메뉴 건너뛰기




Volumn 97, Issue 1, 2009, Pages 173-182

Alternating-site mechanism of kinesin-1 characterized by single-molecule FRET using fluorescent ATP analogues

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; FLUORESCENT DYE; KINESIN 1;

EID: 68949083836     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.02.073     Document Type: Article
Times cited : (12)

References (27)
  • 1
    • 0034303806 scopus 로고    scopus 로고
    • Walking on two heads: The many talents of kinesin
    • Woehlke, G., and M. Schliwa. 2000. Walking on two heads: the many talents of kinesin. Nat. Rev. Mol. Cell Biol. 1:50-58.
    • (2000) Nat. Rev. Mol. Cell Biol , vol.1 , pp. 50-58
    • Woehlke, G.1    Schliwa, M.2
  • 2
    • 19644377414 scopus 로고    scopus 로고
    • Mechanics of the kinesin step
    • Carter, N. J., and R. A. Cross. 2005. Mechanics of the kinesin step. Nature. 435:308-312.
    • (2005) Nature , vol.435 , pp. 308-312
    • Carter, N.J.1    Cross, R.A.2
  • 3
    • 0842263751 scopus 로고    scopus 로고
    • What kinesin does at roadblocks: The coordination mechanism for molecular walking
    • Crevel, I. M., M. Nyitrai, M. C. Alonso, S. Weiss, M. A. Geeves, et al. 2004. What kinesin does at roadblocks: the coordination mechanism for molecular walking. EMBO J. 23:23-32.
    • (2004) EMBO J , vol.23 , pp. 23-32
    • Crevel, I.M.1    Nyitrai, M.2    Alonso, M.C.3    Weiss, S.4    Geeves, M.A.5
  • 4
    • 0141507035 scopus 로고    scopus 로고
    • Configuration of the two kinesin motor domains during ATP hydrolysis
    • Asenjo, A. B., N. Krohn, and H. Sosa. 2003. Configuration of the two kinesin motor domains during ATP hydrolysis. Nat. Struct. Biol. 10:836-842.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 836-842
    • Asenjo, A.B.1    Krohn, N.2    Sosa, H.3
  • 5
    • 33744500985 scopus 로고    scopus 로고
    • Backsteps induced by nucleotide analogs suggest the front head of kinesin is gated by strain
    • Guydosh, N. R., and S. M. Block. 2006. Backsteps induced by nucleotide analogs suggest the front head of kinesin is gated by strain. Proc. Natl. Acad. Sci. USA. 103:8054-8059.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8054-8059
    • Guydosh, N.R.1    Block, S.M.2
  • 6
    • 29444437883 scopus 로고    scopus 로고
    • The tethered motor domain of a kinesin-microtubule complex catalyzes reversible synthesis of bound ATP
    • Hackney, D. D. 2005. The tethered motor domain of a kinesin-microtubule complex catalyzes reversible synthesis of bound ATP. Proc. Natl. Acad. Sci. USA. 102:18338-18343.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18338-18343
    • Hackney, D.D.1
  • 7
    • 34147174317 scopus 로고    scopus 로고
    • Biochemistry. Processive motor movement
    • Hackney, D. D. 2007. Biochemistry. Processive motor movement. Science. 316:58-59.
    • (2007) Science , vol.316 , pp. 58-59
    • Hackney, D.D.1
  • 8
    • 36749068925 scopus 로고    scopus 로고
    • How kinesin waits between steps
    • Mori, T., R. D. Vale, and M. Tomishige. 2007. How kinesin waits between steps. Nature. 450:750-755.
    • (2007) Nature , vol.450 , pp. 750-755
    • Mori, T.1    Vale, R.D.2    Tomishige, M.3
  • 9
    • 0037390304 scopus 로고    scopus 로고
    • Nucleotide-induced conformations in the neck region of dimeric kinesin
    • Skiniotis, G., T. Surrey, S. Altmann, H. Gross, Y. H. Song, et al. 2003. Nucleotide-induced conformations in the neck region of dimeric kinesin. EMBO J. 22:1518-1528.
    • (2003) EMBO J , vol.22 , pp. 1518-1528
    • Skiniotis, G.1    Surrey, T.2    Altmann, S.3    Gross, H.4    Song, Y.H.5
  • 10
    • 51549097934 scopus 로고    scopus 로고
    • Intramolecular strain coordinates kinesin stepping behavior along microtubules
    • Yildiz, A., M. Tomishige, A. Gennerich, and R. D. Vale. 2008. Intramolecular strain coordinates kinesin stepping behavior along microtubules. Cell. 134:1030-1041.
    • (2008) Cell , vol.134 , pp. 1030-1041
    • Yildiz, A.1    Tomishige, M.2    Gennerich, A.3    Vale, R.D.4
  • 11
    • 34147188510 scopus 로고    scopus 로고
    • An ATP gate controls tubulin binding by the tethered head of kinesin-1
    • Alonso, M. C., D. R. Drummond, S. Kain, J. Hoeng, L. Amos, et al. 2007. An ATP gate controls tubulin binding by the tethered head of kinesin-1. Science. 316:120-123.
    • (2007) Science , vol.316 , pp. 120-123
    • Alonso, M.C.1    Drummond, D.R.2    Kain, S.3    Hoeng, J.4    Amos, L.5
  • 12
    • 0028355574 scopus 로고
    • Pre-steady-state kinetics of the microtubule-kinesin ATPase
    • Gilbert, S. P., and K. A. Johnson. 1994. Pre-steady-state kinetics of the microtubule-kinesin ATPase. Biochemistry. 33:1951-1960.
    • (1994) Biochemistry , vol.33 , pp. 1951-1960
    • Gilbert, S.P.1    Johnson, K.A.2
  • 13
    • 0028200793 scopus 로고
    • Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis
    • Hackney, D. D. 1994. Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis. Proc. Natl. Acad. Sci. USA. 91:6865-6869.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6865-6869
    • Hackney, D.D.1
  • 14
    • 0031021473 scopus 로고    scopus 로고
    • Interacting head mechanism of microtubule-kinesin ATPase
    • Ma, Y. Z., and E. W. Taylor. 1997. Interacting head mechanism of microtubule-kinesin ATPase. J. Biol. Chem. 272:724-730.
    • (1997) J. Biol. Chem , vol.272 , pp. 724-730
    • Ma, Y.Z.1    Taylor, E.W.2
  • 15
    • 34047227947 scopus 로고    scopus 로고
    • Kinesin moving through the spotlight: Single-motor fluorescence microscopy with submillisecond time resolution
    • Verbrugge, S., L. C. Kapitein, and E. J. G. Peterman. 2007. Kinesin moving through the spotlight: single-motor fluorescence microscopy with submillisecond time resolution. Biophys. J. 92:2536-2545.
    • (2007) Biophys. J , vol.92 , pp. 2536-2545
    • Verbrugge, S.1    Kapitein, L.C.2    Peterman, E.J.G.3
  • 16
    • 0034722388 scopus 로고    scopus 로고
    • Controlling kinesin by reversible disulfide cross-linking: Identifying the motility-producing conformational change
    • Tomishige, M., and R. D. Vale. 2000. Controlling kinesin by reversible disulfide cross-linking: identifying the motility-producing conformational change. J. Cell Biol. 151:1081-1092.
    • (2000) J. Cell Biol , vol.151 , pp. 1081-1092
    • Tomishige, M.1    Vale, R.D.2
  • 17
    • 33750295496 scopus 로고    scopus 로고
    • Nonblinking and longlasting single-molecule fluorescence imaging
    • Rasnik, I., S. A. McKinney, and T. Ha. 2006. Nonblinking and longlasting single-molecule fluorescence imaging. Nat. Methods. 3: 891-893.
    • (2006) Nat. Methods , vol.3 , pp. 891-893
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 18
    • 35949038838 scopus 로고
    • Thermodynamic fluctuations in a reacting system-measurement by fluorescence correlation spectroscopy
    • Magde, D., W. W. Webb, and E. Elson. 1972. Thermodynamic fluctuations in a reacting system-measurement by fluorescence correlation spectroscopy. Phys. Rev. Lett. 29:705-708.
    • (1972) Phys. Rev. Lett , vol.29 , pp. 705-708
    • Magde, D.1    Webb, W.W.2    Elson, E.3
  • 19
    • 34547348810 scopus 로고    scopus 로고
    • Measuring conformational dynamics: A new FCS-FRET approach
    • Torres, T., and M. Levitus. 2007. Measuring conformational dynamics: a new FCS-FRET approach. J. Phys. Chem. B. 111:7392-7400.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7392-7400
    • Torres, T.1    Levitus, M.2
  • 20
    • 0037331059 scopus 로고    scopus 로고
    • Ultrasensitive investigations of biological systems by fluorescence correlation spectroscopy
    • Haustein, E., and P. Schwille. 2003. Ultrasensitive investigations of biological systems by fluorescence correlation spectroscopy. Methods. 29:153-166.
    • (2003) Methods , vol.29 , pp. 153-166
    • Haustein, E.1    Schwille, P.2
  • 22
    • 3242776257 scopus 로고    scopus 로고
    • The kinetic mechanism of kinesin
    • Cross, R. A. 2004. The kinetic mechanism of kinesin. Trends Biochem. Sci. 29:301-309.
    • (2004) Trends Biochem. Sci , vol.29 , pp. 301-309
    • Cross, R.A.1
  • 23
    • 0035146785 scopus 로고    scopus 로고
    • Conformational changes during kinesin motility
    • Schief, V. R., and O. Howard. 2001. Conformational changes during kinesin motility. Curr. Opin. Cell Biol. 13:19-28.
    • (2001) Curr. Opin. Cell Biol , vol.13 , pp. 19-28
    • Schief, V.R.1    Howard, O.2
  • 24
    • 0347623370 scopus 로고    scopus 로고
    • Kinesin moves by an asymmetric hand-over-hand mechanism
    • Asbury, C. L., A. N. Fehr, and S. M. Block. 2003. Kinesin moves by an asymmetric hand-over-hand mechanism. Science. 302:2130-2134.
    • (2003) Science , vol.302 , pp. 2130-2134
    • Asbury, C.L.1    Fehr, A.N.2    Block, S.M.3
  • 25
    • 0345257160 scopus 로고    scopus 로고
    • Alternate fast and slow stepping of a heterodimeric kinesin molecule
    • Kaseda, K., H. Higuchi, and K. Hirose. 2003. Alternate fast and slow stepping of a heterodimeric kinesin molecule. Nat. Cell Biol. 5:1079-1082.
    • (2003) Nat. Cell Biol , vol.5 , pp. 1079-1082
    • Kaseda, K.1    Higuchi, H.2    Hirose, K.3
  • 27
    • 0031405880 scopus 로고    scopus 로고
    • X-ray structure of motor and neck domains from rat brain kinesin
    • Sack, S., J. Muller, A. Marx, M. Thormahlen, E. M. Mandelkow, et al. 1997. X-ray structure of motor and neck domains from rat brain kinesin. Biochemistry. 36:16155-16165.
    • (1997) Biochemistry , vol.36 , pp. 16155-16165
    • Sack, S.1    Muller, J.2    Marx, A.3    Thormahlen, M.4    Mandelkow, E.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.