메뉴 건너뛰기




Volumn 288, Issue 14, 2013, Pages 9602-9609

A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding interface of actin-tropomyosin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN-BINDING PROTEINS; ATOMIC RESOLUTION STRUCTURES; BINDING INTERFACE; COMPLEX FORMATIONS; COMPUTATIONAL MODELING; FILAMENT STRUCTURE; HYDROPHOBIC INTERACTIONS; PERIODIC PATTERN;

EID: 84875991378     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.451161     Document Type: Article
Times cited : (49)

References (49)
  • 1
    • 38349059960 scopus 로고    scopus 로고
    • Tropomyosin-based regulation of the actin cytoskeleton in time and space
    • Gunning, P., O'Neill, G., and Hardeman, E. (2008) Tropomyosin-based regulation of the actin cytoskeleton in time and space. Physiol. Rev. 88, 1-35
    • (2008) Physiol. Rev. , vol.88 , pp. 1-35
    • Gunning, P.1    O'Neill, G.2    Hardeman, E.3
  • 2
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard, T. D., and Cooper, J. A. (2009) Actin, a central player in cell shape and movement. Science 326, 1208-1212
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 3
    • 77955863118 scopus 로고    scopus 로고
    • New insights into the regulation of the actin cytoskeleton by tropomyosin
    • Wang, C. L., and Coluccio, L. M. (2010) New insights into the regulation of the actin cytoskeleton by tropomyosin. Int. Rev. Cell Mol. Biol. 281, 91-128
    • (2010) Int. Rev. Cell Mol. Biol. , vol.281 , pp. 91-128
    • Wang, C.L.1    Coluccio, L.M.2
  • 4
    • 60849113734 scopus 로고    scopus 로고
    • Tropomyosins in skeletal muscle diseases
    • Kee, A. J., and Hardeman, E. C. (2008) Tropomyosins in skeletal muscle diseases. Adv. Exp. Med. Biol. 644, 143-157
    • (2008) Adv. Exp. Med. Biol. , vol.644 , pp. 143-157
    • Kee, A.J.1    Hardeman, E.C.2
  • 6
    • 0017136639 scopus 로고
    • The 14-fold periodicity in α-tropomyosin and the interaction with actin
    • McLachlan, A. D., and Stewart, M. (1976) The 14-fold periodicity in α-tropomyosin and the interaction with actin. J. Mol. Biol. 103, 271-298
    • (1976) J. Mol. Biol. , vol.103 , pp. 271-298
    • McLachlan, A.D.1    Stewart, M.2
  • 7
    • 0023042854 scopus 로고
    • Construction of an atomic model for tropomyosin and implications for interactions with actin
    • Phillips, G. N., Jr. (1986) Construction of an atomic model for tropomyosin and implications for interactions with actin. J. Mol. Biol. 192, 128-131
    • (1986) J. Mol. Biol. , vol.192 , pp. 128-131
    • Phillips Jr., G.N.1
  • 8
    • 60849123177 scopus 로고    scopus 로고
    • Tropomyosin: Function follows structure
    • Hitchcock-DeGregori, S. E. (2008) Tropomyosin: function follows structure. Adv. Exp. Med. Biol. 644, 60-72
    • (2008) Adv. Exp. Med. Biol. , vol.644 , pp. 60-72
    • Hitchcock-Degregori, S.E.1
  • 9
    • 0344198181 scopus 로고    scopus 로고
    • Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding
    • Singh, A., and Hitchcock-DeGregori, S. E. (2003) Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding. Biochemistry 42, 14114-14121
    • (2003) Biochemistry , vol.42 , pp. 14114-14121
    • Singh, A.1    Hitchcock-Degregori, S.E.2
  • 10
    • 33644795360 scopus 로고    scopus 로고
    • Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin
    • Singh, A., and Hitchcock-DeGregori, S. E. (2006) Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin. Structure 14, 43-50
    • (2006) Structure , vol.14 , pp. 43-50
    • Singh, A.1    Hitchcock-Degregori, S.E.2
  • 11
    • 37349077586 scopus 로고    scopus 로고
    • Tropomyosin's periods are quasi-equivalent for actin binding but have specific regulatory functions
    • Singh, A., and Hitchcock-DeGregori, S. E. (2007) Tropomyosin's periods are quasi-equivalent for actin binding but have specific regulatory functions. Biochemistry 46, 14917-14927
    • (2007) Biochemistry , vol.46 , pp. 14917-14927
    • Singh, A.1    Hitchcock-Degregori, S.E.2
  • 12
    • 0033615687 scopus 로고    scopus 로고
    • Effects of tropomyosin internal deletions on thin filament function
    • Landis, C., Back, N., Homsher, E., and Tobacman, L. S. (1999) Effects of tropomyosin internal deletions on thin filament function. J. Biol. Chem. 274, 31279-31285
    • (1999) J. Biol. Chem. , vol.274 , pp. 31279-31285
    • Landis, C.1    Back, N.2    Homsher, E.3    Tobacman, L.S.4
  • 14
    • 77951977738 scopus 로고    scopus 로고
    • Tropomyosin period 3 is essential for enhancement of isometric tension in thin filament-reconstituted bovine myocardium
    • Kawai, M., Lu, X., Hitchcock-Degregori, S. E., Stanton, K. J., and Wandling, M. W. (2009) Tropomyosin period 3 is essential for enhancement of isometric tension in thin filament-reconstituted bovine myocardium. J. Biophys. 2009, 380967
    • (2009) J. Biophys. , vol.2009 , pp. 380967
    • Kawai, M.1    Lu, X.2    Hitchcock-Degregori, S.E.3    Stanton, K.J.4    Wandling, M.W.5
  • 15
    • 67749145755 scopus 로고    scopus 로고
    • A peek into tropomyosin binding and unfolding on the actin filament
    • Singh, A., and Hitchcock-Degregori, S. E. (2009) A peek into tropomyosin binding and unfolding on the actin filament. PLoS One 4, e6336
    • (2009) PLoS One , vol.4
    • Singh, A.1    Hitchcock-Degregori, S.E.2
  • 17
    • 60849116181 scopus 로고    scopus 로고
    • Tropomyosin and the steric mechanism of muscle regulation
    • Lehman, W., and Craig, R. (2008) Tropomyosin and the steric mechanism of muscle regulation. Adv. Exp. Med. Biol. 644, 95-109
    • (2008) Adv. Exp. Med. Biol. , vol.644 , pp. 95-109
    • Lehman, W.1    Craig, R.2
  • 18
    • 79951834827 scopus 로고    scopus 로고
    • Tropomyosin position on F-actin revealed by em reconstruction and computational chemistry
    • Li, X. E., Tobacman, L. S., Mun, J. Y., Craig, R., Fischer, S., and Lehman, W. (2011) Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry. Biophys. J. 100, 1005-1013
    • (2011) Biophys. J. , vol.100 , pp. 1005-1013
    • Li, X.E.1    Tobacman, L.S.2    Mun, J.Y.3    Craig, R.4    Fischer, S.5    Lehman, W.6
  • 19
    • 82555170220 scopus 로고    scopus 로고
    • A three-dimensional FRET analysis to construct an atomic model of the actin-tropomyosin complex on a reconstituted thin filament
    • Miki, M., Makimura, S., Saitoh, T., Bunya, M., Sugahara, Y., Ueno, Y., Kimura-Sakiyama, C., and Tobita, H. (2011) A three-dimensional FRET analysis to construct an atomic model of the actin-tropomyosin complex on a reconstituted thin filament. J. Mol. Biol. 414, 765-782
    • (2011) J. Mol. Biol. , vol.414 , pp. 765-782
    • Miki, M.1    Makimura, S.2    Saitoh, T.3    Bunya, M.4    Sugahara, Y.5    Ueno, Y.6    Kimura-Sakiyama, C.7    Tobita, H.8
  • 20
    • 79959932890 scopus 로고    scopus 로고
    • Evolutionarily conserved surface residues constitute actin binding sites of tropomyosin
    • Barua, B., Pamula, M. C., and Hitchcock-DeGregori, S. E. (2011) Evolutionarily conserved surface residues constitute actin binding sites of tropomyosin. Proc. Natl. Acad. Sci. U.S.A. 108, 10150-10155
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 10150-10155
    • Barua, B.1    Pamula, M.C.2    Hitchcock-Degregori, S.E.3
  • 23
    • 0028177556 scopus 로고
    • Functional α-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group
    • Monteiro, P. B., Lataro, R. C., Ferro, J. A., and Reinach Fde, C. (1994) Functional α-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group. J. Biol. Chem. 269, 10461-10466
    • (1994) J. Biol. Chem. , vol.269 , pp. 10461-10466
    • Monteiro, P.B.1    Lataro, R.C.2    Ferro, J.A.3    Reinach Fde, C.4
  • 24
    • 0020479817 scopus 로고
    • Changes in actin lysine reactivities during polymerization detected using a competitive labeling method
    • Hitchcock-De Gregori, S. E., Mandala, S., and Sachs, G. A. (1982) Changes in actin lysine reactivities during polymerization detected using a competitive labeling method. J. Biol. Chem. 257, 12573-12580
    • (1982) J. Biol. Chem. , vol.257 , pp. 12573-12580
    • Hitchcock-De Gregori, S.E.1    Mandala, S.2    Sachs, G.A.3
  • 26
    • 77951170096 scopus 로고    scopus 로고
    • Dominant negative mutant actins identified in flightless Drosophila can be classified into three classes
    • Noguchi, T. Q., Gomibuchi, Y., Murakami, K., Ueno, H., Hirose, K., Wakabayashi, T., and Uyeda, T. Q. (2010) Dominant negative mutant actins identified in flightless Drosophila can be classified into three classes. J. Biol. Chem. 285, 4337-4347
    • (2010) J. Biol. Chem. , vol.285 , pp. 4337-4347
    • Noguchi, T.Q.1    Gomibuchi, Y.2    Murakami, K.3    Ueno, H.4    Hirose, K.5    Wakabayashi, T.6    Uyeda, T.Q.7
  • 27
    • 0030067632 scopus 로고    scopus 로고
    • Mapping the functional domains within the carboxyl terminus of α-tropomyosin encoded by the alternatively spliced ninth exon
    • Hammell, R. L., and Hitchcock-DeGregori, S. E. (1996) Mapping the functional domains within the carboxyl terminus of α-tropomyosin encoded by the alternatively spliced ninth exon. J. Biol. Chem. 271, 4236-4242
    • (1996) J. Biol. Chem. , vol.271 , pp. 4236-4242
    • Hammell, R.L.1    Hitchcock-Degregori, S.E.2
  • 28
    • 0029591294 scopus 로고
    • The stability of tropomyosin, a two-stranded coiled-coil protein, is primarily a function of the hydrophobicity of residues at the helix-helix interface
    • Greenfield, N. J., and Hitchcock-DeGregori, S. E. (1995) The stability of tropomyosin, a two-stranded coiled-coil protein, is primarily a function of the hydrophobicity of residues at the helix-helix interface. Biochemistry 34, 16797-16805
    • (1995) Biochemistry , vol.34 , pp. 16797-16805
    • Greenfield, N.J.1    Hitchcock-Degregori, S.E.2
  • 29
    • 0029027492 scopus 로고
    • Flexibility of myosin attachment to surfaces influences F-actin motion
    • Winkelmann, D. A., Bourdieu, L., Ott, A., Kinose, F., and Libchaber, A. (1995) Flexibility of myosin attachment to surfaces influences F-actin motion. Biophys. J. 68, 2444-2453
    • (1995) Biophys. J. , vol.68 , pp. 2444-2453
    • Winkelmann, D.A.1    Bourdieu, L.2    Ott, A.3    Kinose, F.4    Libchaber, A.5
  • 31
    • 0242319629 scopus 로고    scopus 로고
    • Mutations in the motor domain modulate myosin activity and myofibril organization
    • Wang, Q., Moncman, C. L., and Winkelmann, D. A. (2003) Mutations in the motor domain modulate myosin activity and myofibril organization. J. Cell Sci. 116, 4227-4238
    • (2003) J. Cell Sci. , vol.116 , pp. 4227-4238
    • Wang, Q.1    Moncman, C.L.2    Winkelmann, D.A.3
  • 32
    • 0346872983 scopus 로고    scopus 로고
    • Effects of tropomyosin internal deletion Δ23Tm on isometric tension and the cross-bridge kinetics in bovine myocardium
    • Lu, X., Tobacman, L. S., and Kawai, M. (2003) Effects of tropomyosin internal deletion Δ23Tm on isometric tension and the cross-bridge kinetics in bovine myocardium. J. Physiol. 553, 457-471
    • (2003) J. Physiol. , vol.553 , pp. 457-471
    • Lu, X.1    Tobacman, L.S.2    Kawai, M.3
  • 33
    • 33845363591 scopus 로고    scopus 로고
    • Temperature-dependence of isometric tension and cross-bridge kinetics of cardiac muscle fibers reconstituted with a tropomyosin internal deletion mutant
    • Lu, X., Tobacman, L. S., and Kawai, M. (2006) Temperature-dependence of isometric tension and cross-bridge kinetics of cardiac muscle fibers reconstituted with a tropomyosin internal deletion mutant. Biophys. J. 91, 4230-4240
    • (2006) Biophys. J. , vol.91 , pp. 4230-4240
    • Lu, X.1    Tobacman, L.S.2    Kawai, M.3
  • 36
    • 43749096824 scopus 로고    scopus 로고
    • Conserved Asp-137 imparts flexibility to tropomyosin and affects function
    • Sumida, J. P., Wu, E., and Lehrer, S. S. (2008) Conserved Asp-137 imparts flexibility to tropomyosin and affects function. J. Biol. Chem. 283, 6728-6734
    • (2008) J. Biol. Chem. , vol.283 , pp. 6728-6734
    • Sumida, J.P.1    Wu, E.2    Lehrer, S.S.3
  • 38
    • 0000733783 scopus 로고
    • X-ray evidence for a conformational change in the actin-containing filaments of vertebrate striated muscle
    • Spring Harbor Symp. Quant. Biol
    • Haselgrove, J. C. (1972) X-ray evidence for a conformational change in the actin-containing filaments of vertebrate striated muscle. Cold Spring Harbor Symp. Quant. Biol. 37, 341-352
    • (1972) Cold , vol.37 , pp. 341-352
    • Haselgrove, J.C.1
  • 39
    • 0000244537 scopus 로고
    • Structural changes in actin and myosin-containing filaments during contraction
    • Spring Harbor Symp. Quant. Biol
    • Huxley, H. E. (1972) Structural changes in actin and myosin-containing filaments during contraction. Cold Spring Harbor Symp. Quant. Biol. 37, 361-376
    • (1972) Cold , vol.37 , pp. 361-376
    • Huxley, H.E.1
  • 40
    • 0015935349 scopus 로고
    • Structural role of tropomyosin in muscle regulation: Analysis of the x-ray diffraction patterns from relaxed and contracting muscles
    • Parry, D. A., and Squire, J. M. (1973) Structural role of tropomyosin in muscle regulation: analysis of the x-ray diffraction patterns from relaxed and contracting muscles. J. Mol. Biol. 75, 33-55
    • (1973) J. Mol. Biol. , vol.75 , pp. 33-55
    • Parry, D.A.1    Squire, J.M.2
  • 41
    • 0031566964 scopus 로고    scopus 로고
    • Steric-model for activation of muscle thin filaments
    • Vibert, P., Craig, R., and Lehman, W. (1997) Steric-model for activation of muscle thin filaments. J. Mol. Biol. 266, 8-14
    • (1997) J. Mol. Biol. , vol.266 , pp. 8-14
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 43
    • 0025794119 scopus 로고
    • Characterisation of missense mutations in the Act88F gene of Drosophila melanogaster
    • Drummond, D. R., Hennessey, E. S., and Sparrow, J. C. (1991) Characterisation of missense mutations in the Act88F gene of Drosophila melanogaster. Mol. Gen. Genet. 226, 70-80
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 70-80
    • Drummond, D.R.1    Hennessey, E.S.2    Sparrow, J.C.3
  • 44
    • 0034630737 scopus 로고    scopus 로고
    • Purification and polymerization properties of two lethal yeast actin mutants
    • Frieden, C., Du, J., Schriefer, L., and Buzan, J. (2000) Purification and polymerization properties of two lethal yeast actin mutants. Biochem. Biophys. Res. Commun. 271, 464-468
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 464-468
    • Frieden, C.1    Du, J.2    Schriefer, L.3    Buzan, J.4
  • 45
    • 0021724834 scopus 로고
    • Dominant mutations affecting muscle structure in Caenorhabditis elegans that map near the actin gene cluster
    • Waterston, R. H., Hirsh, D., and Lane, T. R. (1984) Dominant mutations affecting muscle structure in Caenorhabditis elegans that map near the actin gene cluster. J. Mol. Biol. 180, 473-496
    • (1984) J. Mol. Biol. , vol.180 , pp. 473-496
    • Waterston, R.H.1    Hirsh, D.2    Lane, T.R.3
  • 46
    • 0026737363 scopus 로고
    • Systematic mutational analysis of the yeast ACT1 gene
    • Wertman, K. F., Drubin, D. G., and Botstein, D. (1992) Systematic mutational analysis of the yeast ACT1 gene. Genetics 132, 337-350
    • (1992) Genetics , vol.132 , pp. 337-350
    • Wertman, K.F.1    Drubin, D.G.2    Botstein, D.3
  • 47
    • 77957996302 scopus 로고    scopus 로고
    • Direct visualization of secondary structures of F-actin by electron cryomicroscopy
    • Fujii, T., Iwane, A. H., Yanagida, T., and Namba, K. (2010) Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature 467, 724-728
    • (2010) Nature , vol.467 , pp. 724-728
    • Fujii, T.1    Iwane, A.H.2    Yanagida, T.3    Namba, K.4
  • 49
    • 0033985268 scopus 로고    scopus 로고
    • Crystal structure of tropomyosin at 7 Angstroms resolution
    • Whitby, F. G., and Phillips, G. N., Jr. (2000) Crystal structure of tropomyosin at 7 Angstroms resolution. Proteins 38, 49-59
    • (2000) Proteins , vol.38 , pp. 49-59
    • Whitby, F.G.1    Phillips Jr., G.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.