellar assembly begins with the basal body, followed by the hook and finally the filament. A carboxyl-terminal cytoplasmic domain of FlhA (FlhAC) forms a nonameric ring structure in the flagellar type III protein export apparatus and coordinates flagellar protein export with assembly. However, the mechanism of this process remains unknown. We report that a flexible linker of FlhAC (FlhAL) is required not only for FlhAC ring formation but also for substrate specificity switching of the protein export apparatus from the hook protein to the filament protein upon completion of the hook structure. FlhAL was required for cooperative ring formation of FlhAC. Alanine substitutions of residues involved in FlhAC ring formation interfered with the substrate specificity switching, thereby inhibiting filament assembly at the hook tip. These observations lead us to propose a mechanistic model for export switching involving structural remodeling of FlhAC.

    DOI: 10.1126/sciadv.aao7054

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  • A triangular loop of domain D1 of FlgE is essential for hook assembly but not for the mechanical function Reviewed International journal

    Tomofumi Sakai, Yumi Inoue, Naoya Terahara, Keiichi Namba, Tohru Minamino

    Biochemical and Biophysical Research Communications   495 ( 2 )   1789 - 1794   2018.1

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    The bacterial flagellar hook is a short, curved tubular structure made of FlgE. The hook connects the basal body as a rotary motor and the filament as a helical propeller and functions as a universal joint to smoothly transmit torque produced by the motor to the filament. Salmonella FlgE consists of D0, Dc, D1 and D2 domains. Axial interactions between a triangular loop of domain D1 (D1-loop) and domain D2 are postulated to be responsible for hook supercoiling. In contrast, Bacillus FlgE lacks the D1-loop and domain D2. Here, to clarify the roles of the D1-loop and domain D2 in the mechanical function, we carried out deletion analysis of Salmonella FlgE. A deletion of the D1-loop conferred a loss-of-function phenotype whereas that of domain D2 did not. The D1-loop deletion inhibited hook polymerization. Suppressor mutations of the D1-loop deletion was located within FlgD, which acts as the hook cap to promote hook assembly. This suggests a possible interaction between the D1-loop of FlgE and FlgD. Suppressor mutant cells produced straight hooks, but retained the ability to form a flagellar bundle behind a cell body, suggesting that the loop deletion does not affect the bending flexibility of the Salmonella hook.

    DOI: 10.1016/j.bbrc.2017.12.037

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  • The role of a cytoplasmic loop of MotA in load-dependent assembly and disassembly dynamics of the MotA/B stator complex in the bacterial flagellar motor Reviewed

    Seyedeh Noorolhoda Shajari Pourjaberi, Naoya Terahara, Keiichi Namba, Tohru Minamino

    Molecular Microbiology   106 ( 4 )   646 - 658   2017.11

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    The proton-driven flagellar motor of Salmonella enterica can accommodate a dozen MotA/B stators in a load-dependent manner. The C-terminal periplasmic domain of MotB acts as a structural switch to regulate the number of active stators in the motor in response to load change. The cytoplasmic loop termed MotA(C) is responsible for the interaction with a rotor protein, FliG. Here, to test if MotA(C) is responsible for stator assembly around the rotor in a load-dependent manner, we analyzed the effect of MotA(C) mutations, M76V, L78W, Y83C, Y83H, I126F, R131L, A145E and E155K, on motor performance over a wide range of external load. All these MotA(C) mutations reduced the maximum speed of the motor near zero load, suggesting that they reduce the rate of conformational dynamics of MotA(C) coupled with proton translocation through the MotA/B proton channel. Dissociation of the stators from the rotor by decrease in the load was facilitated by the M76V, Y83H and A145E mutations compared to the wild-type motor. The E155K mutation reduced the number of active stators in the motor from 10 to 6 under extremely high load. We propose that MotA(C) is responsible for load-dependent assembly and disassembly dynamics of the MotA/B stator units.

    DOI: 10.1111/mmi.13843

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  • Na+-induced structural transition of MotPS for stator assembly of the Bacillus flagellar motor Reviewed

    Naoya Terahara, Noriyuki Kodera, Takayuki Uchihashi, Toshio Ando, Keiichi Namba, Tohru Minamino

    Science Advances   3 ( 11 )   eaao4119   2017.11

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER ASSOC ADVANCEMENT SCIENCE  

    The bacterial flagellar motor consists of a rotor and a dozen stator units and regulates the number of active stator units around the rotor in response to changes in the environment. The MotPS complex is a Na+-type stator unit in the Bacillus subtilis flagellar motor and binds to the peptidoglycan layer through the peptidoglycan-binding (PGB) domain of MotS to act as the stator. The MotPS complex is activated in response to an increase in the Na+ concentration in the environment, but the mechanism of this activation has remained unknown. We report that activation occurs by a Na+-induced folding and dimer formation of the PGB domain of MotS, as revealed in real-time imaging by high-speed atomic force microscopy. The MotPS complex showed two distinct ellipsoid domains connected by a flexible linker. A smaller domain, corresponding to the PGB domain, became structured and unstructured in the presence and absence of 150 mM NaCl, respectively. When the amino-terminal portion of the PGB domain adopted a partially stretched conformation in the presence of NaCl, the center-to-center distance between these two domains increased by up to 5 nm, allowing the PGB domain to reach and bind to the peptidoglycan layer. We propose that assembly of the MotPS complex into a motor proceeds by means of Na+-induced structural transitions of its PGB domain.

    DOI: 10.1126/sciadv.aao4119

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  • Load- and polysaccharide-dependent activation of the Na+-type MotPS stator in the Bacillus subtilis flagellar motor Reviewed

    Naoya Terahara, Yukina Noguchi, Shuichi Nakamura, Nobunori Kami-Ike, Masahiro Ito, Keiichi Namba, Tohru Minamino

    Scientific Reports   7   46081   2017.4

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    The flagellar motor of Bacillus subtilis possesses two distinct H+ -type MotAB and Na+ -type MotPS stators. In contrast to the MotAB motor, the MotPS motor functions efficiently at elevated viscosity in the presence of 200 mM NaCl. Here, we analyzed the torque-speed relationship of the Bacillus MotAB and MotPS motors over a wide range of external loads. The stall torque of the MotAB and MotPS motors at high load was about 2,200 pN nm and 220 pN nm, respectively. The number of active stators in the MotAB and MotPS motors was estimated to be about ten and one, respectively. However, the number of functional stators in the MotPS motor was increased up to ten with an increase in the concentration of a polysaccharide, Ficoll 400, as well as in the load. The maximum speeds of the MotAB and MotPS motors at low load were about 200 Hz and 50 Hz, respectively, indicating that the rate of the torque-generation cycle of the MotPS motor is 4-fold slower than that of the MotAB motor. Domain exchange experiments showed that the C-terminal periplasmic domain of MotS directly controls the assembly and disassembly dynamics of the MotPS stator in a load-and polysaccharide-dependent manner.

    DOI: 10.1038/srep46081

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  • The tetrameric MotA complex as the core of the flagellar motor stator from hyperthermophilic bacterium Reviewed

    Norihiro Takekawa, Naoya Terahara, Takayuki Kato, Mizuki Gohara, Kouta Mayanagi, Atsushi Hijikata, Yasuhiro Onoue, Seiji Kojima, Tsuyoshi Shirai, Keiichi Namba, Michio Homma

    Scientific Reports   6   31526   2016.8

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    Rotation of bacterial flagellar motor is driven by the interaction between the stator and rotor, and the driving energy is supplied by ion influx through the stator channel. The stator is composed of the MotA and MotB proteins, which form a hetero-hexameric complex with a stoichiometry of four MotA and two MotB molecules. MotA and MotB are four-and single-transmembrane proteins, respectively. To generate torque, the MotA/MotB stator unit changes its conformation in response to the ion influx, and interacts with the rotor protein FliG. Here, we overproduced and purified MotA of the hyperthermophilic bacterium Aquifex aeolicus. A chemical crosslinking experiment revealed that MotA formed a multimeric complex, most likely a tetramer. The three-dimensional structure of the purified MotA, reconstructed by electron microscopy single particle imaging, consisted of a slightly elongated globular domain and a pair of arch-like domains with spiky projections, likely to correspond to the transmembrane and cytoplasmic domains, respectively. We show that MotA molecules can form a stable tetrameric complex without MotB, and for the first time, demonstrate the cytoplasmic structure of the stator.

    DOI: 10.1038/srep31526

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  • A Bacillus flagellar motor that can use both Na+ and K+ as a coupling ion is converted by a single mutation to use only Na+ Reviewed

    Naoya Terahara, Motohiko Sano, Masahiro Ito

    PLOS ONE   7 ( 9 )   e46248   2012.9

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    In bacteria, the sodium ion (Na+) cycle plays a critical role in negotiating the challenges of an extremely alkaline and sodium-rich environment. Alkaliphilic bacteria that grow optimally at high pH values use Na+ for solute uptake and flagellar rotation because the proton (H+) motive force is insufficient for use at extremely alkaline pH. Only three types of electrically driven rotary motors exist in nature: the F-type ATPase, the V-type ATPase, and the bacterial flagellar motor. Until now, only H+ and Na+ have been reported as coupling ions for these motors. Here, we report that the alkaliphilic bacterium Bacillus alcalophilus Vedder 1934 can grow not only under a Na+-rich and potassium ion (K+)-poor condition but also under the opposite condition in an extremely alkaline environment. In this organism, swimming performance depends on concentrations of Na+, K+ or Rb+. In the absence of Na+, swimming behavior is clearly K+-dependent. This pattern was confirmed in swimming assays of stator-less Bacillus subtilis and Escherichia coli mutants expressing MotPS from B. alcalophilus (BA-MotPS). Furthermore, a single mutation in BA-MotS was identified that converted the naturally bi-functional BA-MotPS to stators that cannot use K+ or Rb+. This is the first report that describes a flagellar motor that can use K+ and Rb+ as coupling ions. The finding will affect the understanding of the operating principles of flagellar motors and the molecular mechanisms of ion selectivity, the field of the evolution of environmental changes and stresses, and areas of nanotechnology.

    DOI: 10.1371/journal.pone.0046248

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  • 3P287 Molecular phylogenetic analysis of flagellar stator proteins of alkaliphilic Bacillus species(Genome biology: Genome analysis,The 48th Annual Meeting of the Biophysical Society of Japan)

    Terahara Naoya, Noguchi Yukina, Nakano Yuko, Namba Keiichi, Ito Masahiro

    Seibutsu Butsuri   50 ( 2 )   S196   2010

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    DOI: 10.2142/biophys.50.S196_2

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  • Motility and chemotaxis in alkaliphilic Bacillus species Reviewed

    Shun Fujinami, Naoya Terahara, Terry Ann Krulwich, Masahiro Ito

    Future Microbiology   4 ( 9 )   1137 - 1149   2009.11

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    Alkaliphilic Bacillus species grow at pH values up to approximately 11. Motile alkaliphilic Bacillus use electrochemical gradients of Na(+) (sodium-motive force) to power ion-coupled, flagella-mediated motility as opposed to the electrochemical gradients of H(+) (proton-motive force) used by most neutralophilic bacteria. Membrane-embedded stators of bacterial flagella contain ion channels through which either H(+) or Na(+) flow to energize flagellar rotation. Stators of the major H-coupled type, MotAB, are distinguishable from Na(+)-coupled stators, PomAB of marine bacteria and MotPS of alkaliphilic Bacillus. Dual ion-coupling capacity is found in neutralophilic Bacillus strains with both MotAB and MotPS. There is also a MotAB variant that uses both coupling ions, switching as a function of pH. Chemotaxis of alkaliphilic Bacillus depends upon flagellar motility but also requires a distinct voltage-gated NaChBac-type channel. The two alkaliphile Na(+) channels provide new vistas on the diverse adaptations of sensory responses in bacteria.

    DOI: 10.2217/FMB.09.76

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  • 3P-140 Analysis of the conserved charged residues in flagellar stator proteins Mot A and MotP of Bacillus subtilis.(Molecular motor,The 47th Annual Meeting of the Biophysical Society of Japan)

    Takahashi Yuka, Terahara Naoya, Koizumi Yukiyo, Ito Masahiro

    Seibutsu Butsuri   49   S174 - S175   2009

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    Language:English   Publisher:The Biophysical Society of Japan General Incorporated Association  

    DOI: 10.2142/biophys.49.S174_5

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  • Mutations alter the sodium versus proton use of a Bacillus clausii flagellar motor and confer dual ion use on Bacillus subtilis motors Reviewed

    Naoya Terahara, Terry Ann Krulwich, Masahiro Ito

    Proceedings of the National Academy of Sciences of the USA   105 ( 38 )   14359 - 14364   2008.9

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:NATL ACAD SCIENCES  

    Bacterial flagella contain membrane-embedded stators, Mot complexes, that harness the energy of either transmembrane proton or sodium ion gradients to power motility. Use of sodium ion gradients is associated with elevated pH and sodium concentrations. The Mot complexes studied to date contain channels that use either protons or sodium ions, with some bacteria having only one type and others having two distinct Mot types with different ion-coupling. Here, alkaliphilic Bacillus clausii KSM-K16 was shown to be motile in a pH range from 7 to 11 although its genome encodes only one Mot (BCI-MotAB). Assays of swimming as a function of pH, sodium concentration, and ion-selective motility inhibitors showed that BCI-MotAB couples motility to sodium at the high end of its pH range but uses protons at lower pH. This pattern was confirmed in swimming assays of a statorless Bacillus subtilis mutant expressing either BCl-MotAB or one of the two B. subtilis stators, sodium-coupled Bs-MotPS or proton-coupled Bs-MotAB. Pairs of mutations in BCI-MotB were identified that converted the naturally bifunctional BCI-MotAB to stators that preferentially use either protons or sodium ions across the full pH range. We then identified trios of mutations that added a capacity for dual-ion coupling on the distinct B. subtilis Bs-MotAB and Bs-MotPS motors. Determinants that alter the specificity of bifunctional and single-coupled flagellar stators add to insights from studies of other ion-translocating transporters that use both protons and sodium ions.

    DOI: 10.1073/pnas.0802106105

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  • Na+ and flagella-dependent swimming of alkaliphilic Bacillus pseudofirmus OF4: a basis for poor motility at low pH and enhancement in viscous media in an "up-motile" variant Reviewed

    Shun Fujinami, Naoya Terahara, Sunmi Lee, Masahiro Ito

    Archives of Microbiology   187 ( 3 )   239 - 247   2007.3

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:SPRINGER  

    Flagella-based motility of extremely alkaliphilic Bacillus species is completely dependent upon Na+. Little motility is observed at pH values < similar to 8.0. Here we examine the number of flagella/cell as a function of growth pH in the facultative alkaliphile Bacillus pseudofirmus OF4 and a derivative selected for increased motility on soft agar plates. Flagella were produced by both strains during growth in a pH range from 7.5 to 10.3. The number of flagella/cell and flagellin levels of cells were not strongly dependent on growth pH over this range in either strain although both of these parameters were higher in the up-motile strain. Assays of the swimming speed indicated no motility at pH < 8 with 10 mM Na+, but significant motility at pH 7 at much higher Na+ concentrations. At pH 8-10, the swimming speed increased with the increase of Na+ concentration up to 230 mM, with fastest swimming at pH 10. Motility of the up-motile strain was greatly increased relative to wild-type on soft agar at alkaline pH but not in liquid except when polyvinylpyrrolidone was added to increase viscosity. The up-motile phenotype, with increased flagella/cell may support bundle formation that particularly enhances motility under a subset of conditions with specific challenges.

    DOI: 10.1007/s00203-006-0192-7

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  • An intergenic stem-loop mutation in the Bacillus subtilis ccpA-motPS operon increases motPS transcription and the MotPS contribution to motility Reviewed

    Naoya Terahara, Makoto Fujisawa, Benjamin Powers, Tina M Henkin, Terry Ann Krulwich, Masahiro Ito

    Journal of Bacteriology   188 ( 7 )   2701 - 2705   2006.4

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    A stem-loop mutation between cepA and motP in the Bacillus subtilis ccpA-motPS operon increased motPS transcription and membrane-associated MotPS levels, motility, and number of flagella/cell when MotPS is the sole stator and the MotPS contribution to motility at high pH, Na+, and viscosity when MotAB is also present.

    DOI: 10.1128/JB.188.7.2701-2705.2006

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  • Properties of motility in Bacillus subtilis powered by the H+-coupled MotAB flagellar stator, Na+-coupled MotPS or hybrid stators MotAS or MotPB Reviewed

    Masahiro Ito, Naoya Terahara, Shun Fujinami, Terry Ann Krulwich

    Journal of Molecular Biology   352 ( 2 )   396 - 408   2005.9

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    Bacillus subtilis has a single set of flagellar rotor proteins that interact with two distinct stator-force generators, the H+-coupled MotAB complex and the Na+-coupled MotPS complex, that energize rotation. Here, motility on soft agar plates and in liquid was assayed in wild-type B. subtilis and strains expressing only one stator, either MotAB, MotPS or hybrid MotAS or MotPB. The strains expressing MotAB or MotAS had an average of 11 flagella/cell while those expressing MotPS or MotPB had an average of seven flagella/cell, and a Mot-less double mutant had three to four flagella/cell. MotAB had a more dominant role in motility than MotPS under most conditions, but MotPS supported comparable motility to MotAB on malate-containing soft agar plating media at elevated pH and Na+. MotAB supported much faster swimming speeds in liquid than MotPS, MotAS or MotPB under all conditions, but a contribution of MotPS to wild-type swimming was discernible from differences in swimming speeds of wild-type and MotAB at elevated viscosity, pH and Na+. Swimming supported by MotPS and MotAS was stimulated by Na+ and elevated pH whereas the converse was true of MotAB and MotPB. This suggests that MotAS is Na+-coupled and MotPB is H+-coupled and that MotB and MotS are major determinants of ion-coupling. However, the swimming speed supported by MotPB, as well as MotPS and MotAS, was inhibited severely at Na+ concentrations above 300 mM whereas MotAB-dependent swimming was not. The presence of either the MotP or MotS component in the stator also conferred sensitivity to inhibition by an amiloride analogue. These observations suggest that MotP contributes to Na+-coupling and inhibition by Na+ channel inhibitors. Similarly, a role for MotA in H+-dependent stator properties is indicated by the larger effects of pH on the Na+-response of MotAS versus MotPS. Finally, optimal function at elevated viscosity was found only in MotPS and MotPB and is therefore conferred by MotP. (c) 2005 Elsevier Ltd. All rights reserved.

    DOI: 10.1016/j.jmb.2005.07.030

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Books

  • Extremophiles Handbook

    Masahiro Ito, Shun Fujinami, Naoya Terahara( Role: ContributorBioenergetics: Cell Motility and Chemotaxis of Extreme Alkaliphiles)

    Springer Nature  2011 

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MISC

  • FlhAcの高速原子間力顕微鏡画像の解析

    大沢陸輝, 寺原直矢, 古寺哲幸, 今田勝巳, 南野徹, 北尾彰朗

    分子シミュレーション討論会講演要旨集   36th   2022

  • Ion selectivity in the periplasmic domain of the stator complex

    寺原直矢, 寺原直矢, 古寺哲幸, 安藤敏夫, 難波啓一, 難波啓一, 南野徹

    日本生体エネルギー研究会討論会講演要旨集   45th   2019

  • A Novel Hybrid Nano-machine Driven by Potassium and Sodium Ions

    寺原直矢, 佐野元彦, 伊藤政博

    生物物理   54 ( 1 )   022-023 (J-STAGE) - 23   2014

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    Language:Japanese   Publisher:The Biophysical Society of Japan General Incorporated Association  

    DOI: 10.2142/biophys.54.022

    J-GLOBAL

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  • 第3のイオンで駆動するハイブリッド型細菌べん毛モーターの発見

    寺原直矢, 佐野元彦, 伊藤政博

    バイオサイエンスとインダストリー   71 ( 4 )   346 - 348   2013.7

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  • 私達の研究(82)細菌のべん毛モーターの新展開~自然界のハイブリッドモーター~

    寺原直矢, 伊藤政博

    化学療法の領域   26 ( 1 )   90 - 98   2009.12

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    J-GLOBAL

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  • 環境に応じて2種類のエネルギーを使い分ける ハイブリッド型生物モーター べん毛モーターの固定子から考える細菌の環境適応と進化

    伊藤政博, 寺原直矢

    化学と生物   47 ( 7 )   473 - 479   2009.7

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    Language:Japanese   Publisher:Japan Society for Bioscience, Biotechnology, and Agrochemistry  

    DOI: 10.1271/kagakutoseibutsu.47.473

    CiNii Books

    J-GLOBAL

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  • 枯草菌のべん毛モーターに学ぶハイブリッドモーター

    寺原直矢, 伊藤政博

    バイオサイエンスとインダストリー   66 ( 7 )   366 - 368   2008.7

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  • A Bacillus flagellar motor switches from proton to sodium gradients for powering motility at alkaline pH

    Naoya Terahara, Terry Ann Krulwich, Masahiro Ito

    Biochimica et Biophysica Acta-Bioenergetics   1777   S31 - S32   2008.7

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    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:ELSEVIER SCIENCE BV  

    DOI: 10.1016/j.bbabio.2008.05.128

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Presentations

  • べん毛モーター固定子複合体のペリプラズミックドメインにおけるイオン選択性

    寺原直矢, 古寺哲幸, 安藤敏夫, 難波啓一, 南野徹

    日本生体エネルギー研究会第45回討論会  2019.12 

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  • 枯草菌べん毛モーターから見えてきた回転ステップと共役イオン流の関係

    寺原直矢

    第7回THE ToKYo Molecular Motor Show  2019.10 

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  • Na+駆動型枯草菌べん毛モーターのステップ解析

    寺原直矢, 楊未来, 宗行英郎, 難波啓一, 南野徹

    日本生物物理学会第57回年会  2019.9 

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  • 枯草菌べん毛モーターの回転ステップの解析

    寺原直矢, 楊未来, 宗行英郎, 難波啓一, 南野徹

    第9回分子モーター討論会  2019.6 

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  • 固定子複合体のペリプラズミックドメインにおけるイオン選択性

    寺原直矢, 古寺哲幸, 安藤敏夫, 難波啓一, 南野徹

    2018年度べん毛研究交流会  2019.3 

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  • べん毛モーター固定子のイオン透過性を向上させる回転子FliGの変異

    寺原直矢, 難波啓一, 南野徹

    2019年生体運動研究合同班会議  2019.1 

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  • べん毛モーターの回転速度が速くなった変異株の単離と回転計測によるモーター特性の解析

    寺原直矢, 難波啓一, 南野徹

    日本生体エネルギー研究会第44回討論会  2018.12 

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  • べん毛モーター固定子のイオンチャネル活性のフィードバック制御

    寺原直矢, 難波啓一, 南野徹

    日本生物物理学会第56回年会  2018.9 

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  • 枯草菌べん毛モーターの回転ステップの解析

    寺原直矢, 楊未来, 難波啓一, 南野徹

    2017年度べん毛研究交流会  2018.3 

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  • Direct visualization of ring formation of a flagellar type III export gate protein FlhA by high-speed AFM

    Naoya Terahara, Yumi Inoue, Noriyuki Kodera, Yusuke V. Morimoto, Takayuki Uchihashi, Katsumi Imada, Toshio Ando, Keiichi Namba, Tohru Minamino

    International Symposium on Atomic Force Microscopy at Solid-Liquid Interfaces  2017.11 

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  • HS-AFMによるべん毛モーター固定子MotPSのリアルタイムイメージング

    寺原直矢, 古寺哲幸, 内橋貴之, 安藤敏夫, 難波啓一, 南野徹

    日本生物物理学会第55回年会  2017.9 

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  • Na+-induced structural transition for stator assembly of Bacillus flagellar stator MotPS

    Naoya Terahara, Noriyuki Kodera, Takayuki Uchihashi, Toshio Ando, Keiichi Namba, Tohru Minamino

    International symposium on harmonized supramolecular motility machinery and its diversity  2017.9 

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  • 高速AFMイメージングにより明らかになったべん毛モーター固定子複合体MotPSのダイナミクス

    寺原直矢, 古寺哲幸, 内橋貴之, 安藤敏夫, 難波啓一, 南野徹

    日本生体エネルギー研究会第42回討論会  2016.12 

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  • 高速AFMによるべん毛モーター固定子複合体MotPSの動的構造解析

    寺原直矢, 古寺哲幸, 内橋貴之, 安藤敏夫, 難波啓一, 南野徹

    新学術領域研究「運動マシナリー」平成28年度全体会議  2016.6 

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  • べん毛モーター固定子複合体の構造ダイナミクスを高速AFMで見る

    寺原直矢, 古寺哲幸, 内橋貴之, 安藤敏夫, 難波啓一, 南野徹

    2015年度べん毛研究交流会  2016.3 

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  • 細菌べん毛モーターを回す膜タンパク質複合体の機能と構造を探る

    寺原直矢

    第129回生命機能研究科研究交流会  2016.1 

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  • 高速AFMによるべん毛モーター固定子複合体MotPSの動的構造解析

    寺原直矢, 古寺哲幸, 内橋貴之, 安藤敏夫, 難波啓一, 南野徹

    2016年生体運動研究合同班会議  2016.1 

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  • 高分解能クライオ電子顕微鏡法によるべん毛モーター固定子MotPS複合体の構造解析

    寺原直矢, 加藤貴之, 南野徹, 難波啓一

    日本生物物理学会第53回年会  2015.9 

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  • クライオEMによるべん毛モーター固定子MotPS複合体の高分解構造解析

    寺原直矢, 加藤貴之, 南野徹, 難波啓一

    新学術領域研究「運動マシナリー」平成27年度全体会議  2015.6 

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  • クライオ電子顕微鏡法によるべん毛モーター固定子MotPS複合体の高分解構造解析

    寺原直矢, 加藤貴之, 南野徹, 難波啓一

    第12回21世紀大腸菌研究会  2015.6 

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  • クライオ電子顕微鏡法によるNa+駆動型べん毛モーター固定子MotPS複合体の高分解能構造解析

    寺原直矢, 加藤貴之, 南野徹, 難波啓一

    分子研研究会 膜タンパク質内部のプロトン透過を考える  2015.4 

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  • 固定子複合体MotPSのクライオ電子顕微鏡による構造解析

    寺原直矢, 加藤貴之, 南野徹, 難波啓一

    2014年度べん毛研究交流会  2015.3 

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  • Na+駆動型べん毛モーター固定子MotPS複合体の高分解能構造解析

    寺原直矢, 加藤貴之, 南野徹, 難波啓一

    新学術領域研究「運動マシナリー」平成26年度全体会議  2014.6 

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  • 枯草菌べん毛モーターの性能は異なる2種類の固定子によって調節される

    寺原直矢, 野口有希奈, 中村修一, 上池伸徳, 南野徹, 伊藤政博, 難波啓一

    第11回21世紀大腸菌研究会  2014.6 

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  • べん毛固定子MotABとMotPSによるモーターの環境適応

    寺原直矢, 野口有希奈, 中村修一, 上池伸徳, 南野徹, 伊藤政博, 難波啓一

    2013年度べん毛研究交流会  2014.3 

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  • Bacillus属細菌のべん毛モーター固定子の進化と環境適応戦略

    寺原直矢

    大阪大学公開シンポジウム バクテリアべん毛研究の最前線  2013.12 

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  • グラム陽性−陰性細菌間におけるべん毛モーター固定子の異種発現とトルク特性の解析

    寺原直矢, 上池伸徳, 難波啓一, 南野徹

    日本生体エネルギー研究会第39回討論会  2013.12 

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  • 異なる2種類の固定子を持つ枯草菌べん毛モーターのトルク特性

    寺原直矢, 野口有希奈, 中村修一, 上池伸徳, 南野徹, 伊藤政博, 難波啓一

    日本生物物理学会第51回年会  2013.10 

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  • 2種類の固定子を持つ枯草菌べん毛モーターの1分子回転計測

    寺原直矢, 野口有希奈, 中村修一, 上池伸徳, 南野徹, 伊藤政博, 難波啓一

    新学術領域研究「運動マシナリー」平成25年度全体会議  2013.6 

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  • 異なる2種類の固定子を持つ枯草菌べん毛モーターの1分子回転計測

    寺原直矢, 野口有希奈, 中村修一, 上池伸徳, 南野徹, 伊藤政博, 難波啓一

    第10回21世紀大腸菌研究会  2013.6 

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  • ハイブリッドエンジンを搭載した枯草菌べん毛モーター

    寺原直矢, 野口有希奈, 中村修一, 上池伸徳, 南野徹, 伊藤政博, 難波啓一

    2012年度べん毛研究交流会  2013.3 

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  • 枯草菌—サルモネラ菌間におけるべん毛モーター固定子の異種発現とトルク特性の解析

    寺原直矢, 上池伸徳, 難波啓一, 南野徹

    2013年生体運動研究合同班会  2013.1 

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  • 異なる2種類の固定子で駆動する枯草菌べん毛モーターのトルク特性の解析

    寺原直矢, 野口有希奈, 中村修一, 上池伸徳, 南野徹, 伊藤政博, 難波啓一

    日本生体エネルギー研究会第38回討論会  2012.12 

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  • 異なる2種類の固定子で駆動する枯草菌べん毛モーター

    寺原直矢, 野口有希奈, 中村修一, 上池伸徳, 伊藤政博, 難波啓一

    日本分子生物学会第35回年会  2012.12 

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  • 異なる2種類の固定子で駆動する枯草菌べん毛モーターのトルク特性

    寺原直矢, 野口有希奈, 中村修一, 上池伸徳, 伊藤政博, 難波啓一

    日本生物物理学会第50回年会  2012.9 

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  • 好アルカリ性Bacillus属細菌の分子系統学的解析から見つかった“K+で駆動する”新奇べん毛モーター

    寺原直矢, 佐野元彦, 伊藤政博, 難波啓一

    第9回21世紀大腸菌研究会  2012.6 

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  • 外環境pHによりイオン選択性が変化するべん毛モーター固定子のX線結晶構造解析

    寺原直矢, 今田勝巳, 南野徹, 難波啓一

    新学術領域研究「構造細胞生物学」平成24年度全体会議  2012.6 

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  • 好アルカリ性Bacillus属細菌のべん毛モーター固定子の分子系統学的解析と新規べん毛モーターの発見

    寺原直矢, 佐野元彦, 難波啓一, 伊藤政博

    日本生体エネルギー研究会第37回討論会  2011.12 

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  • 好アルカリ性Bacillus属細菌のべん毛モーター固定子の分子系統学的解析による新規べん毛モーターの発見

    寺原直矢, 佐野元彦, 難波啓一, 伊藤政博

    日本分子生物学会第34回年会  2011.12 

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  • 好アルカリ性Bacillus属細菌が持つべん毛モーター固定子の分子系統解析

    寺原直矢, 野口有希奈, 中野悠子, 難波啓一, 伊藤政博

    日本生物物理学会第48回年会  2010.9 

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  • 好アルカリ性Bacillus属細菌のべん毛モーター固定子の分子系統解析

    寺原直矢, 野口有希奈, 中野悠子, 伊藤政博

    日本細菌学会第83回年会  2010.3 

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  • The flagellar motor of Bacillus clausii changes the ion motive force for the rotational energy in response to external pH

    Naoya Terahara, Terry A. Krulwich, Masahiro Ito

    21st COE Programme 7th International Symposium on Bioscience and Nanotechnology  2009.11 

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  • 好アルカリ性Bacillus属細菌の新規べん毛モーター固定子の探索と分子系統解析

    寺原直矢, 野口有希奈, 中野悠子, 伊藤政博

    極限環境微生物学会第10回年会  2009.10 

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  • 好アルカリ性Bacillus属細菌が持つMotABのイオン選択性の解析

    寺原直矢, Terry A. Krulwich, 伊藤政博

    2008年度べん毛研究交流会  2009.3 

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  • Bacillus属細菌で見つかった環境pH応答型べん毛モーター固定子のイオン選択性の解析

    寺原直矢, Terry A. Krulwich, 伊藤政博

    第31回日本分子生物学会年会  2008.12 

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  • A first report of a new flagellar stator that can use both proton and sodium gradients for bacterial motility

    Naoya Terahara, Terry A. Krulwich, Masahiro Ito

    21st COE Programme 6th International Symposium on Bioscience and Nanotechnology  2008.11 

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  • 2種類の共役イオンを利用するべん毛モーター固定子の発見とイオン選択性に重要なアミノ酸残基の同定

    寺原直矢, Terry A. Krulwich, 伊藤政博

    日本生体エネルギー研究会第34回討論会  2008.11 

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  • 好アルカリ性細菌Bacillus clausiiのMotABから見えてきたべん毛モーター固定子のイオン選択性に重要なアミノ酸残基

    寺原直矢, Terry A. Krulwich, 伊藤政博

    極限環境微生物学会第9回年会  2008.11 

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  • 好アルカリ性細菌Bacillus clausiiのべん毛モーター固定子MotABは共役イオンとして2種類のイオンを利用することができる

    寺原直矢, 伊藤政博

    第3回トランスポーター研究会年会  2008.6 

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  • Torque-speed relationship of the hybrid flagellar motor of Bacillus subtilis

    Naoya Terahara, Masahiro Ito

    21st COE Programme 5th International Symposium on Bioscience and Nanotechnology  2007.12 

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  • 枯草菌べん毛モーターは2種類のエネルギーを利用できるハイブリッドモーター

    寺原直矢, 伊藤政博

    日本農芸化学会関東支部2007年度大会  2007.11 

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  • 好アルカリ性細菌のべん毛モーター固定子MotPSのホモログを持つ枯草菌でのMotPSの生理的な役割

    寺原直矢, 伊藤政博

    2006年度べん毛研究交流会  2007.3 

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  • Molecular Basis and Swimming Properties of a MotPS-Dependent Motility Mutant of Bacillus subtilis

    Naoya Terahara, Masahiro Ito

    21st COE Programme 4th International Symposium on Bioscience and Nanotechnology  2006.11 

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  • The functional roles of Na+-dependent MotPS-type flagellar motor of Bacillus subtilis that is a homologue of the Stator-Force Generator for Alkaliphile Motility

    Naoya Terahara, Masahiro Ito

    Extremophiles 2006  2006.9 

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  • 枯草菌のべん毛モーターは生物が獲得した天然のハイブリッドモーターである

    寺原直矢, 伊藤政博

    2006年度グラム陽性細菌ゲノム生物学研究会  2006.9 

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  • 枯草菌における第2のべん毛モーター固定子MotPSの発現とその機能解析

    寺原直矢, 藤澤誠, 伊藤政博

    第28回日本分子生物学会年会  2005.12 

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  • The Na+-dependent MotPS of Bacillus subtilis that is a homologue of the Stator Force Generator for Alkaliphile Motility Plays a Physiological Role in its Neutralophile Setting

    Naoya Terahara, Masahiro Ito

    International Symposium on Extremophiles and Their Applications  2005.11 

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  • The functional analysis of the bacterial flagellar nanomachine that consist of two distinct stator force generators in Bacillus subtilis

    Naoya Terahara, Masahiro Ito

    21st COE Programme 3rd International Symposium on Bioscience and Nanotechnology  2005.11 

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  • 好アルカリ性細菌のべん毛モーター固定子MotPSのホモログをもつ枯草菌でのMotPSの生理的な役割の解明

    寺原直矢, Terry A. Krulwich, 伊藤政博

    極限環境微生物学会第6回年会  2005.11 

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  • 枯草菌中でのキメラモーター固定子の発現とそのイオン選択性の解析

    寺原直矢, 伊藤政博

    日本農芸化学会2005年度大会  2005.3 

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Awards

  • 10th Anniversary Best Cover Awards Third Place

    2021.4   Biomolecules   「Structural and functional comparison of Salmonella flagellar filaments composed of FljB and FliC」

    Tomoko Yamaguchi, Shoko Toma, Naoya Terahara, Tomoko Miyata, Masamichi Ashihara, Tohru Minamino, Keiichi Namba, Takayuki Kato

  • 第9回年会ポスター賞

    2008.11   極限環境微生物学会  

    寺原直矢

  • 第3回年会優秀演題賞

    2008.6   トランスポーター研究会  

    寺原直矢

  • 関東支部大会若手奨励賞(口頭発表部門)

    2007.11   日本農芸化学会  

    寺原直矢

  • 校友会学生研究奨励賞(大学院)

    2006.3   東洋大学  

    寺原直矢

  • 校友会学生研究奨励賞(学部)

    2005.3   東洋大学  

    寺原直矢

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Research Projects

  • べん毛モーターにおけるイオン流から回転力へのエネルギー変換メカニズムの解明

    Grant number:21K06073  2021.4 - 2024.3

    日本学術振興会  基盤(C)  基盤研究(C)  中央大学

    寺原 直矢

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    Grant amount: \4160000 ( Direct Cost: \3200000 、 Indirect Cost: \960000 )

    細菌べん毛モーターは、H+またはNa+の細胞内外の濃度差および膜電位によって決定される電気化学ポテンシャル差をトルクに変換する生体ナノマシンである。べん毛モーターは回転子と固定子から構成され、イオンチャネルとして機能する固定子内部に共役イオンが流れることで固定子と回転子が相互作用し、回転力を発生させる。1回転あたり26回のステップ状変位が観測されており、固定子と回転子の相互作用素過程がステップとして反映されていると考えられている。しかし、回転速度が非常に速いため精度の高い回転ステップの検出が難しく、さらに1つのモーターに対して固定子が10個前後組み込まれることから、イオンの流れと力の発生の関係性を見出すことが大変困難である。そこで、生理条件下でモーターに組み込まれる固定子数が1個と少なく、回転速度が遅い枯草菌べん毛モーターの回転ステップを解析することで、イオンの流れがどのように力に変換されているのか明らかにすることを目指した。
    べん毛モーターが生み出すトルクは、ビーズアッセイ法によって解析する。ビーズアッセイ法は、スライドガラス上に接着させた菌体の1本のべん毛フィラメントにポリスチレンビーズで標識し、べん毛の回転をビーズの回転軌道として計測する方法である。高速回転しているビーズの位相差像から重心位置を求め、ビーズの重心位置を示すXY座標とビーズの回転速度を求める。さらに、得られたXY座標を回転楕円補正することで回転半径を求める。これらの計測結果および測定時の溶液の粘度から発生トルクを算出する。今回、枯草菌のべん毛モーターの測定を可能とする系の構築に漕ぎ着けた。

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  • べん毛モーター固定子複合体の高分解能構造解析による回転メカニズムの解明

    2018.4 - 2021.3

    基盤(C) 

    寺原 直矢

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  • The elucidation of the molecular mechanisms of ion selectivity of hybrid bacterial flagellar motors

    Grant number:24117005  2013.4 - 2017.3

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)  Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)  Toyo University

    ITO MASAHIRO

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    Grant amount: \83720000 ( Direct Cost: \64400000 、 Indirect Cost: \19320000 )

    Many bacteria migrate through the environment using the flagellar apparatus which is a motion organelle. Until now, the flagellar motor was known to be driven by an ion motive force such as proton and sodium ion. In this study, we succeeded to isolate Paenibacillus sp. TCA20 with flagellar motors driven by divalent cations such as calcium ions and magnesium ions for the first time in the world. Besides this, we also characterized nonconventional cation-coupled flagellar motors derived from the alkaliphilic Bacillus. Differences in ion selective permeability between these flagellar motors and conventional motors were elucidated using molecular biological techniques. Based on the results of this study, it is expected to create artificial nanomachines and molecular switches that can selectively use driving energy.

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  • べん毛超分子モーターの運動エネルギー変換メカニズム

    2013.4 - 2017.3

    新学術領域「運動マシナリー」 

    本間 道夫

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  • ハイブリッド型バクテリアべん毛モーターの環境変化感知と回転力発生の分子基盤

    2014.4 - 2016.3

    若手(B) 

    寺原 直矢

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  • GFPラベルを用いた位置同定単粒子像解析法(GPS法)の開発

    2014.4 - 2016.3

    挑戦的萌芽 

    加藤 貴之

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  • 環境適応型ハイブリッドべん毛モーターのトルク特性と固定子の結晶構造解析

    2010.4 - 2013.3

    学振(PD) 

    寺原 直矢

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  • バチルス属細菌がもつ新奇なべん毛モーター固定子複合体の機能と構造の解明

    2009.4 - 2010.3

    基盤(B) 

    伊藤 政博

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  • 枯草菌のべん毛モーター固定子の細胞内局在性の解明とモータートルク特性の解析

    2007.4 - 2009.3

    学振(DC2) 

    寺原 直矢

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Media Coverage

  • クライオ電顕で生体分子の3D構造解明が加 Newspaper, magazine

    日経バイオテク  2019.2

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  • 大阪大学、細菌べん毛タンパク質輸送の交通整理のしくみを解明 Newspaper, magazine

    日経バイオテク  2018.5

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  • 阪大・金沢大・名大・九州工大、べん毛タンパク質輸送の交通整理の仕組みを解明-細菌感染症薬のスクリーニングへ応用 Newspaper, magazine

    日本経済新聞  2018.4

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  • 細菌のべん毛形成解明 Newspaper, magazine

    北國新聞  2018.4

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  • 外環境を感知してエネルギー源を切り替えるエコロジカルなナノモーター Internet

    Academist Journal  2018.4

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  • 阪大・金沢大・名大、細菌べん毛モーターがバイオセンサーとして働くしくみを解明 Newspaper, magazine

    日本経済新聞  2017.11

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  • 阪大、べん毛モーター固定子の働き解明−超微細マシン開発に道 Newspaper, magazine

    日刊工業新聞  2017.11

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  • F1級の回転、効率100%ナノマシンに…細菌べん毛モーター駆動タンパク質の構造解明 Newspaper, magazine

    産経WEST  2016.8

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  • べん毛モータータンパク質解明 Newspaper, magazine

    中日新聞  2016.8

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  • 第3のイオンで動くハイブリッドナノマシン Newspaper, magazine

    科学新聞  2013.1

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  • カリウムイオンで駆動 Newspaper, magazine

    日刊工業新聞  2012.10

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  • 細菌のべん毛動力源 環境で切り替え Newspaper, magazine

    読売新聞  2008.11

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