메뉴 건너뛰기




Volumn 90, Issue 2, 2007, Pages 449-455

Tropomyosin as a regulator of the sliding movement of actin filaments

Author keywords

Actin filaments; Muscle contraction; Myosin; Sliding movement; Tropomysin; Troponin

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM; MONOMER; MYOSIN; TROPOMYOSIN; TROPONIN;

EID: 34548431322     PISSN: 03032647     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biosystems.2006.11.001     Document Type: Article
Times cited : (6)

References (34)
  • 1
    • 0000547129 scopus 로고
    • Tropomyosin: a new asymmetric protein component of the muscle fibril
    • Bailey K. Tropomyosin: a new asymmetric protein component of the muscle fibril. Biochem. J. 43 (1948) 271-279
    • (1948) Biochem. J. , vol.43 , pp. 271-279
    • Bailey, K.1
  • 3
    • 0015840125 scopus 로고
    • The subunits and biological activity of polymorphic forms of tropomyosin
    • Cummins P., and Perry S.V. The subunits and biological activity of polymorphic forms of tropomyosin. Biochem. J. 133 (1973) 765-777
    • (1973) Biochem. J. , vol.133 , pp. 765-777
    • Cummins, P.1    Perry, S.V.2
  • 5
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon A.M., Homsher E., and Regnier M. Regulation of contraction in striated muscle. Physiol. Rev. 80 (2000) 853-924
    • (2000) Physiol. Rev. , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 6
    • 0036213649 scopus 로고    scopus 로고
    • 2+- and S1-induced conformational changes of reconstituted skeletal muscle thin filaments observed by fluorescence energy transfer spectroscopy: structural evidence for three states of thin filament
    • 2+- and S1-induced conformational changes of reconstituted skeletal muscle thin filaments observed by fluorescence energy transfer spectroscopy: structural evidence for three states of thin filament. J. Biochem. (Tokyo) 131 (2002) 407-418
    • (2002) J. Biochem. (Tokyo) , vol.131 , pp. 407-418
    • Hai, H.1    Sano, K.2    Maeda, K.3    Maeda, Y.4    Miki, M.5
  • 7
    • 0023655442 scopus 로고
    • Altered actin and troponin binding of amino-terminal variants of chicken striated muscle alpha-tropomyosin expressed in Escherichia coli
    • Hitchcock-DeGregori S.E., and Heald R.W. Altered actin and troponin binding of amino-terminal variants of chicken striated muscle alpha-tropomyosin expressed in Escherichia coli. J. Biol. Chem. 262 (1987) 9730-9735
    • (1987) J. Biol. Chem. , vol.262 , pp. 9730-9735
    • Hitchcock-DeGregori, S.E.1    Heald, R.W.2
  • 8
    • 0015527223 scopus 로고
    • Effect of calcium ions on the flexibility of reconstituted thin filament of muscle studied by quasielastic scattering of laser light
    • Ishiwata S., and Fujime S. Effect of calcium ions on the flexibility of reconstituted thin filament of muscle studied by quasielastic scattering of laser light. J. Mol. Biol. 68 (1972) 511-522
    • (1972) J. Mol. Biol. , vol.68 , pp. 511-522
    • Ishiwata, S.1    Fujime, S.2
  • 9
    • 0017379083 scopus 로고
    • Polymerizability of rabbit skeletal tropomyosin: effects of enzymic and chemical modifications
    • Johnson P., and Smillie L.B. Polymerizability of rabbit skeletal tropomyosin: effects of enzymic and chemical modifications. Biochemistry 16 (1977) 2264-2269
    • (1977) Biochemistry , vol.16 , pp. 2264-2269
    • Johnson, P.1    Smillie, L.B.2
  • 10
    • 2442655493 scopus 로고    scopus 로고
    • Stabilizing and destabilizing clusters in the hydrophobic core of long two-stranded alpha-helical coiled-coils
    • Kwok S.C., and Hodges R.S. Stabilizing and destabilizing clusters in the hydrophobic core of long two-stranded alpha-helical coiled-coils. J. Biol. Chem. 279 (2004) 21576-21588
    • (2004) J. Biol. Chem. , vol.279 , pp. 21576-21588
    • Kwok, S.C.1    Hodges, R.S.2
  • 12
    • 0020172195 scopus 로고
    • Distinct alpha-tropomyosin mRNA sequences in chicken skeletal muscle
    • MacLEOD A.R. Distinct alpha-tropomyosin mRNA sequences in chicken skeletal muscle. Eur. J. Biochem. 126 (1982) 293-297
    • (1982) Eur. J. Biochem. , vol.126 , pp. 293-297
    • MacLEOD, A.R.1
  • 13
    • 0019882706 scopus 로고
    • Non-polymerizable tropomyosin: preparation, some properties and F-actin binding
    • Mak A.S., and Smillie L.B. Non-polymerizable tropomyosin: preparation, some properties and F-actin binding. Biochem. Biophys. Res. Commun. 101 (1981) 208-214
    • (1981) Biochem. Biophys. Res. Commun. , vol.101 , pp. 208-214
    • Mak, A.S.1    Smillie, L.B.2
  • 14
    • 0022379564 scopus 로고
    • Purification and characterization of multiple isoforms of tropomyosin from rat cultured cells
    • Matsumura F., and Yamashiro-Matsumura S. Purification and characterization of multiple isoforms of tropomyosin from rat cultured cells. J. Biol. Chem. 260 (1985) 13851-13859
    • (1985) J. Biol. Chem. , vol.260 , pp. 13851-13859
    • Matsumura, F.1    Yamashiro-Matsumura, S.2
  • 15
    • 33645314385 scopus 로고    scopus 로고
    • Troponin is a potential regulator for actomyosin interactions
    • Mizuno H., and Honda H. Troponin is a potential regulator for actomyosin interactions. J. Biochem. 139 (2006) 289-293
    • (2006) J. Biochem. , vol.139 , pp. 289-293
    • Mizuno, H.1    Honda, H.2
  • 16
  • 17
    • 0019023822 scopus 로고
    • Cross-linking study on tropomyosin
    • Ohara O., Takahashi S., and Ooi T. Cross-linking study on tropomyosin. J. Biochem. 87 (1980) 1795-1803
    • (1980) J. Biochem. , vol.87 , pp. 1795-1803
    • Ohara, O.1    Takahashi, S.2    Ooi, T.3
  • 18
    • 0025830291 scopus 로고
    • Kinetics of adenosine triphosphate hydrolysis by shortening myofibrils from rabbit psoas muscle
    • Ohno T., and Kodama T. Kinetics of adenosine triphosphate hydrolysis by shortening myofibrils from rabbit psoas muscle. J. Physiol. 44 (1991) 685-702
    • (1991) J. Physiol. , vol.44 , pp. 685-702
    • Ohno, T.1    Kodama, T.2
  • 19
    • 0022395513 scopus 로고
    • A streamlined method of subfragment one preparation from myosin
    • Okamoto Y., and Sekine T. A streamlined method of subfragment one preparation from myosin. J. Biochem. 98 (1985) 1143-1145
    • (1985) J. Biochem. , vol.98 , pp. 1143-1145
    • Okamoto, Y.1    Sekine, T.2
  • 20
    • 77956984659 scopus 로고
    • Myosin adenosinetriphosphatase
    • Perry S.V. Myosin adenosinetriphosphatase. Methods Enzymol. 2 (1955) 582-588
    • (1955) Methods Enzymol. , vol.2 , pp. 582-588
    • Perry, S.V.1
  • 21
    • 0034841005 scopus 로고    scopus 로고
    • Vertebrate tropomyosin: distribution, properties and function
    • Perry S.V. Vertebrate tropomyosin: distribution, properties and function. J. Muscle Res. Cell Motil. 22 (2001) 5-49
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 5-49
    • Perry, S.V.1
  • 22
    • 0016174778 scopus 로고
    • The content of troponin, tropomyosin, actin, and myosin in rabbit skeletal muscle myofibrils
    • Potter J.D. The content of troponin, tropomyosin, actin, and myosin in rabbit skeletal muscle myofibrils. Arch. Biochem. Biophys. 162 (1974) 436-441
    • (1974) Arch. Biochem. Biophys. , vol.162 , pp. 436-441
    • Potter, J.D.1
  • 23
    • 0025685506 scopus 로고
    • Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility
    • Prochniewicz E., and Yanagida T. Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility. J. Mol. Biol. 216 (1990) 761-772
    • (1990) J. Mol. Biol. , vol.216 , pp. 761-772
    • Prochniewicz, E.1    Yanagida, T.2
  • 24
    • 0035875760 scopus 로고    scopus 로고
    • A highly sensitive method for measurement of myosin ATPase activity by reversed-phase high-performance liquid chromatography
    • Samizo K., Ishikawa R., Nakamura A., and Kohama K. A highly sensitive method for measurement of myosin ATPase activity by reversed-phase high-performance liquid chromatography. Anal. Biochem. 293 (2001) 212-215
    • (2001) Anal. Biochem. , vol.293 , pp. 212-215
    • Samizo, K.1    Ishikawa, R.2    Nakamura, A.3    Kohama, K.4
  • 25
    • 0344198181 scopus 로고    scopus 로고
    • Local destabilization of the tropomyosin coiled coil gibes the molecular flexibility required for actin binding
    • Singh A., and Hitchcock-DeGregori S.E. Local destabilization of the tropomyosin coiled coil gibes the molecular flexibility required for actin binding. Biochemistry 42 (2003) 14114-14121
    • (2003) Biochemistry , vol.42 , pp. 14114-14121
    • Singh, A.1    Hitchcock-DeGregori, S.E.2
  • 26
    • 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. 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 (1971) 4866-4871
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 27
    • 33746374729 scopus 로고    scopus 로고
    • Myofibrillar troponin exists in three states and there is signal transduction along skeletal myofibrillar thin filaments
    • Swartz D.R., Yang Z., Sen A., Tikunova S.B., and Davis J.P. Myofibrillar troponin exists in three states and there is signal transduction along skeletal myofibrillar thin filaments. J. Mol. Biol. 361 (2006) 420-435
    • (2006) J. Mol. Biol. , vol.361 , pp. 420-435
    • Swartz, D.R.1    Yang, Z.2    Sen, A.3    Tikunova, S.B.4    Davis, J.P.5
  • 28
    • 0016768185 scopus 로고
    • Non-polymerizable tropomyosin and control of the superprecipitation of actomyosin
    • Tawada Y., Ohara H., Ooi T., and Tawada K. Non-polymerizable tropomyosin and control of the superprecipitation of actomyosin. J. Biochem. 78 (1975) 65-72
    • (1975) J. Biochem. , vol.78 , pp. 65-72
    • Tawada, Y.1    Ohara, H.2    Ooi, T.3    Tawada, K.4
  • 29
    • 0017084785 scopus 로고
    • Properties of non-polymerizable tropomyosin obtained by carboxypeptidase A digestion
    • Ueno H., Tawada Y., and Ooi T. Properties of non-polymerizable tropomyosin obtained by carboxypeptidase A digestion. J. Biochem. 80 (1976) 283-290
    • (1976) J. Biochem. , vol.80 , pp. 283-290
    • Ueno, H.1    Tawada, Y.2    Ooi, T.3
  • 30
    • 0022429269 scopus 로고
    • Removal of tropomyosin overlap and the co-operative response to increasing calcium concentrations of the acto-subfragment-1 ATPase
    • Walsh T.P., Trueblood C.E., Evans R., and Weber A. Removal of tropomyosin overlap and the co-operative response to increasing calcium concentrations of the acto-subfragment-1 ATPase. J. Mol. Biol. 182 (1985) 265-269
    • (1985) J. Mol. Biol. , vol.182 , pp. 265-269
    • Walsh, T.P.1    Trueblood, C.E.2    Evans, R.3    Weber, A.4
  • 32
    • 0021261156 scopus 로고
    • Direct observation of motion of single F-actin filaments in the presence of myosin
    • Yanagida T., Nakase M., Nishiyama K., and Oosawa F. Direct observation of motion of single F-actin filaments in the presence of myosin. Nature 307 (1984) 58-60
    • (1984) Nature , vol.307 , pp. 58-60
    • Yanagida, T.1    Nakase, M.2    Nishiyama, K.3    Oosawa, F.4
  • 33
    • 0020641706 scopus 로고
    • Troponin subunit stoichiometry and content in rabbit skeletal muscle and myofibrils
    • Yates L.D., and Greaser M.L. Troponin subunit stoichiometry and content in rabbit skeletal muscle and myofibrils. J. Biol. Chem. 258 (1983) 5570-5574
    • (1983) J. Biol. Chem. , vol.258 , pp. 5570-5574
    • Yates, L.D.1    Greaser, M.L.2
  • 34
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • Zot A.S., and Potter J.D. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Annu. Rev. Biophys. Biophys. Chem. 16 (1987) 535-559
    • (1987) Annu. Rev. Biophys. Biophys. Chem. , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.