메뉴 건너뛰기




Volumn 84, Issue 1, 2003, Pages 634-642

The 2′-O- and 3′-O-Cy3-EDA-ATP(ADP) complexes with myosin subfragment-1 are spectroscopically distinct

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE DERIVATIVE; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN SUBFRAGMENT 1; ADENOSINE TRIPHOSPHATE; DRUG DERIVATIVE; MYOSIN SUBFRAGMENT;

EID: 0037215766     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74883-8     Document Type: Article
Times cited : (24)

References (36)
  • 1
    • 0023317270 scopus 로고
    • Fluorescence lifetime distributions in proteins
    • Alcala, J. R., E. Gratton, and F. G. Prendergast. 1987. Fluorescence lifetime distributions in proteins. Biophys. J. 51:597-604.
    • (1987) Biophys. J. , vol.51 , pp. 597-604
    • Alcala, J.R.1    Gratton, E.2    Prendergast, F.G.3
  • 2
    • 85031256465 scopus 로고    scopus 로고
    • Fluorescence lifetime and polarization measurements by phase fluorometry of 2′-O- and O-Cy3-EDA-ATP(ADP) on binding to myosin subfragment-1
    • Abstr
    • Anson, M., K. Oiwa, J. F. Eccleston, and D. M. Jameson. 2000. Fluorescence lifetime and polarization measurements by phase fluorometry of 2′-O- and O-Cy3-EDA-ATP(ADP) on binding to myosin subfragment-1. Biophys. J. 78:A753. (Abstr.)
    • (2000) Biophys. J. , vol.78
    • Anson, M.1    Oiwa, K.2    Eccleston, J.F.3    Jameson, D.M.4
  • 3
    • 85031254575 scopus 로고    scopus 로고
    • Transient anisotropy and lifetime studies of 2′ and 3′-O-Cy3-EDA-AT(D)P complexes with myosin-S1
    • Abstr
    • Anson, M., J. F. Eccleston, K. Oiwa, J. C. Croney, and D. M. Jameson. 2002. Transient anisotropy and lifetime studies of 2′ and 3′-O-Cy3-EDA-AT(D)P complexes with myosin-S1. Biophys. J. 82:436A. (Abstr.)
    • (2002) Biophys. J. , vol.82
    • Anson, M.1    Eccleston, J.F.2    Oiwa, K.3    Croney, J.C.4    Jameson, D.M.5
  • 5
    • 0034536399 scopus 로고    scopus 로고
    • A comparison of optical geometries for combined flash photolysis and total internal reflection fluorescence microscopy
    • Conibear, P. B., and C. R. Bagshaw. 2000. A comparison of optical geometries for combined flash photolysis and total internal reflection fluorescence microscopy. J. Microsc. 200:218-229.
    • (2000) J. Microsc. , vol.200 , pp. 218-229
    • Conibear, P.B.1    Bagshaw, C.R.2
  • 6
    • 0032483129 scopus 로고    scopus 로고
    • Raman difference spectroscopic studies of the myosin S1.MgADP.vanadate complex
    • Deng, H., J. Wang, R. H. Callender, J. C. Grammer, and R. G. Yount. 1998. Raman difference spectroscopic studies of the myosin S1.MgADP.vanadate complex. Biochemistry. 37:10972-10979.
    • (1998) Biochemistry , vol.37 , pp. 10972-10979
    • Deng, H.1    Wang, J.2    Callender, R.H.3    Grammer, J.C.4    Yount, R.G.5
  • 9
    • 0028945654 scopus 로고
    • Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
    • Funatsu, T., Y. Harada, M. Tokunaga, K. Saito, and T. Yanagida. 1995. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature. 374:555-559.
    • (1995) Nature , vol.374 , pp. 555-559
    • Funatsu, T.1    Harada, Y.2    Tokunaga, M.3    Saito, K.4    Yanagida, T.5
  • 10
    • 0001064670 scopus 로고
    • Inhibition of myosin ATPase by vanadate ion
    • Goodno, C. C. 1979. Inhibition of myosin ATPase by vanadate ion. Proc. Natl. Acad. Sci. USA. 76:2620-2624.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2620-2624
    • Goodno, C.C.1
  • 11
    • 1542457435 scopus 로고
    • Inhibition of actomyosin ATPase by vanadate
    • Goodno, C. C., and E. W. Taylor. 1981. Inhibition of actomyosin ATPase by vanadate. Proc. Natl. Acad. Sci. USA. 79:21-25.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 21-25
    • Goodno, C.C.1    Taylor, E.W.2
  • 15
    • 0024501937 scopus 로고
    • Time-resolved fluorescence studies on the ternary complex formed between bacterial elongation factor Tu, guanosine 5′-triphosphate, and phenylalanyltRNAPhe
    • Hazlett, T. L., A. E. Johnson, and D. M. Jameson. 1989. Time-resolved fluorescence studies on the ternary complex formed between bacterial elongation factor Tu, guanosine 5′-triphosphate, and phenylalanyltRNAPhe. Biochemistry. 28:4109-4117.
    • (1989) Biochemistry , vol.28 , pp. 4109-4117
    • Hazlett, T.L.1    Johnson, A.E.2    Jameson, D.M.3
  • 16
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • Ishijima, A., H. Kojima, T. Funatsu, M. Tokunaga, H. Higuchi, H. Tanaka, and T. Yanagida. 1998. Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell. 92:161-171.
    • (1998) Cell , vol.92 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7
  • 17
    • 0039617818 scopus 로고    scopus 로고
    • Single molecular assay of individual ATP turnover by a myosin-GFP fusion protein expressed in vitro
    • Iwane, A. H., T. Funatsu, Y. Harada, M. Tokunaga, O. Ohara, S. Morimoto, and T. Yanagida. 1997. Single molecular assay of individual ATP turnover by a myosin-GFP fusion protein expressed in vitro. FEBS Lett. 407:235-238.
    • (1997) FEBS Lett. , vol.407 , pp. 235-238
    • Iwane, A.H.1    Funatsu, T.2    Harada, Y.3    Tokunaga, M.4    Ohara, O.5    Morimoto, S.6    Yanagida, T.7
  • 18
    • 0030971247 scopus 로고    scopus 로고
    • Fluorescent nucleotide analogs: Synthesis and applications
    • Jameson, D. M., and J. F. Eccleston. 1997. Fluorescent nucleotide analogs: Synthesis and applications. Meth. Enzymol. 278:363-390.
    • (1997) Meth. Enzymol. , vol.278 , pp. 363-390
    • Jameson, D.M.1    Eccleston, J.F.2
  • 19
    • 0003053080 scopus 로고
    • The measurement and analysis of heterogeneous emissions by multifrequency
    • Jameson, D. M., E. Gratton, and R. D. Hall. 1984. The measurement and analysis of heterogeneous emissions by multifrequency. Appl. Spectro. Rev. 20:55-106.
    • (1984) Appl. Spectro. Rev. , vol.20 , pp. 55-106
    • Jameson, D.M.1    Gratton, E.2    Hall, R.D.3
  • 20
    • 0002328791 scopus 로고
    • Time-resolved fluorescence measurements in biology and biochemistry
    • G. Dewey, editor. Plenum Press, New York
    • Jameson, D. M., and T. L. Hazlett. 1991. Time-resolved fluorescence measurements in biology and biochemistry. In Biophysical and Biochemical Aspects of Fluorescence. G. Dewey, editor. Plenum Press, New York. 105-133.
    • (1991) Biophysical and Biochemical Aspects of Fluorescence , pp. 105-133
    • Jameson, D.M.1    Hazlett, T.L.2
  • 21
    • 85031258322 scopus 로고    scopus 로고
    • Single molecule kinetic studies using fluorescent ATP analogs: Photobleaching and myosin ATPase rates of Alexa546-, Alexa532- and Cy3-EDA-ATP
    • Abstr
    • Kikumoto, M., K. Oiwa, and M. Anson. 2000. Single molecule kinetic studies using fluorescent ATP analogs: Photobleaching and myosin ATPase rates of Alexa546-, Alexa532- and Cy3-EDA-ATP. Biophys. J. 78:385A. (Abstr.)
    • (2000) Biophys. J. , vol.78
    • Kikumoto, M.1    Oiwa, K.2    Anson, M.3
  • 22
    • 0032484096 scopus 로고    scopus 로고
    • Single-molecule enzymatic dynamics
    • Lu, H. P., L. Xun, and X. S. Xie. 1998. Single-molecule enzymatic dynamics. Science. 282:1877-1882.
    • (1998) Science , vol.282 , pp. 1877-1882
    • Lu, H.P.1    Xun, L.2    Xie, X.S.3
  • 24
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian, S. S., and S. Lowey. 1982. Preparation of myosin and its subfragments from rabbit skeletal muscle. Meth. Enzymol. 85:55-71.
    • (1982) Meth. Enzymol. , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 26
    • 0001107520 scopus 로고    scopus 로고
    • Microscopic observations of single Cy3-EDA-Adenine nucleotide molecules interacting with myosin filaments in vitro
    • Abstr
    • Oiwa, K., M. Anson, J. F. Eccleston, J. E. T. Corrie, A. Yamada, H. Nakayama, and D. R. Trentham. 1996. Microscopic observations of single Cy3-EDA-Adenine nucleotide molecules interacting with myosin filaments in vitro. Biophys. J. 70:A159. (Abstr.)
    • (1996) Biophys. J. , vol.70
    • Oiwa, K.1    Anson, M.2    Eccleston, J.F.3    Corrie, J.E.T.4    Yamada, A.5    Nakayama, H.6    Trentham, D.R.7
  • 27
    • 4243245416 scopus 로고    scopus 로고
    • Isolation and characterization of 2′-O- and 3′-O-isomers of Cy3-EDA-ATP: Kinetics and single molecule studies
    • Abstr
    • Oiwa, K., M. Anson, J. F. Eccleston, and D. R. Trentham. 1998. Isolation and characterization of 2′-O- and 3′-O-isomers of Cy3-EDA-ATP: Kinetics and single molecule studies. Biophys. J. 74:A260. (Abstr.)
    • (1998) Biophys. J. , vol.74
    • Oiwa, K.1    Anson, M.2    Eccleston, J.F.3    Trentham, D.R.4
  • 29
    • 85031264295 scopus 로고    scopus 로고
    • Fluorescence, anisotropy and lifetime measurements of 2′ and 3′-O-Cy3-EDA-A(T)DP binding in myosin-S1. Vanadate complexes
    • Abstr
    • Oiwa, K., D. M. Jameson, J. C. Croney, J. F. Eccleston, and M. Anson. 2001. Fluorescence, anisotropy and lifetime measurements of 2′ and 3′-O-Cy3-EDA-A(T)DP binding in myosin-S1. Vanadate complexes. Biophys. J. 80:A1401. (Abstr.)
    • (2001) Biophys. J. , vol.80
    • Oiwa, K.1    Jameson, D.M.2    Croney, J.C.3    Eccleston, J.F.4    Anson, M.5
  • 30
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesium(II)·ADP·vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution
    • Smith, C. A., and I. Rayment. 1996. X-ray structure of the magnesium(II)·ADP·vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution. Biochemistry. 35:5404-5417.
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 31
    • 84981857769 scopus 로고
    • Measurement of subnanosecond fluorescence lifetimes with a cross-correlation phase fluorometer
    • Spencer, R. D., and G. Weber. 1969. Measurement of subnanosecond fluorescence lifetimes with a cross-correlation phase fluorometer. Ann. N. Y. Acad. Sci. 158:361-376.
    • (1969) Ann. N. Y. Acad. Sci. , vol.158 , pp. 361-376
    • Spencer, R.D.1    Weber, G.2
  • 32
    • 36849115843 scopus 로고
    • Influence of Brownian rotations and energy transfer upon the measurements of fluorescence lifetime
    • Spencer, R. D., and G. Weber. 1970. Influence of Brownian rotations and energy transfer upon the measurements of fluorescence lifetime. J. Phys. Chem. 52:1654-1663.
    • (1970) J. Phys. Chem. , vol.52 , pp. 1654-1663
    • Spencer, R.D.1    Weber, G.2
  • 34
    • 0033548686 scopus 로고    scopus 로고
    • Fluorescence spectroscopy of single biomolecules
    • Weiss, S. 1999. Fluorescence spectroscopy of single biomolecules. Science. 283:1676-1683.
    • (1999) Science , vol.283 , pp. 1676-1683
    • Weiss, S.1
  • 35
    • 0026018966 scopus 로고
    • Kinetics of the interaction of 2′(3′)-O-(N-methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1: Characterization of two acto-S1-ADP complexes
    • Woodward, S. K. A., J. F. Eccleston, and M. A. Geeves. 1991. Kinetics of the interaction of 2′(3′)-O-(N-methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1: Characterization of two acto-S1-ADP complexes. Biochemistry. 30:422-430.
    • (1991) Biochemistry , vol.30 , pp. 422-430
    • Woodward, S.K.A.1    Eccleston, J.F.2    Geeves, M.A.3
  • 36
    • 0033523011 scopus 로고    scopus 로고
    • Single-molecule enzymology
    • Xie, X. S., and H. P. Lu. 1999. Single-molecule enzymology. J. Biol. Chem. 274:15967-15970.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15967-15970
    • Xie, X.S.1    Lu, H.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.