메뉴 건너뛰기




Volumn 389, Issue 3, 2009, Pages 575-583

Ca2+-Dependent Photocrosslinking of Tropomyosin Residue 146 to Residues 157-163 in the C-Terminal Domain of Troponin I in Reconstituted Skeletal Muscle Thin Filaments

Author keywords

calcium regulation; photocrosslinking; striated muscle; tropomyosin; troponin

Indexed keywords

4 MALEIMIDOBENZOPHENONE; BENZOPHENONE DERIVATIVE; CALCIUM; MALEIMIDE DERIVATIVE; TROPOMYOSIN; TROPONIN I; UNCLASSIFIED DRUG; ACTIN; PEPTIDE;

EID: 65649150702     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.04.027     Document Type: Article
Times cited : (25)

References (32)
  • 1
    • 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
  • 2
    • 0034703378 scopus 로고    scopus 로고
    • Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments
    • Lehman W., Hatch V., Korman V., Rosol M., Thomas L., Maytum R., et al. Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments. J. Mol. Biol. 302 (2000) 593-606
    • (2000) J. Mol. Biol. , vol.302 , pp. 593-606
    • Lehman, W.1    Hatch, V.2    Korman, V.3    Rosol, M.4    Thomas, L.5    Maytum, R.6
  • 3
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament
    • McKillop D.F.A., and Geeves M.A. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys. J. 65 (1993) 693-701
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 4
    • 0036300408 scopus 로고    scopus 로고
    • Troponin-I interacts with the Met47 region of skeletal muscle actin. Implications for the mechanism of thin filament regulation by calcium
    • Luo Y., Leszyk J., Li B., Li Z., Gergely J., and Tao T. Troponin-I interacts with the Met47 region of skeletal muscle actin. Implications for the mechanism of thin filament regulation by calcium. J. Mol. Biol. 316 (2002) 429-434
    • (2002) J. Mol. Biol. , vol.316 , pp. 429-434
    • Luo, Y.1    Leszyk, J.2    Li, B.3    Li, Z.4    Gergely, J.5    Tao, T.6
  • 5
    • 0036359401 scopus 로고    scopus 로고
    • The role of troponin in the Ca(2+)-regulation of skeletal muscle contraction
    • Szczesna D., and Potter J.D. The role of troponin in the Ca(2+)-regulation of skeletal muscle contraction. Results Probl. Cell Differ. 36 (2002) 171-190
    • (2002) Results Probl. Cell Differ. , vol.36 , pp. 171-190
    • Szczesna, D.1    Potter, J.D.2
  • 6
    • 0016213363 scopus 로고
    • Troponin, tropomyosin and actin interactions in the regulation of muscle contraction
    • Potter J.D., and Gergely J. Troponin, tropomyosin and actin interactions in the regulation of muscle contraction. Biochemistry 13 (1974) 2697
    • (1974) Biochemistry , vol.13 , pp. 2697
    • Potter, J.D.1    Gergely, J.2
  • 7
    • 0034622584 scopus 로고    scopus 로고
    • Inhibition of actin-myosin subfragment 1 ATPase activity by troponin I and IC: relationship to the thin filament states of muscle
    • Geeves M.A., Chai M., and Lehrer S.S. Inhibition of actin-myosin subfragment 1 ATPase activity by troponin I and IC: relationship to the thin filament states of muscle. Biochemistry 39 (2000) 9345-9350
    • (2000) Biochemistry , vol.39 , pp. 9345-9350
    • Geeves, M.A.1    Chai, M.2    Lehrer, S.S.3
  • 8
    • 0034620545 scopus 로고    scopus 로고
    • Binding of troponin I and the troponin I-troponin C complex to actin-tropomyosin. Dissociation by myosin subfragment 1
    • Zhou X., Morris E.P., and Lehrer S.S. Binding of troponin I and the troponin I-troponin C complex to actin-tropomyosin. Dissociation by myosin subfragment 1. Biochemistry 39 (2000) 1128-1132
    • (2000) Biochemistry , vol.39 , pp. 1128-1132
    • Zhou, X.1    Morris, E.P.2    Lehrer, S.S.3
  • 9
    • 0037588762 scopus 로고    scopus 로고
    • Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form
    • Takeda S., Yamashita A., Maeda K., and Maeda Y. Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form. Nature 424 (2003) 35-41
    • (2003) Nature , vol.424 , pp. 35-41
    • Takeda, S.1    Yamashita, A.2    Maeda, K.3    Maeda, Y.4
  • 13
    • 84934435729 scopus 로고    scopus 로고
    • Structural basis for calcium-regulated relaxation of striated muscles at interaction sites of troponin with actin and tropomyosin
    • Murakami K., Yumoto F., Ohki S.Y., Yasunaga T., Tanokura M., and Wakabayashi T. Structural basis for calcium-regulated relaxation of striated muscles at interaction sites of troponin with actin and tropomyosin. Adv. Exp. Med. Biol. 592 (2007) 71-86
    • (2007) Adv. Exp. Med. Biol. , vol.592 , pp. 71-86
    • Murakami, K.1    Yumoto, F.2    Ohki, S.Y.3    Yasunaga, T.4    Tanokura, M.5    Wakabayashi, T.6
  • 14
    • 0028177556 scopus 로고
    • Functional alpha-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. Functional alpha-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group. J. Biol. Chem. 269 (1994) 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
  • 15
    • 0023091230 scopus 로고
    • Structure of co-crystals of tropomyosin and troponin
    • White S.P., Cohen C., and Phillips Jr. G.N. Structure of co-crystals of tropomyosin and troponin. Nature 325 (1987) 826-828
    • (1987) Nature , vol.325 , pp. 826-828
    • White, S.P.1    Cohen, C.2    Phillips Jr., G.N.3
  • 16
    • 0017334248 scopus 로고
    • Affinity-chromatographic isolation and some properties of troponin C from different muscle types
    • Head J.F., and Weeks R.A. Affinity-chromatographic isolation and some properties of troponin C from different muscle types. Biochem. J. 16 (1977) 465-471
    • (1977) Biochem. J. , vol.16 , pp. 465-471
    • Head, J.F.1    Weeks, R.A.2
  • 17
    • 0022853074 scopus 로고
    • Site-specific photo-cross-linking studies on interactions between troponin and tropomyosin and between subunits of troponin
    • Tao T., Scheiner C.J., and Lamkin M. Site-specific photo-cross-linking studies on interactions between troponin and tropomyosin and between subunits of troponin. Biochemistry 25 (1986) 7633-7639
    • (1986) Biochemistry , vol.25 , pp. 7633-7639
    • Tao, T.1    Scheiner, C.J.2    Lamkin, M.3
  • 18
    • 0000810370 scopus 로고
    • Localization and mode of action of the inhibitory protein component of the troponin complex
    • Perry S.V., Cole H.A., Head J.F., and Wilson F.J. Localization and mode of action of the inhibitory protein component of the troponin complex. Cold Spring Harbor Symp. Quant. Biol. 37 (1972) 251-262
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.37 , pp. 251-262
    • Perry, S.V.1    Cole, H.A.2    Head, J.F.3    Wilson, F.J.4
  • 19
    • 0016610748 scopus 로고
    • Regulation of muscle contraction: bindings of troponin and its components to actin and tropomyosin
    • Hitchcock S.E. Regulation of muscle contraction: bindings of troponin and its components to actin and tropomyosin. Eur. J. Biochem. 52 (1975) 255-263
    • (1975) Eur. J. Biochem. , vol.52 , pp. 255-263
    • Hitchcock, S.E.1
  • 21
    • 43749096824 scopus 로고    scopus 로고
    • Conserved Asp-137 imparts flexibility to tropomyosin and affects function
    • Sumida J.P., Wu E., and Lehrer S.S. Conserved Asp-137 imparts flexibility to tropomyosin and affects function. J. Biol. Chem. 283 (2008) 6728-6734
    • (2008) J. Biol. Chem. , vol.283 , pp. 6728-6734
    • Sumida, J.P.1    Wu, E.2    Lehrer, S.S.3
  • 22
    • 0023651178 scopus 로고
    • Fluorescence probe studies of the state of tropomyosin in reconstituted muscle thin filaments
    • Ishii Y., and Lehrer S.S. Fluorescence probe studies of the state of tropomyosin in reconstituted muscle thin filaments. Biochemistry 26 (1987) 4922-4925
    • (1987) Biochemistry , vol.26 , pp. 4922-4925
    • Ishii, Y.1    Lehrer, S.S.2
  • 25
    • 0019862956 scopus 로고
    • Structural interpretation of the two-site binding of troponin on the muscle thin filament
    • Mak A.S., and Smillie L.B. Structural interpretation of the two-site binding of troponin on the muscle thin filament. J. Mol. Biol. 149 (1981) 541-550
    • (1981) J. Mol. Biol. , vol.149 , pp. 541-550
    • Mak, A.S.1    Smillie, L.B.2
  • 26
    • 0021251356 scopus 로고
    • Troponin-tropomyosin interactions. Fluorescence studies of the binding of troponin, troponin T, and chymotryptic troponin T fragments to specifically labeled tropomyosin
    • Morris E.P., and Lehrer S.S. Troponin-tropomyosin interactions. Fluorescence studies of the binding of troponin, troponin T, and chymotryptic troponin T fragments to specifically labeled tropomyosin. Biochemistry 23 (1984) 221420
    • (1984) Biochemistry , vol.23 , pp. 221420
    • Morris, E.P.1    Lehrer, S.S.2
  • 27
    • 0015526770 scopus 로고
    • Intrinsic fluorescence of actin
    • Lehrer S.S., and Kerwar G. Intrinsic fluorescence of actin. Biochemistry 11 (1972) 1211-1217
    • (1972) Biochemistry , vol.11 , pp. 1211-1217
    • Lehrer, S.S.1    Kerwar, G.2
  • 28
    • 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., 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.1    Watt, S.2
  • 29
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments
    • Margossian S., and Lowey S. Preparation of myosin and its subfragments. Methods Enzymol. 85 (1982) 55-71
    • (1982) Methods Enzymol. , vol.85 , pp. 55-71
    • Margossian, S.1    Lowey, S.2
  • 30
    • 0018254914 scopus 로고
    • Preparation of myosin and its subfragments
    • Margossian S.S., and Lowey S. Preparation of myosin and its subfragments. Biochemistry 17 (1978) 5431
    • (1978) Biochemistry , vol.17 , pp. 5431
    • Margossian, S.S.1    Lowey, S.2
  • 31
    • 0033462203 scopus 로고    scopus 로고
    • Smooth muscle alpha-tropomyosin crosslinks to caldesmon, to actin and to myosin subfragment 1 on the muscle thin filament
    • Golitsina N.L., and Lehrer S.S. Smooth muscle alpha-tropomyosin crosslinks to caldesmon, to actin and to myosin subfragment 1 on the muscle thin filament. FEBS Lett. 463 (1999) 146-150
    • (1999) FEBS Lett. , vol.463 , pp. 146-150
    • Golitsina, N.L.1    Lehrer, S.S.2
  • 32
    • 0033918391 scopus 로고    scopus 로고
    • Mass spectrometry: a tool for the identification of proteins separated by gels
    • Lahm H.W., and Langen H. Mass spectrometry: a tool for the identification of proteins separated by gels. Electrophoresis 21 (2000) 2105-2114
    • (2000) Electrophoresis , vol.21 , pp. 2105-2114
    • Lahm, H.W.1    Langen, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.