메뉴 건너뛰기




Volumn 120, Issue 3, 1996, Pages 580-586

Mapping myosin-binding sites on actin probed by peptides that inhibit actomyosin interaction

Author keywords

Actin; Acto S1; Acto S1 ATPase; Actomyosin; Myosin

Indexed keywords

1 (3 DIMETHYLAMINOPROPYL) 3 ETHYLCARBODIIMIDE; ACTIN; ADENOSINE TRIPHOSPHATE; DANSYL CHLORIDE; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN HEAVY CHAIN; PEPTIDASE; PEPTIDE;

EID: 0029740307     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021453     Document Type: Article
Times cited : (3)

References (29)
  • 1
    • 0021992946 scopus 로고
    • Muscle contraction and free energy transduction in biological systems
    • Eisenberg, E. and Hill, T.L. (1985) Muscle contraction and free energy transduction in biological systems. Science 227, 999-1006
    • (1985) Science , vol.227 , pp. 999-1006
    • Eisenberg, E.1    Hill, T.L.2
  • 4
    • 0029558590 scopus 로고
    • Crosslinking of a 28-residue N-terminal peptide of actin to myosin subfragment 1
    • Kunori, S., Katoh, T., Mogi, Y., and Morita, F. (1995) Crosslinking of a 28-residue N-terminal peptide of actin to myosin subfragment 1. J. Biochem. 118, 1239-1247
    • (1995) J. Biochem. , vol.118 , pp. 1239-1247
    • Kunori, S.1    Katoh, T.2    Mogi, Y.3    Morita, F.4
  • 5
    • 0027053493 scopus 로고
    • Synthetic peptide of the sequence 632-642 on myosin subfragment 1 inhibits actomyosin ATPase activity
    • Cheung, P. and Reisler, E. (1992) Synthetic peptide of the sequence 632-642 on myosin subfragment 1 inhibits actomyosin ATPase activity. Biochem. Biophys. Res. Commun. 189, 1143-1149
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 1143-1149
    • Cheung, P.1    Reisler, E.2
  • 6
    • 0026593988 scopus 로고
    • Actomyosin interactions in the presence of ATP and N-terminal segment of actin
    • DasGupta, G. and Reisler, E. (1992) Actomyosin interactions in the presence of ATP and N-terminal segment of actin. Biochemistry 31, 1836-1841
    • (1992) Biochemistry , vol.31 , pp. 1836-1841
    • Dasgupta, G.1    Reisler, E.2
  • 7
    • 0025858239 scopus 로고
    • Site-directed mutations of Dictyostelium actin: Disruption of a negative charge cluster at the N terminus
    • Sutoh, K., Ando, M., Sutoh, K., and Toyoshima, Y.Y. (1991) Site-directed mutations of Dictyostelium actin: Disruption of a negative charge cluster at the N terminus. Proc. Natl. Acad. Sci. USA 88, 7711-7714
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7711-7714
    • Sutoh, K.1    Ando, M.2    Sutoh, K.3    Toyoshima, Y.Y.4
  • 9
    • 0027509598 scopus 로고
    • Actin-bindingpeptides obtained from the C-terminal 24-kDa fragment of porcine aorta smooth muscle myosin subfragment-1 heavy chain
    • Katoh, T. and Morita, F. (1993) Actin-bindingpeptides obtained from the C-terminal 24-kDa fragment of porcine aorta smooth muscle myosin subfragment-1 heavy chain. J. Biol. Chem. 268, 2380-2388
    • (1993) J. Biol. Chem. , vol.268 , pp. 2380-2388
    • Katoh, T.1    Morita, F.2
  • 10
    • 77956984659 scopus 로고
    • Myosin adenosinetriphosphatase
    • Perry, S.V. (1955) Myosin adenosinetriphosphatase. Methods Enzymol. 2, 582-588
    • (1955) Methods Enzymol. , vol.2 , pp. 582-588
    • Perry, S.V.1
  • 11
    • 0014975959 scopus 로고
    • Studies on enzymatically active subfragments of myosin-adenosine triphosphatase. I. Preparation using chymotrypsin
    • Onodera, M, and Yagi, K. (1971) Studies on enzymatically active subfragments of myosin-adenosine triphosphatase. I. Preparation using chymotrypsin. J. Biochem. 69, 145-153
    • (1971) J. Biochem. , vol.69 , pp. 145-153
    • Onodera, M.1    Yagi, K.2
  • 12
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J.A. and Watt, S. (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246, 4866-4871
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 13
    • 0028832434 scopus 로고
    • The effect of cross-linking of the two heads of porcine aorta smooth muscle myosin on its conformation and enzymic activity
    • Katoh, T. and Morita, F. (1995) The effect of cross-linking of the two heads of porcine aorta smooth muscle myosin on its conformation and enzymic activity. Eur. J. Biochem. 233, 123-131
    • (1995) Eur. J. Biochem. , vol.233 , pp. 123-131
    • Katoh, T.1    Morita, F.2
  • 14
    • 3342922088 scopus 로고
    • A microcolorimetric method for the determination of inorganic phosphorous
    • Taussky, H.H. and Shorr, E. (1953) A microcolorimetric method for the determination of inorganic phosphorous. J. Biol. Chem. 202, 675-685
    • (1953) J. Biol. Chem. , vol.202 , pp. 675-685
    • Taussky, H.H.1    Shorr, E.2
  • 15
    • 0020013525 scopus 로고
    • Special instrumentation and techniques for kinetic studies of contractile systems
    • White, H.D. (1982) Special instrumentation and techniques for kinetic studies of contractile systems. Methods Enzymol. 85, 698-708
    • (1982) Methods Enzymol. , vol.85 , pp. 698-708
    • White, H.D.1
  • 16
    • 0023498598 scopus 로고
    • A rapid vapor-phase acid (hydrochloric acid and trifluoroacetic acid) hydrolysis of peptide and protein
    • Tsugita, A., Uchida, T., Mewes, H.W., and Ataka, T. (1987) A rapid vapor-phase acid (hydrochloric acid and trifluoroacetic acid) hydrolysis of peptide and protein. J. Biochem. 102, 1593-1597
    • (1987) J. Biochem. , vol.102 , pp. 1593-1597
    • Tsugita, A.1    Uchida, T.2    Mewes, H.W.3    Ataka, T.4
  • 17
    • 0017342054 scopus 로고
    • Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Porzio, M.A. and Pearson, A.M. (1977) Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochim. Biophys. Acta 490, 27-34
    • (1977) Biochim. Biophys. Acta , vol.490 , pp. 27-34
    • Porzio, M.A.1    Pearson, A.M.2
  • 18
    • 0013937062 scopus 로고
    • N-terminal sequence of actin
    • Alving, R.E. and Laki, K. (1966) N-terminal sequence of actin. Biochemistry 5, 2597-2601
    • (1966) Biochemistry , vol.5 , pp. 2597-2601
    • Alving, R.E.1    Laki, K.2
  • 20
    • 0024352016 scopus 로고
    • Binding manner of actin to the lysine-rich sequence of myosin subfragment 1 in the presence and absence of ATP
    • Yamamoto, K. (1989) Binding manner of actin to the lysine-rich sequence of myosin subfragment 1 in the presence and absence of ATP. Biochemistry 28, 5573-5577
    • (1989) Biochemistry , vol.28 , pp. 5573-5577
    • Yamamoto, K.1
  • 21
    • 0027214208 scopus 로고
    • Localization of two myosin-subfragment-1 binding contacts in the 96-132 region of actin subdomain-1
    • Labbe, J.-P., Boyer, M., Mejean, C., Roustan, C., and Benyamin, Y. (1993) Localization of two myosin-subfragment-1 binding contacts in the 96-132 region of actin subdomain-1. Eur. J. Biochem. 215, 17-24
    • (1993) Eur. J. Biochem. , vol.215 , pp. 17-24
    • Labbe, J.-P.1    Boyer, M.2    Mejean, C.3    Roustan, C.4    Benyamin, Y.5
  • 22
    • 0027522830 scopus 로고
    • Charge-reversion mutagenesis of Dyctyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion
    • Johara, M., Toyoshima, Y.Y., Ishijima, A., Kojima, H., Yanagida, T., and Sutoh, K. (1993) Charge-reversion mutagenesis of Dyctyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion. Proc. Natl. Acad. Sci. USA 90, 2127-2131
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2127-2131
    • Johara, M.1    Toyoshima, Y.Y.2    Ishijima, A.3    Kojima, H.4    Yanagida, T.5    Sutoh, K.6
  • 23
    • 0028906383 scopus 로고
    • Role of charged amino acid pairs in subdomain-1 of actin in interactions with myosin
    • Miller, C.J. and Reisler, E. (1995) Role of charged amino acid pairs in subdomain-1 of actin in interactions with myosin. Biochemistry 34, 2694-2700
    • (1995) Biochemistry , vol.34 , pp. 2694-2700
    • Miller, C.J.1    Reisler, E.2
  • 24
    • 0029781632 scopus 로고    scopus 로고
    • Binding of myosin subfragment 1 to actin
    • Katoh, T. and Morita, F. (1996) Binding of myosin subfragment 1 to actin. J. Biochem. 120, 189-192
    • (1996) J. Biochem. , vol.120 , pp. 189-192
    • Katoh, T.1    Morita, F.2
  • 25
    • 0016696284 scopus 로고
    • The primary structure of actin from rabbit skeletal muscle. Completion and analysis of the amino acid sequence
    • Collins, J.H. and Elzinga, M. (1975) The primary structure of actin from rabbit skeletal muscle. Completion and analysis of the amino acid sequence. J. Biol. Chem. 250, 5915-5920
    • (1975) J. Biol. Chem. , vol.250 , pp. 5915-5920
    • Collins, J.H.1    Elzinga, M.2
  • 26
    • 0017595722 scopus 로고
    • Partial amino acid sequence of brain actin and its homology with muscle actin
    • Lu, R.C. and Elzinga, M. (1977) Partial amino acid sequence of brain actin and its homology with muscle actin. Biochemistry 16, 5801-5806
    • (1977) Biochemistry , vol.16 , pp. 5801-5806
    • Lu, R.C.1    Elzinga, M.2
  • 27
    • 0009780328 scopus 로고
    • Mammalian cytoplasmic actins are the products of at least two genes and differ in primary structure in at least 25 identified positions from skeletal muscle actins
    • Vandekerckhove, J. and Weber, K. (1978) Mammalian cytoplasmic actins are the products of at least two genes and differ in primary structure in at least 25 identified positions from skeletal muscle actins. Proc. Natl. Acad. Sci. USA 75, 1106-1110
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 1106-1110
    • Vandekerckhove, J.1    Weber, K.2
  • 28
    • 0018118577 scopus 로고
    • Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin
    • Vandekerckhove, J. and Weber, K. (1978) Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin. Eur. J. Biochem. 90, 451-462
    • (1978) Eur. J. Biochem. , vol.90 , pp. 451-462
    • Vandekerckhove, J.1    Weber, K.2
  • 29
    • 0018276994 scopus 로고
    • At least six different actins are expressed in a higher mammal: An analysis based on the amino acid sequence of the amino-terminal tryptic peptide
    • Vandekerckhove, J. and Weber, K. (1978) At least six different actins are expressed in a higher mammal: An analysis based on the amino acid sequence of the amino-terminal tryptic peptide. J. Mol. Biol. 126, 783-802
    • (1978) J. Mol. Biol. , vol.126 , pp. 783-802
    • Vandekerckhove, J.1    Weber, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.