研究者詳細 - 小嶋　誠司

論文 - 小嶋　誠司

分割表示 222 件中 181 - 200 件目／全件表示 >>

Collaboration of FlhF and FlhG to regulate polar-flagella number and localization in Vibrio alginolyticus. 査読有り

Kusumoto A, Shinohara A, Terashima H, Kojima S, Yakushi T, Homma M.

Microbiology 154 巻頁： 1390-1399 2008年

Roles of charged residues in the C-terminal region of PomA, a stator component of the Na+-driven flagellar motor. 査読有り

Obara M, Yakushi T, Kojima S, Homma M.

Journal of Bacteriology 190 巻頁： 3565-3571 2008年

Systematic Cys mutagenesis of FlgI, the flagellar P-ring component of Escherichia coli. 査読有り

Hizukuri Y, Kojima S, Yakushi T, Kawagishi I, Homma M.

Microbiology 154 巻頁： 810-817 2008年

FLAGELLAR MOTILITY IN BACTERIA: STRUCTURE AND FUNCTION OF FLAGELLAR MOTOR 査読有り

Terashima, H; Kojima, S; Homma, M

INTERNATIONAL REVIEW OF CELL AND MOLECULAR BIOLOGY, VOL 270 270 巻頁： 39 - 85 2008年

Single evaluation of C. Elegans inside environmental scanning electron microscope 査読有り

Masahiro Nakajima, Mohd Ridzuan Ahmad, Seiji Kojima, Michio Homma, Toshio Fukuda

2008 International Symposium on Micro-NanoMechatronics and Human Science, MHS 2008 頁： 83 - 88 2008年

記述言語：英語掲載種別：研究論文（国際会議プロシーディングス）

This paper presents the single evaluation of Caenorhabditìs Elegans (C. Elegans) by the nanorobotic manipulation system inside an Environmental-Scanning Electron Microscope (E-SEM). C. Elegans has complex outer and inner structures constructed by approximately one thousand cells. Their fine structures were observed by E-SEM directly
without any drying or dyeing processes. For example, the lateral alae are the surface mark of seam cell body. The observation environments are controlled under different E-SEM chamber pressures for clear observation of C. Elegans. The local stiffness evaluation method of C. Elegans was proposed by buckling nanoprobe. The Silicon nanoprobe was fabricated by Focus Ion Beam (FIB) etching at the tip of Atomic Force Microscope (AFM) cantilever. The measurement position can arbitrarily be controlled by the nanorobotic manipulator inside the E-SEM. The local stiffness on or around the lateral alae evaluated from the experimental results. This local stiffness measurement technique can readily be applied to reveal unknown biological local stiffness, cell health conditions and novel cell diagnosis. © 2008 IEEE.

DOI： 10.1109/MHS.2008.4752427

Scopus

Na+駆動型べん毛モーターにおける遊泳速度の圧力応答(Pressure-velocity relationship of sodium-driven flagellar motor of Vibrio alginolyticus)

下田義樹, 西山雅祥, 小嶋誠司, 本間道夫, 木村佳文, 寺嶋正秀

生物物理 47 巻 ( Suppl.1 ) 頁： S247 - S247 2007年11月

Visualization of functional rotor proteins of the bacterial flagellar motor in the cell membrane 査読有り

Fukuoka, H; Sowa, Y; Kojima, S; Ishijima, A; Homma, M

JOURNAL OF MOLECULAR BIOLOGY 367 巻 ( 3 ) 頁： 692 - 701 2007年3月

Visualization of functional rotor proteins of the bacterial flagellar motor in the cell membrane 査読有り

Fukuoka H, Sowa Y, Kojima S, Ishijima A and Homma M

Journal of Molecular Biology 367 巻 ( 3 ) 頁： 692-701 2007年3月

Crystallization and preliminary X-ray analysis of MotY, a stator component of the Vibrio alginolyticus polar flagellar motor 査読有り

Shinohara A, Sakuma M, Yakushi T, Kojima S, Namba K Homma M and Imada K

Acta Crystallograph Sect F 63 巻頁： 89-92 2007年2月

Crystallization and preliminary X-ray analysis of MotY, a stator component of the Vibrio alginolyticus polar flagellar motor 査読有り

Shinohara, A; Sakuma, M; Yakushi, T; Kojima, S; Namba, K; Homma, M; Imada, K

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS 63 巻 ( Pt 2 ) 頁： 89 - 92 2007年2月

The Vibrio motor proteins, MotX and MotY, are associated with the basal body of Na-driven flagella and required for stator formation 査読有り

Terashima H, Fukuoka H, Yakushi T, Kojima S and Homma M

Molecular Microbiology 62 巻 ( 4 ) 頁： 1170-1180 2006年11月

The Vibrio motor proteins, MotX and MotY, are associated with the basal body of Na+-driven flagella and required for stator formation 査読有り

Terashima, H; Fukuoka, H; Yakushi, T; Kojima, S; Homma, M

MOLECULAR MICROBIOLOGY 62 巻 ( 4 ) 頁： 1170 - 1180 2006年11月

[Topology of bacterial cells focused on polar-localized proteins]. 査読有り

Kusumoto A, Kojima S, Homma M

Nihon saikingaku zasshi. Japanese journal of bacteriology 61 巻 ( 3 ) 頁： 325 - 337 2006年8月

Arrangement of core membrane segments in the MotA/MotB proton-channel complex of Escherichia coli 査読有り

TF Braun, LQ Al-Mawsawi, S Kojima, DF Blair

BIOCHEMISTRY 43 巻 ( 1 ) 頁： 35 - 45 2004年1月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：AMER CHEMICAL SOC

The stator of the bacterial flagellar motor is formed from the membrane proteins MotA and MotB, which associate in complexes with stoichiometry MotA(4)MotB(2) (Kojima, S., and Blair, D. F., preceding paper in this issue). The MotA/MotB complexes conduct ions across the membrane, and couple ion flow to flagellar rotation by a mechanism that appears to involve conformational changes within the complex. MotA has four membrane-crossing segments, termed A1-A4, and MotB has one, termed B. We are studying the organization of the 18 membrane segments in the MotA(4)MotB(2) complex by using targeted disulfide cross-linking. A previous cross-linking study showed that the two B segments in the complex (one from each MotB subunit) are arranged as a symmetrical dimer of alpha-helices. Here, we extend the cross-linking study to segments A3 and A4. Single Cys residues were introduced by mutation in several consecutive positions in segments A3 and A4, and double mutants were made by pairwise combination of subsets of the Cys replacements in segments A3, A4, and B. Disulfide cross-linking of the single- and double-Cys proteins was studied in whole cells, in membranes, and in detergent solution. Several combinations of Cys residues in segments A3 and B gave a high yield of disulfide-linked MotA/MotB heterodimer upon oxidation with iodine. Positions of efficient cross-linking identify a helix face on segment A3 that is in proximity to segment(s) B. Some combinations of Cys residues in segments A4 and B also gave a significant yield of disulfide-linked heterodimer, indicating that segment A4 is also near segment(s) B. Certain combinations of Cys residues in segments A3 and A4 cross-linked to form MotA tetramers in high yield upon oxidation. The high-yield positions identify faces on A3 and A4 that are at an interface between MotA subunits. Taken together with mutational studies and patterns of amino acid conservation, the cross-linking results delineate the overall arrangement of 10 membrane segments in the MotA/MotB complex, and identify helix faces likely to line the proton channels.

DOI： 10.1021/bi035406d

Web of Science

PubMed

Solubilization and purification of the MotA/MotB complex of Escherichia coli 査読有り

S Kojima, DF Blair

BIOCHEMISTRY 43 巻 ( 1 ) 頁： 26 - 34 2004年1月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：AMER CHEMICAL SOC

Bacterial flagella are driven at their base by a rotary motor fueled by the membrane gradient of protons or sodium ions. The stator of the flagellar motor is formed from the membrane proteins MotA and MotB, which function together to conduct ions across the membrane and couple ion flow to rotation. An invariant aspartate residue in MotB (Asp32 in the protein of E. coli) is essential for rotation and appears to have a direct role in proton conduction. A recent study showed that changes at Asp32 in MotB cause a conformational change in the complex, as evidenced by altered patterns of protease susceptibility of MotA [Kojima, S., and Blair, D. F. (2001) Biochemistry 40 (43), 13041-13050]. It was proposed that protonation/deprotonation of Asp32 might regulate a conformational change in the stator that acts as the powerstroke to drive rotation of the rotor. Biochemical studies of the MotA/MotB complex have been hampered by the absence of a suitable assay for its integrity in detergent solution. Here, we have studied the behavior of the MotA/MotB complex in a variety of detergents, making use of the protease-susceptibility assay to monitor its integrity. Among about 25 detergents tested, a few were found to solubilize the proteins effectively while preserving certain conformational properties characteristic of an intact complex. The detergent dodecylphosphocholine, or DPC, proved especially effective. MotA/MotB complexes purified in DPC migrate with an apparent size of similar to300 kDa in gel-filtration columns, and retain the Asp32-modulated conformational differences seen in membranes. S-35-radiolabeling showed that MotA and MotB are present in a 2:1 ratio in the complex. Purified MotA/MotB complexes should enable in vitro study of the proton-induced conformational change and other aspects of stator function.

DOI： 10.1021/bi0354051

Web of Science

PubMed

Solubilization and purification of the MotA/MotB complex of Escherichia coli 査読有り

Kojima, S., and Blair, D.F.

Biochemistry 43 巻頁： 26-35 2004年

The bacterial flagellar motor: Structure and function of a complex molecular machine. 招待有り

Kojima, S., & Blair, D.F.

International Review of Cytology 233 巻頁： 93-134 2004年

Arrangement of core membrane segments in the MotA/MotB proton-channel complex of Escherichia coli 査読有り

Braun, T.F., Al-Mawsawi, L.Q., Kojima, S., & Blair, D.F.

Biochemistry 43 巻頁： 35-45 2004年

The bacterial flagellar motor: Structure and function of a complex molecular machine 査読有り

S Kojima, DF Blair

INTERNATIONAL REVIEW OF CYTOLOGY - A SURVEY OF CELL BIOLOGY, VOL. 233 233 巻頁： 93 - 134 2004年

Rotary motors (bacterial). 招待有り

Kojima, S., & Blair, D.F.

McGraw-Hill Yearbook of Science & Technology 2003 頁： 363-366 2003年

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