메뉴 건너뛰기




Volumn 73, Issue 2, 1997, Pages 895-904

Interhead distances in myosin attached to F-actin estimated by fluorescence energy transfer spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

F ACTIN; MYOSIN;

EID: 0030749603     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78122-0     Document Type: Article
Times cited : (5)

References (57)
  • 1
    • 0021923806 scopus 로고
    • Skeletal muscle myosin subfragment-1 induces bundle formation by actin filaments
    • Ando, T., and D. Scales. 1985. Skeletal muscle myosin subfragment-1 induces bundle formation by actin filaments. J. Biol. Chem. 260: 2321-2327.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2321-2327
    • Ando, T.1    Scales, D.2
  • 3
    • 85030294246 scopus 로고    scopus 로고
    • Distance between the alkali light chains of myosin subfragment-1 bound to F-actin measured using fluorescence spectroscopy
    • Abstr.
    • Brown, L., and B. Hambly. 1996. Distance between the alkali light chains of myosin subfragment-1 bound to F-actin measured using fluorescence spectroscopy. Biophys. J. 70:A264. (Abstr.)
    • (1996) Biophys. J. , vol.70
    • Brown, L.1    Hambly, B.2
  • 4
    • 0023042843 scopus 로고
    • Interhead fluorescence energy transfer between probes attached to translationally equivalent sites on the regulatory light chains of scallop myosin
    • Chantier, P. D., and T. Tao. 1986. Interhead fluorescence energy transfer between probes attached to translationally equivalent sites on the regulatory light chains of scallop myosin. J. Mol. Biol. 192:87-99.
    • (1986) J. Mol. Biol. , vol.192 , pp. 87-99
    • Chantier, P.D.1    Tao, T.2
  • 5
    • 0000315888 scopus 로고
    • Fluorescence polarization measurement with ultraviolet polarizing filters in a spectrophotofluorometer
    • Chen, R. F., and R. L. Bowman. 1965. Fluorescence polarization measurement with ultraviolet polarizing filters in a spectrophotofluorometer. Science. 147:729-732.
    • (1965) Science , vol.147 , pp. 729-732
    • Chen, R.F.1    Bowman, R.L.2
  • 7
    • 0018464261 scopus 로고
    • Orientational freedom of molecular probes. Orientation factor in intramolecular energy transfer
    • Dale, R. E., J. Eisinger, and W. E. Blumberg. 1979. Orientational freedom of molecular probes. Orientation factor in intramolecular energy transfer. Biophys. J. 26:161-194.
    • (1979) Biophys. J. , vol.26 , pp. 161-194
    • Dale, R.E.1    Eisinger, J.2    Blumberg, W.E.3
  • 8
    • 0023316741 scopus 로고
    • Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation
    • dos Remedios, C. G., M. Miki, and J. A. Barden. 1987. Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation. J. Muscle Res. Cell Motil. 8:97-117.
    • (1987) J. Muscle Res. Cell Motil. , vol.8 , pp. 97-117
    • Dos Remedios, C.G.1    Miki, M.2    Barden, J.A.3
  • 9
    • 0028919458 scopus 로고
    • Actin and the actomyosin interface: A review
    • dos Remedios, C. G., and P. D. J. Moens. 1995a. Actin and the actomyosin interface: a review. Biochim. Biophys. Acta. 1228:99-124.
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 99-124
    • Dos Remedios, C.G.1    Moens, P.D.J.2
  • 10
    • 0028884014 scopus 로고
    • Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor
    • dos Remedios, C. G., and P. D. J. Moens. 1995b. Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor. J. Struct. Biol. 115:175-185.
    • (1995) J. Struct. Biol. , vol.115 , pp. 175-185
    • Dos Remedios, C.G.1    Moens, P.D.J.2
  • 11
    • 0002413436 scopus 로고
    • Delocalized excitation and excitation transfer
    • O. Sinanoglu, editor. Academic Press, New York
    • Förster, T. 1965. Delocalized excitation and excitation transfer. In Modern Quantum Chemistry. O. Sinanoglu, editor. Academic Press, New York. 93-137.
    • (1965) Modern Quantum Chemistry , pp. 93-137
    • Förster, T.1
  • 12
    • 0015514259 scopus 로고
    • F-actin-heavy meromyosin complex studied by optical homodyne and heterodyne methods
    • Fujime, S., S. Ishiwata, and T. Maeda. 1972. F-actin-heavy meromyosin complex studied by optical homodyne and heterodyne methods. Biochim. Biophys. Acta. 283:351-363.
    • (1972) Biochim. Biophys. Acta , vol.283 , pp. 351-363
    • Fujime, S.1    Ishiwata, S.2    Maeda, T.3
  • 13
    • 0019332185 scopus 로고
    • Dissociation of the actin-subfragment 1 complex by adenyl-5′-yl imidodiphosphate, ADP, and PPi
    • Greene, L. E., and E. Eisenberg. 1980. Dissociation of the actin-subfragment 1 complex by adenyl-5′-yl imidodiphosphate, ADP, and PPi. J. Biol. Chem. 255:543-548.
    • (1980) J. Biol. Chem. , vol.255 , pp. 543-548
    • Greene, L.E.1    Eisenberg, E.2
  • 14
    • 0017382537 scopus 로고
    • The effects of temperature and salts on myosin subfragment-1 and F-actin association
    • Highsmith, S. 1977. The effects of temperature and salts on myosin subfragment-1 and F-actin association. Arch. Biochem. Biophys. 180: 404-408.
    • (1977) Arch. Biochem. Biophys. , vol.180 , pp. 404-408
    • Highsmith, S.1
  • 15
    • 0017885347 scopus 로고
    • Heavy meromyosin binds actin with negative cooperativity
    • Highsmith, S. 1978. Heavy meromyosin binds actin with negative cooperativity. Biochemistry. 17:22-26.
    • (1978) Biochemistry , vol.17 , pp. 22-26
    • Highsmith, S.1
  • 16
  • 17
    • 0015820465 scopus 로고
    • Synthesis and characterization of two fluorescent sulfhydryl reagents
    • Hudson, E. N., and G. Weber. 1973. Synthesis and characterization of two fluorescent sulfhydryl reagents. Biochemistry. 12:4154-4161.
    • (1973) Biochemistry , vol.12 , pp. 4154-4161
    • Hudson, E.N.1    Weber, G.2
  • 18
    • 0023655206 scopus 로고
    • Rotational motions of myosin heads in myofibril studied by phosphorescence anisotropy decay measurements
    • Ishiwata, S., K. Kinosita, Jr., H. Yoshimura, and A. Ikegami. 1987a. Rotational motions of myosin heads in myofibril studied by phosphorescence anisotropy decay measurements. J. Biol. Chem. 262: 8314-8317.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8314-8317
    • Ishiwata, S.1    Kinosita K., Jr.2    Yoshimura, H.3    Ikegami, A.4
  • 19
    • 85030297245 scopus 로고
    • Measurement of inter-head distance of myosin using fluorescence energy transfer method
    • Abstr.
    • Ishiwata, S., M. Miki, and C. G. dos Remedios. 1987b. Measurement of inter-head distance of myosin using fluorescence energy transfer method. Biophys. Suppl. (Japanese). 27:S86. (Abstr.)
    • (1987) Biophys. Suppl. (Japanese) , vol.27
    • Ishiwata, S.1    Miki, M.2    Dos Remedios, C.G.3
  • 21
    • 85030297381 scopus 로고    scopus 로고
    • Distance between myosin heads in rigor complex measured by fluorescence resonance energy transfer
    • Abstr.
    • Ishiwata, S., M. Miki, I. Shin, T. Funatsu, K. Yasuda, and C. G. dos Remedios. 1996. Distance between myosin heads in rigor complex measured by fluorescence resonance energy transfer. Biophys. J. 70: A14. (Abstr.)
    • (1996) Biophys. J. , vol.70
    • Ishiwata, S.1    Miki, M.2    Shin, I.3    Funatsu, T.4    Yasuda, K.5    Dos Remedios, C.G.6
  • 22
    • 0021203107 scopus 로고
    • ADP binds similarly to rigor muscle myofibrils and to actomyosin-subfragment one
    • Johnson, R. E., and P. H. Adams. 1984. ADP binds similarly to rigor muscle myofibrils and to actomyosin-subfragment one. FEBS Lett. 174: 11-14.
    • (1984) FEBS Lett. , vol.174 , pp. 11-14
    • Johnson, R.E.1    Adams, P.H.2
  • 24
    • 0024286070 scopus 로고
    • Orientation of the actin monomer in the F-actin filament: Radial coordinate of glutamine-41 and effect of myosin subfragment-1 binding on the monomer orientation
    • Kasprzak, A. A., R. Takashi, and M. F. Morales. 1988. Orientation of the actin monomer in the F-actin filament: radial coordinate of glutamine-41 and effect of myosin subfragment-1 binding on the monomer orientation. Biochemistry. 27:4512-4522.
    • (1988) Biochemistry , vol.27 , pp. 4512-4522
    • Kasprzak, A.A.1    Takashi, R.2    Morales, M.F.3
  • 25
    • 0019486961 scopus 로고
    • Three-dimensional image-analysis of the complex of thin filaments and myosin molecules from skeletal muscle. III. The multi-domain structure of actin heavy meromyosin complex
    • Katayama, E., and T. Wakabayashi. 1981. Three-dimensional image-analysis of the complex of thin filaments and myosin molecules from skeletal muscle. III. The multi-domain structure of actin heavy meromyosin complex. J. Biochem. 90:703-714.
    • (1981) J. Biochem. , vol.90 , pp. 703-714
    • Katayama, E.1    Wakabayashi, T.2
  • 26
    • 84961006038 scopus 로고
    • The relation between sulfhydryl groups and the activation of myosin adenosinetriphosphatase
    • Kielley, W. W., and L. B. Bradley. 1956. The relation between sulfhydryl groups and the activation of myosin adenosinetriphosphatase. J. Biol. Chem. 218:653-659.
    • (1956) J. Biol. Chem. , vol.218 , pp. 653-659
    • Kielley, W.W.1    Bradley, L.B.2
  • 27
    • 0021672333 scopus 로고
    • Submicrosecond and microsecond rotational motions of myosin head in solution and in myosin synthetic filaments as revealed by time-resolved optical anisotropy decay measurements
    • Kinosita, Jr., K., S. Ishiwata, H. Yoshimura, H. Asai, and A. Ikegami. 1984. Submicrosecond and microsecond rotational motions of myosin head in solution and in myosin synthetic filaments as revealed by time-resolved optical anisotropy decay measurements. Biochemistry. 23:5963-5975.
    • (1984) Biochemistry , vol.23 , pp. 5963-5975
    • Kinosita K., Jr.1    Ishiwata, S.2    Yoshimura, H.3    Asai, H.4    Ikegami, A.5
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0015526770 scopus 로고
    • Intrinsic fluorescence of actin
    • Lehrer, S. S., and G. Kerwar. 1972. Intrinsic fluorescence of actin. Biochemistry. 11:1211-1217.
    • (1972) Biochemistry , vol.11 , pp. 1211-1217
    • Lehrer, S.S.1    Kerwar, G.2
  • 30
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz, M., D. Popp, and K. C. Holmes. 1993. Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 31
    • 0018254914 scopus 로고
    • Interaction of myosin subfragments with F-actin
    • Margossian, S. S., and S. Lowey. 1978. Interaction of myosin subfragments with F-actin. Biochemistry. 17:5431-5439.
    • (1978) Biochemistry , vol.17 , pp. 5431-5439
    • Margossian, S.S.1    Lowey, S.2
  • 32
    • 0016724777 scopus 로고
    • The dissociation constant of the actin-heavy meromyosin subfragment-1 complex
    • Marston, S., and A. Weber. 1975. The dissociation constant of the actin-heavy meromyosin subfragment-1 complex. Biochemistry. 14: 3868-3873.
    • (1975) Biochemistry , vol.14 , pp. 3868-3873
    • Marston, S.1    Weber, A.2
  • 33
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin, P. J., J. T. Gooch, H.-G. Mannherz, and A. G. Weeds. 1993. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature. 364:685-692.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.-G.3    Weeds, A.G.4
  • 34
    • 0023090644 scopus 로고
    • The recovery of the polymerization of Lys-61-labeled actin by the addition of phalloidin
    • Miki, M. 1987. The recovery of the polymerization of Lys-61-labeled actin by the addition of phalloidin. Eur. J. Biochem. 164:229-235.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 229-235
    • Miki, M.1
  • 35
    • 0026535887 scopus 로고
    • Structure of actin observed by fluorescence resonance energy transfer spectroscopy
    • Miki, M., S. I. O'Donoghue, and C. G. dos Remedios. 1992. Structure of actin observed by fluorescence resonance energy transfer spectroscopy. J. Muscle Res. Cell Motil. 13:132-145.
    • (1992) J. Muscle Res. Cell Motil. , vol.13 , pp. 132-145
    • Miki, M.1    O'Donoghue, S.I.2    Dos Remedios, C.G.3
  • 36
    • 0021759053 scopus 로고
    • Fluorescence energy transfer between points in acto-subfragment-1 rigor complex
    • Miki, M., and P. Wahl. 1984. Fluorescence energy transfer between points in acto-subfragment-1 rigor complex. Biochim. Biophys. Acta. 790: 275-283.
    • (1984) Biochim. Biophys. Acta , vol.790 , pp. 275-283
    • Miki, M.1    Wahl, P.2
  • 37
    • 0024596276 scopus 로고
    • Differential behavior of two cysteine residues on the myosin head in muscle fibers
    • Miyanishi, T., and J. Borejdo. 1989. Differential behavior of two cysteine residues on the myosin head in muscle fibers. Biochemistry. 28: 1287-1294.
    • (1989) Biochemistry , vol.28 , pp. 1287-1294
    • Miyanishi, T.1    Borejdo, J.2
  • 38
    • 0028077728 scopus 로고
    • Determination of the radial coordinate of Cys-374 in F-actin using fluorescence resonance energy transfer spectroscopy: Effect of phalloidin on polymer assembly
    • Moens, P. D. J., D. J. Yee, and C. G. dos Remedios. 1994. Determination of the radial coordinate of Cys-374 in F-actin using fluorescence resonance energy transfer spectroscopy: effect of phalloidin on polymer assembly. Biochemistry. 33:13102-13108.
    • (1994) Biochemistry , vol.33 , pp. 13102-13108
    • Moens, P.D.J.1    Yee, D.J.2    Dos Remedios, C.G.3
  • 39
    • 0025274490 scopus 로고
    • The rigor configuration of smooth muscle heavy meromyosin trapped by a zero-length cross-linker
    • Onishi, H., and K. Fujiwara. 1990. The rigor configuration of smooth muscle heavy meromyosin trapped by a zero-length cross-linker. Biochemistry. 29:3013-3023.
    • (1990) Biochemistry , vol.29 , pp. 3013-3023
    • Onishi, H.1    Fujiwara, K.2
  • 40
    • 0024554122 scopus 로고
    • Evidence for the association between two myosin heads in rigor acto-smooth muscle heavy meromyosin
    • Onishi, H., T. Maita, G. Matsuda, and K. Fujiwara. 1989. Evidence for the association between two myosin heads in rigor acto-smooth muscle heavy meromyosin. Biochemistry. 28:1898-1904.
    • (1989) Biochemistry , vol.28 , pp. 1898-1904
    • Onishi, H.1    Maita, T.2    Matsuda, G.3    Fujiwara, K.4
  • 45
    • 0014518456 scopus 로고
    • Similar effects on enzymic activity due Io chemical modification of either of two sulfhydryl groups of myosin
    • Seidel, J. C. 1969. Similar effects on enzymic activity due Io chemical modification of either of two sulfhydryl groups of myosin. Biochim. Biophys. Acta. 180:216-219.
    • (1969) Biochim. Biophys. Acta , vol.180 , pp. 216-219
    • Seidel, J.C.1
  • 46
    • 0000673210 scopus 로고
    • Enzymic properties of N-ethylmaleimide modified myosin
    • Sekine, T., and W. W. Kielley. 1964. Enzymic properties of N-ethylmaleimide modified myosin. Biochim. Biophys. Acta. 81:336-345.
    • (1964) Biochim. Biophys. Acta , vol.81 , pp. 336-345
    • Sekine, T.1    Kielley, W.W.2
  • 47
    • 0019889053 scopus 로고
    • Location of SH1 and SH2 along a heavy chain of myosin subfragment 1
    • Sutoh, K. 1981. Location of SH1 and SH2 along a heavy chain of myosin subfragment 1. Biochemistry. 20:3281-3285.
    • (1981) Biochemistry , vol.20 , pp. 3281-3285
    • Sutoh, K.1
  • 48
    • 0021590825 scopus 로고
    • Electron microscopic visualization of the SH1 thiol of myosin by the use of an avidin-biotin system
    • Sutoh, K., K. Yamamoto, and T. Wakabayashi. 1984. Electron microscopic visualization of the SH1 thiol of myosin by the use of an avidin-biotin system. J. Mol. Biol. 178:323-339.
    • (1984) J. Mol. Biol. , vol.178 , pp. 323-339
    • Sutoh, K.1    Yamamoto, K.2    Wakabayashi, T.3
  • 49
    • 0022495021 scopus 로고
    • Electron microscopic visualization of the ATPase site of myosin by photoaffinity labeling with a biotinylated photoreactive ATP analog
    • Sutoh, K., K. Yamamoto, and T. Wakabayashi. 1986. Electron microscopic visualization of the ATPase site of myosin by photoaffinity labeling with a biotinylated photoreactive ATP analog. Proc. Natl. Acad. Sci. USA. 83:212-216.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 212-216
    • Sutoh, K.1    Yamamoto, K.2    Wakabayashi, T.3
  • 50
    • 0018789686 scopus 로고
    • Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of acto subfragment-1
    • Takashi, R. 1979. Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of acto subfragment-1. Biochemistry. 18:5164-5169.
    • (1979) Biochemistry , vol.18 , pp. 5164-5169
    • Takashi, R.1
  • 51
    • 0019442257 scopus 로고
    • Detection of actin assembly by fluorescence energy transfer
    • Taylor, D. L., J. Reidler, J. A. Spudich, and L. Stryer. 1981. Detection of actin assembly by fluorescence energy transfer. J. Cell Biol. 89: 362-367.
    • (1981) J. Cell Biol. , vol.89 , pp. 362-367
    • Taylor, D.L.1    Reidler, J.2    Spudich, J.A.3    Stryer, L.4
  • 52
    • 0028861589 scopus 로고
    • Normal modes as refinement parameters for the F-actin model
    • Tirion, M. M., D. ben-Avraham, M. Lorenz, and K. C. Holmes. 1995. Normal modes as refinement parameters for the F-actin model. Biophys. J. 68:5-12.
    • (1995) Biophys. J. , vol.68 , pp. 5-12
    • Tirion, M.M.1    Ben-Avraham, D.2    Lorenz, M.3    Holmes, K.C.4
  • 53
    • 0023261634 scopus 로고
    • Location of the ATPase site of myosin determined by three-dimensional electron microscopy
    • Tokunaga, M., K. Sutoh, C. Toyoshima, and T. Wakabayashi. 1987. Location of the ATPase site of myosin determined by three-dimensional electron microscopy. Nature. 329:635-638.
    • (1987) Nature , vol.329 , pp. 635-638
    • Tokunaga, M.1    Sutoh, K.2    Toyoshima, C.3    Wakabayashi, T.4
  • 54
    • 0343877397 scopus 로고
    • Three-dimensional image analysis of the actin-tropomyosin-myosin subfragment-1 complex: Location of specifically reactive thiol SH1
    • Y. Mukohata, M. F. Morales, and S. Fleischer, editors. Yamada Science Foundation, Osaka
    • Toyoshima, C., K. Yamamoto, K. Sutoh, T. Sekine, and T. Wakabayashi. 1985. Three-dimensional image analysis of the actin-tropomyosin-myosin subfragment-1 complex: location of specifically reactive thiol SH1. Proceedings of Yamada Conference XI on Energy Transduction in ATPases, Y. Mukohata, M. F. Morales, and S. Fleischer, editors. Yamada Science Foundation, Osaka. 162-163.
    • (1985) Proceedings of Yamada Conference XI on Energy Transduction in ATPases , pp. 162-163
    • Toyoshima, C.1    Yamamoto, K.2    Sutoh, K.3    Sekine, T.4    Wakabayashi, T.5
  • 55
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility
    • Weeds, A. G., and B. Pope. 1977. Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111:129-157.
    • (1977) J. Mol. Biol. , vol.111 , pp. 129-157
    • Weeds, A.G.1    Pope, B.2
  • 56
    • 0017044811 scopus 로고
    • Energetics and mechanism of actomyosin adenosine triphosphatase
    • White, H. D., and E. W. Taylor. 1976. Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry. 15:5818-5826.
    • (1976) Biochemistry , vol.15 , pp. 5818-5826
    • White, H.D.1    Taylor, E.W.2
  • 57
    • 0029049213 scopus 로고
    • Rigor cross-bridges bind to two actin monomers in thin filaments of rabbit psoas muscle
    • Xiao, M., Andreev, O. A., and J. Borejdo. 1995. Rigor cross-bridges bind to two actin monomers in thin filaments of rabbit psoas muscle. J. Mol. Biol. 248:294-307.
    • (1995) J. Mol. Biol. , vol.248 , pp. 294-307
    • Xiao, M.1    Andreev, O.A.2    Borejdo, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.