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Volumn 97, Issue 11, 2009, Pages 2930-2938

Motor-substrate interactions in Mycoplasma motility explains non-Arrhenius temperature dependence

Author keywords

[No Author keywords available]

Indexed keywords

KINESIN; MYOSIN;

EID: 72549093544     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.09.020     Document Type: Article
Times cited : (27)

References (36)
  • 1
    • 0031770391 scopus 로고    scopus 로고
    • Molecular biology and pathogenicity of mycoplasmas
    • Razin, S., D. Yogev, and Y. Naot. 1998. Molecular biology and pathogenicity of mycoplasmas. Microbiol. Mol. Biol. Rev. 62:1094-1156.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1094-1156
    • Razin, S.1    Yogev, D.2    Naot, Y.3
  • 2
    • 14244254325 scopus 로고    scopus 로고
    • Gliding motility of mycoplasmas: The mechanism cannot be explained by current biology
    • A. Blanchard and G. Browning, editors. Horizon Bioscience, Wymondham, UK
    • Miyata, M. 2005. Gliding motility of mycoplasmas: the mechanism cannot be explained by current biology. In Mycoplasmas: Molecular Biology, Pathogenicity and Strategies for Control. A. Blanchard and G. Browning, editors. Horizon Bioscience, Wymondham, UK. 137-163.
    • (2005) Mycoplasmas: Molecular Biology, Pathogenicity and Strategies for Control , pp. 137-163
    • Miyata, M.1
  • 5
    • 0035113906 scopus 로고    scopus 로고
    • Visualization of the attachment organelle and cytadherence proteins of Mycoplasma pneumoniae by immunofluorescence microscopy
    • DOI 10.1128/JB.183.5.1621-1630.2001
    • Seto, S., G. Layh-Schmitt, T. Kenri, and M. Miyata. 2001. Visualization of the attachment organelle and cytadherence proteins of Mycoplasma pneumoniae by immunofluorescence microscopy. J. Bacteriol. 183: 1621-1630. (Pubitemid 32172305)
    • (2001) Journal of Bacteriology , vol.183 , Issue.5 , pp. 1621-1630
    • Seto, S.1    Layh-Schmitt, G.2    Kenri, T.3    Miyata, M.4
  • 6
    • 33645306591 scopus 로고    scopus 로고
    • Three-dimensional structure of Mycoplasma pneumoniae's attachment organelle and a model for its role in gliding motility
    • Henderson, G. P., and G. J. Jensen. 2006. Three-dimensional structure of Mycoplasma pneumoniae's attachment organelle and a model for its role in gliding motility. Mol. Microbiol. 60:376-385.
    • (2006) Mol. Microbiol. , vol.60 , pp. 376-385
    • Henderson, G.P.1    Jensen, G.J.2
  • 7
    • 0037044472 scopus 로고    scopus 로고
    • Movement on the cell surface of the gliding bacterium, Mycoplasma mobile, is limited to its head-like structure
    • Miyata, M., and A. Uenoyama. 2002. Movement on the cell surface of the gliding bacterium, Mycoplasma mobile, is limited to its head-like structure. FEMS Microbiol. Lett. 215:285-289.
    • (2002) FEMS Microbiol. Lett. , vol.215 , pp. 285-289
    • Miyata, M.1    Uenoyama, A.2
  • 8
    • 4944232464 scopus 로고    scopus 로고
    • Use of fluorescent-protein tagging to determine the subcellular localization of Mycoplasma pneumoniae proteins encoded by the cytadherence regulatory locus
    • DOI 10.1128/JB.186.20.6944-6955.2004
    • Kenri, T., S. Seto, A. Horino, Y. Sasaki, T. Sasaki, et al. 2004. Use of fluorescent-protein tagging to determine the subcellular localization of Mycoplasma pneumoniae proteins encoded by the cytadherence regulatory locus. J. Bacteriol. 186:6944-6955. (Pubitemid 39332134)
    • (2004) Journal of Bacteriology , vol.186 , Issue.20 , pp. 6944-6955
    • Kenri, T.1    Seto, S.2    Horino, A.3    Sasaki, Y.4    Sasaki, T.5    Miyata, M.6
  • 9
    • 10544255079 scopus 로고    scopus 로고
    • Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae
    • DOI 10.1093/nar/24.22.4420
    • Himmelreich, R., H. Hilbert, H. Plagens, E. Pirkl, B. C. Li, et al. 1996. Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae. Nucleic Acids Res. 24:4420-4449. (Pubitemid 26388629)
    • (1996) Nucleic Acids Research , vol.24 , Issue.22 , pp. 4420-4449
    • Himmelreich, R.1    Hubert, H.2    Plagens, H.3    Pirkl, E.4    Li, B.-C.5    Herrmann, R.6
  • 13
    • 0023176566 scopus 로고
    • Gliding motility of Mycoplasma sp. nov. strain 163K
    • Rosengarten, R., and H. Kirchhoff. 1987. Gliding motility of Mycoplasma strain 163K. J. Bacteriol. 169:1891-1898. (Pubitemid 17081741)
    • (1987) Journal of Bacteriology , vol.169 , Issue.5 , pp. 1891-1898
    • Rosengarten, R.1    Kirchhoff, H.2
  • 14
    • 3042515670 scopus 로고    scopus 로고
    • Energetics of gliding motility in Mycoplasma mobile
    • Jaffe, J. D., M. Miyata, and H. C. Berg. 2004. Energetics of gliding motility in Mycoplasma mobile. J. Bacteriol. 186:4254-4261.
    • (2004) J. Bacteriol. , vol.186 , pp. 4254-4261
    • Jaffe, J.D.1    Miyata, M.2    Berg, H.C.3
  • 15
    • 24644452446 scopus 로고    scopus 로고
    • Gliding ghosts of Mycoplasma mobile
    • Uenoyama, A., and M. Miyata. 2005. Gliding ghosts of Mycoplasma mobile. Proc. Natl. Acad. Sci. USA. 102:12754-12758.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12754-12758
    • Uenoyama, A.1    Miyata, M.2
  • 16
    • 34147146510 scopus 로고    scopus 로고
    • Identification of a novel nucleoside triphosphatase from Mycoplasma mobile: A prime candidate motor for gliding motility
    • DOI 10.1042/BJ20061439
    • Ohtani, N., and M. Miyata. 2007. Identification of a novel nucleoside triphosphatase from Mycoplasma mobile: a prime candidate motor for gliding motility. Biochem. J. 403:71-77. (Pubitemid 46569868)
    • (2007) Biochemical Journal , vol.403 , Issue.1 , pp. 71-77
    • Ohtani, N.1    Miyata, M.2
  • 17
    • 37648998892 scopus 로고    scopus 로고
    • Cytoskeletal "jellyfish" structure of Mycoplasma mobile
    • Nakane, D., and M. Miyata. 2007. Cytoskeletal "jellyfish" structure of Mycoplasma mobile. Proc. Natl. Acad. Sci. USA. 104:19518-19523.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19518-19523
    • Nakane, D.1    Miyata, M.2
  • 18
    • 3042615587 scopus 로고    scopus 로고
    • Spike structure at the interface between gliding Mycoplasma mobile cells and glass surfaces visualized by rapidfreeze-and-fracture electron microscopy
    • Miyata,M., and J.D. Petersen. 2004. Spike structure at the interface between gliding Mycoplasma mobile cells and glass surfaces visualized by rapidfreeze-and-fracture electron microscopy. J. Bacteriol. 186:4382-4386.
    • (2004) J. Bacteriol. , vol.186 , pp. 4382-4386
    • Miyata, M.1    Petersen, J.D.2
  • 19
    • 1342304075 scopus 로고    scopus 로고
    • Identification of a 349-Kilodalton Protein (Gli349) Responsible for Cytadherence and Glass Binding during Gliding of Mycoplasma mobile
    • DOI 10.1128/JB.186.5.1537-1545.2004
    • Uenoyama, A., A. Kusumoto, and M. Miyata. 2004. Identification of a 349-kiloDalton protein (Gli349) responsible for cytadherence and glass binding during gliding of Mycoplasma mobile. J. Bacteriol. 186:1537-1545. (Pubitemid 38248744)
    • (2004) Journal of Bacteriology , vol.186 , Issue.5 , pp. 1537-1545
    • Uenoyama, A.1    Kusumoto, A.2    Miyata, M.3
  • 20
    • 23644447602 scopus 로고    scopus 로고
    • Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile
    • Metsugi, S., A. Uenoyama, J. Adan-Kubo, M. Miyata, K. Yura, et al. 2005. Sequence analysis of the gliding protein Gli349 in Mycoplasma mobile. Biophysics. 1:33-43.
    • (2005) Biophysics , vol.1 , pp. 33-43
    • Metsugi, S.1    Uenoyama, A.2    Adan-Kubo, J.3    Miyata, M.4    Yura, K.5
  • 21
    • 33645995096 scopus 로고    scopus 로고
    • Morphology of isolated Gli349, a leg protein responsible for Mycoplasma mobile gliding via glass binding, revealed by rotary shadowing electron microscopy
    • Adan-Kubo, J., A. Uenoyama, T. Arata, and M. Miyata. 2006. Morphology of isolated Gli349, a leg protein responsible for Mycoplasma mobile gliding via glass binding, revealed by rotary shadowing electron microscopy. J. Bacteriol. 188:2821-2828.
    • (2006) J. Bacteriol. , vol.188 , pp. 2821-2828
    • Adan-Kubo, J.1    Uenoyama, A.2    Arata, T.3    Miyata, M.4
  • 22
    • 63049089326 scopus 로고    scopus 로고
    • Regions on Gli349 and Gli521 protein molecules directly involved in movements of Mycoplasma mobile gliding machinery, suggested by use of inhibitory antibodies and mutants
    • Uenoyama, A., S. Seto, D. Nakane, and M. Miyata. 2009. Regions on Gli349 and Gli521 protein molecules directly involved in movements of Mycoplasma mobile gliding machinery, suggested by use of inhibitory antibodies and mutants. J. Bacteriol. 191:1982-1985.
    • (2009) J. Bacteriol. , vol.191 , pp. 1982-1985
    • Uenoyama, A.1    Seto, S.2    Nakane, D.3    Miyata, M.4
  • 23
    • 0036208641 scopus 로고    scopus 로고
    • Force and velocity of Mycoplasma mobile gliding
    • DOI 10.1128/JB.184.7.1827-1831.2002
    • Miyata, M., W. Ryu, and H. Berg. 2002. Force and velocity of Mycoplasma mobile gliding. J. Bacteriol. 184:1827-1831. (Pubitemid 34275523)
    • (2002) Journal of Bacteriology , vol.184 , Issue.7 , pp. 1827-1831
    • Miyata, M.1    Ryu, W.S.2    Berg, H.C.3
  • 24
    • 28044469043 scopus 로고    scopus 로고
    • Adhesion controls bacterial actin polymerization-based movement
    • Soo, F. S., and J. A. Theriot. 2005. Adhesion controls bacterial actin polymerization-based movement. Proc. Natl. Acad. Sci. USA. 102: 16233-16238.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16233-16238
    • Soo, F.S.1    Theriot, J.A.2
  • 25
    • 0342445427 scopus 로고    scopus 로고
    • Effect of temperature on kinesin-driven microtubule gliding and kinesin ATPase activity
    • Böhm, K. J., R. Stracke, M. Baum, M. Zieren, and E. Unger. 2000. Effect of temperature on kinesin-driven microtubule gliding and kinesin ATPase activity. FEBS Lett. 466:59-62.
    • (2000) FEBS Lett. , vol.466 , pp. 59-62
    • Böhm, K.J.1    Stracke, R.2    Baum, M.3    Zieren, M.4    Unger, E.5
  • 26
    • 0026545104 scopus 로고
    • Temperature dependence and Arrhenius activation energy of F-actin velocity generated in vitro by skeletal myosin
    • Anson, M. 1992. Temperature dependence and Arrhenius activation energy of F-actin velocity generated in vitro by skeletal myosin. J. Mol. Biol. 224:1029-1038.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1029-1038
    • Anson, M.1
  • 27
    • 64149110284 scopus 로고    scopus 로고
    • Molecular mechanism of Mycoplasma gliding - a novel cell motility system
    • P. Lenz, editor. Springer, New York
    • Miyata, M. 2007. Molecular mechanism of Mycoplasma gliding - a novel cell motility system. In Cell Motility. P. Lenz, editor. Springer, New York. 131-175.
    • (2007) Cell Motility , pp. 131-175
    • Miyata, M.1
  • 28
    • 37749037745 scopus 로고    scopus 로고
    • Centipede and inchworm models to explain Mycoplasma gliding
    • Miyata, M. 2008. Centipede and inchworm models to explain Mycoplasma gliding. Trends Microbiol. 16:6-12.
    • (2008) Trends Microbiol. , vol.16 , pp. 6-12
    • Miyata, M.1
  • 30
    • 33748774924 scopus 로고    scopus 로고
    • Gliding motility of Mycoplasma mobile can occur by repeated binding to N-acetylneuraminyllactose (sialyllactose) fixed on solid surfaces
    • DOI 10.1128/JB.00754-06
    • Nagai, R., and M. Miyata. 2006. Gliding motility of Mycoplasma mobile can occur by repeated binding to N-acetylneuraminyllactose (sialyllactose) fixed on solid surfaces. J. Bacteriol. 188:6469-6475. (Pubitemid 44412055)
    • (2006) Journal of Bacteriology , vol.188 , Issue.18 , pp. 6469-6475
    • Nagai, R.1    Miyata, M.2
  • 31
    • 0032037915 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of sialoadhesin in complex with 30 sialyllactose at 1.85 A° resolution
    • May, A. P., R. C. Robinson, M. Vinson, P. R. Crocker, and E. Y. Jones. 1998. Crystal structure of the N-terminal domain of sialoadhesin in complex with 30 sialyllactose at 1.85 A° resolution. Mol. Cell. 1:719-728.
    • (1998) Mol. Cell , vol.1 , pp. 719-728
    • May, A.P.1    Robinson, R.C.2    Vinson, M.3    Crocker, P.R.4    Jones, E.Y.5
  • 32
    • 37849051356 scopus 로고    scopus 로고
    • Temperature-sensitive reaction intermediate of F1-ATPase
    • Watanabe, R., R. Iino, Y. Shimaburo, M. Yoshida, and H. Noji. 2008. Temperature-sensitive reaction intermediate of F1-ATPase. EMBO Rep. 9:84-90.
    • (2008) EMBO Rep. , vol.9 , pp. 84-90
    • Watanabe, R.1    Iino, R.2    Shimaburo, Y.3    Yoshida, M.4    Noji, H.5
  • 34
    • 0026570397 scopus 로고
    • Evidence that the stalk of Drosophila kinesin heavy-chain is an α-helical coiled coil
    • Decuevas, M., T. Tao, and L. S. B. Goldstein. 1992. Evidence that the stalk of Drosophila kinesin heavy-chain is an α-helical coiled coil. J. Cell Biol. 116:957-965.
    • (1992) J. Cell Biol. , vol.116 , pp. 957-965
    • Decuevas, M.1    Tao, T.2    Goldstein, L.S.B.3
  • 35
    • 1842588296 scopus 로고    scopus 로고
    • The bacterial flagellar motor: Structure and function of a complex molecular machine
    • Kojima, S., and D. F. Blair. 2004. The bacterial flagellar motor: structure and function of a complex molecular machine. Int. Rev. Cytol. Survey Cell Biol. 233:93-134.
    • (2004) Int. Rev. Cytol. Survey Cell Biol. , vol.233 , pp. 93-134
    • Kojima, S.1    Blair, D.F.2
  • 36
    • 0041673353 scopus 로고    scopus 로고
    • The rotary motor of bacterial flagella
    • Berg, H. C. 2003. The rotary motor of bacterial flagella. Annu. Rev. Biochem. 72:19-54.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 19-54
    • Berg, H.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.