메뉴 건너뛰기




Volumn 250, Issue 2, 1997, Pages 484-491

Interaction of F-actin with synthetic peptides spanning the loop region of human cardiac β-myosin heavy chain containing Arg403

Author keywords

Actomycin interface; Cardiomyopathy; Synthetic myosin Arg403 loop peptide

Indexed keywords

F ACTIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN HEAVY CHAIN; MYOSIN SUBFRAGMENT 1; SYNTHETIC PEPTIDE;

EID: 0031466513     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.0484a.x     Document Type: Article
Times cited : (9)

References (50)
  • 2
    • 0029006373 scopus 로고
    • TEDES rule: A molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head
    • Bement, W. M. & Mooseker, M. S. (1995) TEDES rule: A molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head, Cell Motil. Cytoskeleton 31, 87-92.
    • (1995) Cell Motil. Cytoskeleton , vol.31 , pp. 87-92
    • Bement, W.M.1    Mooseker, M.S.2
  • 3
    • 0029093462 scopus 로고
    • Production and properties of skeletal myosin subfragment 1 selectively labeled with fluorescein at lysine-553 proximal to the strong actin-binding site
    • Bertrand, R., Derancourt, J. & Kassab, R. (1995) Production and properties of skeletal myosin subfragment 1 selectively labeled with fluorescein at lysine-553 proximal to the strong actin-binding site, Biochemistry 34, 9500-9507.
    • (1995) Biochemistry , vol.34 , pp. 9500-9507
    • Bertrand, R.1    Derancourt, J.2    Kassab, R.3
  • 4
    • 0030054719 scopus 로고    scopus 로고
    • Regulation of class I and class II myosins by heavy chain phosphorylation
    • Brzeska, H. & Korn, H. D. (1996) Regulation of class I and class II myosins by heavy chain phosphorylation, J. Biol. Chem. 271, 16983-16986.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16983-16986
    • Brzeska, H.1    Korn, H.D.2
  • 5
    • 2142714206 scopus 로고
    • Peptide antibody specific for the amino terminus of skeletal muscle alpha-actin
    • Bulinski, J. C., Kumar, S., Titani, K. & Hauschka, S. D. (1983) Peptide antibody specific for the amino terminus of skeletal muscle alpha-actin, Proc. Natl Acad. Sci. USA 80, 1506-1510.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 1506-1510
    • Bulinski, J.C.1    Kumar, S.2    Titani, K.3    Hauschka, S.D.4
  • 6
    • 0022588633 scopus 로고
    • Abolition of ATPase activities of skeletal myosin subfragment 1 by a new selective proteolytic cleavage within the 50-kilodalton heavy chain segment
    • Chaussepied, P., Mornet, D., Audemard, E., Derancourt, J. & Kassab, R. (1986) Abolition of ATPase activities of skeletal myosin subfragment 1 by a new selective proteolytic cleavage within the 50-kilodalton heavy chain segment, Biochemistry 25, 1134-1140.
    • (1986) Biochemistry , vol.25 , pp. 1134-1140
    • Chaussepied, P.1    Mornet, D.2    Audemard, E.3    Derancourt, J.4    Kassab, R.5
  • 7
    • 0342293921 scopus 로고
    • Modifying preselected sites on proteins: The stretch of residues 633-642 of the myosin heavy chain is part of the actin-binding site
    • Chaussepied, P. & Morales, M. F. (1988) Modifying preselected sites on proteins: the stretch of residues 633-642 of the myosin heavy chain is part of the actin-binding site, Proc Natl Acad. Sci. USA 85, 7471-7475.
    • (1988) Proc Natl Acad. Sci. USA , vol.85 , pp. 7471-7475
    • Chaussepied, P.1    Morales, M.F.2
  • 8
    • 0030976860 scopus 로고    scopus 로고
    • The in vitro motility activity of β-cardiac myosin depends on the nature of the β-myosin heavy chain gene mutation in hypertrophic cardiomyopathy
    • Cuda, G., Fananapazir, L., Epstein, N. D. & Sellers, J. R. (1997) The in vitro motility activity of β-cardiac myosin depends on the nature of the β-myosin heavy chain gene mutation in hypertrophic cardiomyopathy, J. Muscle Res. Cell Motil. 18, 275-283.
    • (1997) J. Muscle Res. Cell Motil. , vol.18 , pp. 275-283
    • Cuda, G.1    Fananapazir, L.2    Epstein, N.D.3    Sellers, J.R.4
  • 9
    • 0027302431 scopus 로고
    • Skeletal muscle expression and abnormal function of β-myosin in hypertrophic cardiomyopathy
    • Cuda, G., Fananapazir, L., Zhu, W.-S., Sellers, J. R. & Epstein, N. D. (1993) Skeletal muscle expression and abnormal function of β-myosin in hypertrophic cardiomyopathy, J. Clin. Invest. 91, 2861-2865.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2861-2865
    • Cuda, G.1    Fananapazir, L.2    Zhu, W.-S.3    Sellers, J.R.4    Epstein, N.D.5
  • 10
    • 0026593988 scopus 로고
    • Actomyosin interactions in the presence of ATP and the N-terminal segment of actin
    • Das Gupta, G. & Reisler, H. (1992) Actomyosin interactions in the presence of ATP and the N-terminal segment of actin, Biochemistry 32, 1836-1841.
    • (1992) Biochemistry , vol.32 , pp. 1836-1841
    • Das Gupta, G.1    Reisler, H.2
  • 11
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide 1 infrared spectra
    • Dong, A., Huang, P. & Caughey, W. S. (1990) Protein secondary structures in water from second-derivative amide 1 infrared spectra, Biochemistry 29, 3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 12
    • 14444270346 scopus 로고
    • Peptide mimetics to define the structure of the actin-myosin interface
    • Eastwood, A. M. & Trayer, I. P. (1995) Peptide mimetics to define the structure of the actin-myosin interface, J. Muscle Res. Cell. Motil. 16, 146a.
    • (1995) J. Muscle Res. Cell. Motil. , vol.16
    • Eastwood, A.M.1    Trayer, I.P.2
  • 13
    • 0028918608 scopus 로고
    • The cardiac heavy chain Arg-403→Gln mutation that causes hypertrophic cardiomyopathy does not affect the actin- or ATP-binding capacities of two size-limited recombinant myosin heavy chain fragments
    • Eldin, P., Le Cunff, M., Mornet, D., & Leger, J. J. (1995) The cardiac heavy chain Arg-403→Gln mutation that causes hypertrophic cardiomyopathy does not affect the actin-or ATP-binding capacities of two size-limited recombinant myosin heavy chain fragments, Biochem. J. 306, 345-351.
    • (1995) Biochem. J. , vol.306 , pp. 345-351
    • Eldin, P.1    Le Cunff, M.2    Mornet, D.3    Leger, J.J.4
  • 14
    • 0016168984 scopus 로고
    • Troponin-tropomyosin complex. Column chromatographic separation and activity of the three active troponin components with and without tropomyosin present
    • Eisenberg, H. & Kielley, W. W. (1974) Troponin-tropomyosin complex. Column chromatographic separation and activity of the three active troponin components with and without tropomyosin present, J. Biol. Chem. 249, 4742-4748.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4742-4748
    • Eisenberg, H.1    Kielley, W.W.2
  • 15
    • 0026082863 scopus 로고
    • The dynamics of actin and myosin association and the crossbridge model of muscle contraction
    • Geeves, M. A. (1991) The dynamics of actin and myosin association and the crossbridge model of muscle contraction, Biochem. J. 274, 1-14.
    • (1991) Biochem. J. , vol.274 , pp. 1-14
    • Geeves, M.A.1
  • 16
    • 0028915522 scopus 로고
    • The role of three-state docking of myosin S1 with actin in force generation
    • Geeves, M. A. & Conibear, P. B. (1995) The role of three-state docking of myosin S1 with actin in force generation, Biophys. J. 68, 194s-201s.
    • (1995) Biophys. J. , vol.68
    • Geeves, M.A.1    Conibear, P.B.2
  • 17
    • 0025040392 scopus 로고
    • A molecular basis for familial hypertrophic cardiomyopathy: A β cardiac myosin heavy chain missense mutation
    • Geisterfer-Lowrance, A. A., Kass, S., Tanigawa, G., Vosberg, H. P., McKenna, W., Seidman, C. E. & Seidman, J. G. (1990) A molecular basis for familial hypertrophic cardiomyopathy: a β cardiac myosin heavy chain missense mutation, Cell 62, 999-1006.
    • (1990) Cell , vol.62 , pp. 999-1006
    • Geisterfer-Lowrance, A.A.1    Kass, S.2    Tanigawa, G.3    Vosberg, H.P.4    McKenna, W.5    Seidman, C.E.6    Seidman, J.G.7
  • 18
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C. & Von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 19
    • 0026573693 scopus 로고
    • Localization of a vitamin-D-binding protein interaction in the COOH-terminal sequence of actin
    • Houmeida, A., Hanin, V., Constans, J., Benyamin, Y. & Roustan, C. (1992) Localization of a vitamin-D-binding protein interaction in the COOH-terminal sequence of actin, Eur. J. Biochem. 203, 499-503.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 499-503
    • Houmeida, A.1    Hanin, V.2    Constans, J.3    Benyamin, Y.4    Roustan, C.5
  • 20
    • 0028954281 scopus 로고
    • Actomyosin interaction and its control by tropomyosin
    • Holmes, K. C. (1995) Actomyosin interaction and its control by tropomyosin, Biophys. J. 68, 2s-7s.
    • (1995) Biophys. J. , vol.68
    • Holmes, K.C.1
  • 21
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M. & Mantsch, H. H. (1995) The use and misuse of FTIR spectroscopy in the determination of protein structure, Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 23
    • 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
  • 24
    • 0024287405 scopus 로고
    • Cation binding sites on actin: A structural relationship between antigenic epitopes and cation exchange
    • Mejean, C., Hue, H. K., Pons, F., Roustan, C. & Benyamin, Y. (1988) Cation binding sites on actin: a structural relationship between antigenic epitopes and cation exchange, Biochem. Biophys. Res. Commun. 152, 368-375.
    • (1988) Biochem. Biophys. Res. Commun. , vol.152 , pp. 368-375
    • Mejean, C.1    Hue, H.K.2    Pons, F.3    Roustan, C.4    Benyamin, Y.5
  • 25
    • 0026774746 scopus 로고
    • Localization and identification of actin structures involved in the filamin-actin interaction
    • Mejean, C., Lebart, M. C., Boyer, M., Roustan, C. & Benyamin, Y. (1992) Localization and identification of actin structures involved in the filamin-actin interaction, Eur. J. Biochem. 209, 555-562.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 555-562
    • Mejean, C.1    Lebart, M.C.2    Boyer, M.3    Roustan, C.4    Benyamin, Y.5
  • 26
    • 0028906383 scopus 로고
    • Role of charged amino acid pairs in subdomain-1 of aclin in interactions with myosin
    • Miller, C. J. & Reisler, E. (1995) Role of charged amino acid pairs in subdomain-1 of aclin in interactions with myosin, Biochemistry 34, 2694-2700.
    • (1995) Biochemistry , vol.34 , pp. 2694-2700
    • Miller, C.J.1    Reisler, E.2
  • 27
    • 0029972769 scopus 로고    scopus 로고
    • Mutational analysis of the role of hydrophobic residues in the 338-348 helix on actin in actomyosin interactions
    • Miller, C. J., Doyle, T. C., Bobkova, E., Bolstein, D. & Reisler, F. (1996) Mutational analysis of the role of hydrophobic residues in the 338-348 helix on actin in actomyosin interactions, Biochemistry 35, 3670-3676.
    • (1996) Biochemistry , vol.35 , pp. 3670-3676
    • Miller, C.J.1    Doyle, T.C.2    Bobkova, E.3    Bolstein, D.4    Reisler, F.5
  • 29
    • 0028228518 scopus 로고
    • Dynamic properties of actin structural changes induced by beryllium fluoride
    • Muhlrad, A., Cheung, P., Phan, B. C., Miller, C. & Reisler, E. (1994) Dynamic properties of actin structural changes induced by beryllium fluoride, J. Biol. Chem. 269, 11 852-11 858.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11852-11858
    • Muhlrad, A.1    Cheung, P.2    Phan, B.C.3    Miller, C.4    Reisler, E.5
  • 30
    • 0029584033 scopus 로고
    • The putative actin-binding role of hydrophobic residues Trp546 and Phe547 in chiken gizzard heavy meromyosin
    • Onishi, H., Morales, M. F., Katoh, K. & Fujiwara, K. (1995) The putative actin-binding role of hydrophobic residues Trp546 and Phe547 in chiken gizzard heavy meromyosin, Proc. Natl Acad. Sci. USA 92, 11 965-11 969.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11965-11969
    • Onishi, H.1    Morales, M.F.2    Katoh, K.3    Fujiwara, K.4
  • 31
    • 0031556946 scopus 로고    scopus 로고
    • Cooperative rigor binding of myosin to actin is a function of F-actin structure
    • Orlova, A. & Egelman, E. H. (1997) Cooperative rigor binding of myosin to actin is a function of F-actin structure, J. Mol. Biol. 265, 469-474.
    • (1997) J. Mol. Biol. , vol.265 , pp. 469-474
    • Orlova, A.1    Egelman, E.H.2
  • 32
    • 0001228403 scopus 로고
    • The effect of crossbridges on the calcium sensitivity of the structural change of the regulated thin filament
    • Poole, K. J. V., Evans, G., Rosenbaum, G., Lorenz, M. & Holmes, K. C. (1995) The effect of crossbridges on the calcium sensitivity of the structural change of the regulated thin filament, Biophys. J. 68, A365.
    • (1995) Biophys. J. , vol.68
    • Poole, K.J.V.1    Evans, G.2    Rosenbaum, G.3    Lorenz, M.4    Holmes, K.C.5
  • 35
    • 0021995042 scopus 로고
    • Further characterization of the structural and functional properties of the cross-linked complex between F-actin and myosin S-1
    • Rouayrenc, J. F., Bertrand, R., Kassab, R., Walzthony, D., Bahler, M. & Wallimann, T. (1985) Further characterization of the structural and functional properties of the cross-linked complex between F-actin and myosin S-1, Eur. J. Biochem. 146, 391-401.
    • (1985) Eur. J. Biochem. , vol.146 , pp. 391-401
    • Rouayrenc, J.F.1    Bertrand, R.2    Kassab, R.3    Walzthony, D.4    Bahler, M.5    Wallimann, T.6
  • 37
    • 0028075752 scopus 로고
    • How molecular motors work
    • Spudich, J. (1964) How molecular motors work, Nature 372, 515-518.
    • (1964) Nature , vol.372 , pp. 515-518
    • Spudich, J.1
  • 38
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • Surewicz, W. K., Mautsch, H. H. & Chapman, D. (1993) Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment, Biochemistry 32, 389-394.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mautsch, H.H.2    Chapman, D.3
  • 39
    • 0020563473 scopus 로고
    • Mapping of actin-binding sites on the heavy chain of myosin subfragment 1
    • Sutoh, K. (1983) Mapping of actin-binding sites on the heavy chain of myosin subfragment 1, Biochemistry 22, 1579-1585.
    • (1983) Biochemistry , vol.22 , pp. 1579-1585
    • Sutoh, K.1
  • 40
    • 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. & 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
  • 41
    • 0027980111 scopus 로고
    • Heterologous expression of a cardiomyopathic myosin that is defective in its actin interaction
    • Sweeney, H. L., Straceski, A. J., Leinwand, L. A., Tikunov, B. A. & Faust, L. (1994) Heterologous expression of a cardiomyopathic myosin that is defective in its actin interaction, J. Biol. Chem. 269, 1603-1605.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1603-1605
    • Sweeney, H.L.1    Straceski, A.J.2    Leinwand, L.A.3    Tikunov, B.A.4    Faust, L.5
  • 42
    • 0017079984 scopus 로고
    • Defining the 'fast-reacting' thiols of myosin by reaction with 1,5 IAEDANS
    • Takashi, R., Duke, J., Ue, K. & Morales, M. F. (1976) Defining the 'fast-reacting' thiols of myosin by reaction with 1,5 IAEDANS, Arch. Biochem. Biophys. 175, 279-283.
    • (1976) Arch. Biochem. Biophys. , vol.175 , pp. 279-283
    • Takashi, R.1    Duke, J.2    Ue, K.3    Morales, M.F.4
  • 43
    • 0018791940 scopus 로고
    • Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range
    • Thomas, D. D., Seidel, J. C. & Gergely, J. (1979) Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range, J. Mol. Biol. 132, 257-273.
    • (1979) J. Mol. Biol. , vol.132 , pp. 257-273
    • Thomas, D.D.1    Seidel, J.C.2    Gergely, J.3
  • 44
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications, Proc. Natl Acad. Sci. USA 70, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.70 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 45
    • 0029025291 scopus 로고
    • A novel 27/16 kDa form of subtilisin cleaved actin: Structural and functional consequences of cleavage between Ser 234 and Ser 235
    • Vahdat, A., Miller, C., Phillips, M., Muhlrad, A. & Reisler, E. (1995) A novel 27/16 kDa form of subtilisin cleaved actin: structural and functional consequences of cleavage between Ser 234 and Ser 235, FEBS Lett. 365, 149-151.
    • (1995) FEBS Lett. , vol.365 , pp. 149-151
    • Vahdat, A.1    Miller, C.2    Phillips, M.3    Muhlrad, A.4    Reisler, E.5
  • 46
    • 0026639072 scopus 로고
    • Continuous flow synthesis of a biologically active small protein and a large peptide
    • Valembois, C., Mendre, C., Cavadore, J. C. & Calas, B. (1992) Continuous flow synthesis of a biologically active small protein and a large peptide, Tetrahedron Lett. 33, 4005-4008.
    • (1992) Tetrahedron Lett. , vol.33 , pp. 4005-4008
    • Valembois, C.1    Mendre, C.2    Cavadore, J.C.3    Calas, B.4
  • 47
    • 0031566964 scopus 로고    scopus 로고
    • Steric-model for activation of muscle thin filaments
    • Vibert, P., Craig, R. & Lehman, W. (1997) Steric-model for activation of muscle thin filaments, J. Mol. Bipl. 266, 8-14.
    • (1997) J. Mol. Bipl. , vol.266 , pp. 8-14
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 48
    • 0016752124 scopus 로고
    • Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
    • Weeds, A. G. & Taylor, R. S. (1975) Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin, Nature 257, 54-56.
    • (1975) Nature , vol.257 , pp. 54-56
    • Weeds, A.G.1    Taylor, R.S.2
  • 49
    • 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
  • 50
    • 0019751470 scopus 로고
    • 2+-dependent regulatory protein of actin gel-sol transformation, and its intracellular distribution in a variety of cells and tissues
    • 2+-dependent regulatory protein of actin gel-sol transformation, and its intracellular distribution in a variety of cells and tissues, J. Cell. Biol. 91, 901-906.
    • (1981) J. Cell. Biol. , vol.91 , pp. 901-906
    • Yin, H.L.1    Alberecht, J.H.2    Fattoum, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.