메뉴 건너뛰기




Volumn 83, Issue 5, 2002, Pages 2726-2732

Thin filament regulation and ionic interactions between the N-terminal region in actin and troponin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE; ASPARTIC ACID; CALCIUM ION; GLUTAMIC ACID; MUTANT PROTEIN; MYOSIN; TROPOMYOSIN; TROPONIN; ALANINE; CALCIUM; FLUORESCENT DYE; ION; PYRENE DERIVATIVE;

EID: 0036840324     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(02)75282-X     Document Type: Article
Times cited : (6)

References (47)
  • 1
    • 0032511083 scopus 로고    scopus 로고
    • Tropomyosin and troponin regulation of wild type and E93K mutant actin filaments from Drosophila flight muscle. Charge reversal on actin changes actintropomyosin from on to off state
    • Bing, W., A. Razzaq, J. Sparrow, and S. Marston. 1998. Tropomyosin and troponin regulation of wild type and E93K mutant actin filaments from Drosophila flight muscle. Charge reversal on actin changes actintropomyosin from on to off state. J. Biol. Chem. 273:15016-15021.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15016-15021
    • Bing, W.1    Razzaq, A.2    Sparrow, J.3    Marston, S.4
  • 2
    • 0029018214 scopus 로고
    • The effect of the S14A mutation on the conformation and thermostability of S. cerevisiae G-actin and its interaction with adenine nucleotides
    • Chen, X., J. Peng, M. Pedram, C. A. Swenson, and P. A. Rubenstein. 1995. The effect of the S14A mutation on the conformation and thermostability of S. cerevisiae G-actin and its interaction with adenine nucleotides. J. Biol. Chem. 270:11415-11423.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11415-11423
    • Chen, X.1    Peng, J.2    Pedram, M.3    Swenson, C.A.4    Rubenstein, P.A.5
  • 3
    • 0026794025 scopus 로고
    • Removal of the amino-terminal acidic residues of yeast actin. Studies in vitro and in vivo
    • Cook, R. K., W. Blake, and P. A. Rubenstein. 1992. Removal of the amino-terminal acidic residues of yeast actin. Studies in vitro and in vivo. J. Biol. Chem. 267:9430-9436.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9430-9436
    • Cook, R.K.1    Blake, W.2    Rubenstein, P.A.3
  • 5
    • 0036371383 scopus 로고    scopus 로고
    • Insights into actomyosin interactions from actin mutations
    • D.D. Thomas and C.G. DosRemidios, Editors. Springer-Verlag, Berlin, Heidelberg
    • Doyle, T. C., and E. Reisler. 2002. Insights into actomyosin interactions from actin mutations. In Molecular Interactions of Actin, Results and Problems in Cell Differentiation. Vol. 36. D.D. Thomas and C.G. DosRemidios, Editors. Springer-Verlag, Berlin, Heidelberg.
    • (2002) Molecular Interactions of Actin, Results and Problems in Cell Differentiation , vol.36
    • Doyle, T.C.1    Reisler, E.2
  • 7
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah, C. S., and F. C. Reinach. 1995. The troponin complex and regulation of muscle contraction. FASEB J. 9:755-767.
    • (1995) FASEB J. , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinach, F.C.2
  • 8
    • 0028340236 scopus 로고
    • Dynamics of the muscle thin filament regulatory switch: The size of the cooperative unit
    • Geeves, M. A., and S. S. Lehrer. 1994. Dynamics of the muscle thin filament regulatory switch: The size of the cooperative unit. Biophys. J. 67:273-282.
    • (1994) Biophys. J. , vol.67 , pp. 273-282
    • Geeves, M.A.1    Lehrer, S.S.2
  • 9
    • 0034622584 scopus 로고    scopus 로고
    • Kinetic analyses of a truncated mammalian myosin I suggest a novel isomerization event preceding nucleotide binding
    • Geeves, M. A., M. Chai, and S. S. Lehrer. 2000. Kinetic analyses of a truncated mammalian myosin I suggest a novel isomerization event preceding nucleotide binding. J. Biol. Chem. 39:9345-9350.
    • (2000) J. Biol. Chem. , vol.39 , pp. 9345-9350
    • Geeves, M.A.1    Chai, M.2    Lehrer, S.S.3
  • 11
    • 0033581012 scopus 로고    scopus 로고
    • Role of residues 311/312 in actin-tropomyosin interaction. In vitro motility study using yeast actin mutant E311A/R312A
    • Gerson, J. H., E. Bobkova, E. Homsher, and E. Reisler. 1999. Role of residues 311/312 in actin-tropomyosin interaction. In vitro motility study using yeast actin mutant E311A/R312A. J. Biol. Chem. 274:17545-17550.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17545-17550
    • Gerson, J.H.1    Bobkova, E.2    Homsher, E.3    Reisler, E.4
  • 12
    • 0014952464 scopus 로고
    • Self-association in the myosin system at high ionic strength. I. Sensitivity of the interaction to pH and ionic environment
    • Godfrey, J. E., and W. F. Harrington. 1970. Self-association in the myosin system at high ionic strength. I. Sensitivity of the interaction to pH and ionic environment. Biochemistry. 9:886-895.
    • (1970) Biochemistry , vol.9 , pp. 886-895
    • Godfrey, J.E.1    Harrington, W.F.2
  • 13
    • 0034701014 scopus 로고    scopus 로고
    • Structural transition at actin's N-terminus in the actomyosin cross-bridge cycle
    • Hansen, J. E., J. Marner, D. Pavlov, P. A. Rubenstein, and E. Reisler. 2000. Structural transition at actin's N-terminus in the actomyosin cross-bridge cycle. Biochemistry. 39:1792-1799.
    • (2000) Biochemistry , vol.39 , pp. 1792-1799
    • Hansen, J.E.1    Marner, J.2    Pavlov, D.3    Rubenstein, P.A.4    Reisler, E.5
  • 14
    • 0029924132 scopus 로고    scopus 로고
    • Calcium regulation of thin filament movement in an in vitro motility assay
    • Homsher, E., B. Kim, A. Bokkova, and L. S. Tobacman. 1996. Calcium regulation of thin filament movement in an in vitro motility assay. Biophys. J. 70:1881-1892.
    • (1996) Biophys. J. , vol.70 , pp. 1881-1892
    • Homsher, E.1    Kim, B.2    Bokkova, A.3    Tobacman, L.S.4
  • 15
    • 0034177712 scopus 로고    scopus 로고
    • Regulation of force and unloaded sliding speed in single thin filaments: Effects of regulatory proteins and calcium
    • Homsher, E., D. M. Lee, C. Morris, D. Pavlov, and L. S. Tobacman. 2000. Regulation of force and unloaded sliding speed in single thin filaments: Effects of regulatory proteins and calcium. J. Physiol. 524:233-243.
    • (2000) J. Physiol. , vol.524 , pp. 233-243
    • Homsher, E.1    Lee, D.M.2    Morris, C.3    Pavlov, D.4    Tobacman, L.S.5
  • 16
    • 0026522849 scopus 로고
    • Factors affecting movement of F-actin filaments propelled by skeletal muscle heavy meromyosin
    • Homsher, E., F. Wang, and J. Sellers. 1992. Factors affecting movement of F-actin filaments propelled by skeletal muscle heavy meromyosin. Am. J. Physiol. Cell Physiol. 262:C714-C723.
    • (1992) Am. J. Physiol. Cell Physiol. , vol.262
    • Homsher, E.1    Wang, F.2    Sellers, J.3
  • 18
    • 0030450050 scopus 로고    scopus 로고
    • Polymerization and in vitro motility properties of yeast actin: A comparison with rabbit skeletal α-actin
    • Kim, E., C. J. Miller, and E. Reisler. 1996. Polymerization and in vitro motility properties of yeast actin: A comparison with rabbit skeletal α-actin. Biochemistry. 35:16566-16572.
    • (1996) Biochemistry , vol.35 , pp. 16566-16572
    • Kim, E.1    Miller, C.J.2    Reisler, E.3
  • 19
    • 0033529663 scopus 로고    scopus 로고
    • Mutations in actin subdomain 3 that impair thin filament regulation by troponin and tropomyosin
    • Korman, V. L., and L. S. Tobacman. 1999. Mutations in actin subdomain 3 that impair thin filament regulation by troponin and tropomyosin. J. Biol. Chem. 274:22191-22196.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22191-22196
    • Korman, V.L.1    Tobacman, L.S.2
  • 20
    • 0034698021 scopus 로고    scopus 로고
    • An actin subdomain 2 mutation that impairs thin filament regulation by troponin and tropomyosin
    • Korman, V. L., V. Hatch, K. Y. Dixon, R. Craig, W. Lehman, and L. S. Tobacman. 2000. An actin subdomain 2 mutation that impairs thin filament regulation by troponin and tropomyosin. J. Biol. Chem. 275:22470-22478.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22470-22478
    • Korman, V.L.1    Hatch, V.2    Dixon, K.Y.3    Craig, R.4    Lehman, W.5    Tobacman, L.S.6
  • 21
    • 0025782977 scopus 로고
    • Assays for actin sliding movement over myosin-coated surfaces
    • Kron, S., Y. Toyoshima, T. Uyeda, and J. Spudich. 1991. Assays for actin sliding movement over myosin-coated surfaces. Methods Enzymol. 197:403-414.
    • (1991) Methods Enzymol. , vol.197 , pp. 403-414
    • Kron, S.1    Toyoshima, Y.2    Uyeda, T.3    Spudich, J.4
  • 22
    • 0021151109 scopus 로고
    • Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction
    • Leavis, P. C., and J. Gergely. 1984. Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction. CRC Crit. Rev. Biochem. 16:235-305.
    • (1984) CRC Crit. Rev. Biochem. , vol.16 , pp. 235-305
    • Leavis, P.C.1    Gergely, J.2
  • 23
    • 0028179144 scopus 로고
    • 2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction
    • 2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature. 368:65-67.
    • (1994) Nature , vol.368 , pp. 65-67
    • Lehman, W.1    Craig, R.2    Vibert, P.3
  • 24
    • 0035970288 scopus 로고    scopus 로고
    • Troponin organization on relaxed and activated thin filaments revealed by electron microscopy and three-dimensional reconstruction
    • Lehman, W., M. Rosol, L. S. Tobacman, and R. Craig. 2001. Troponin organization on relaxed and activated thin filaments revealed by electron microscopy and three-dimensional reconstruction. J. Mol. Biol. 307:739-744.
    • (2001) J. Mol. Biol. , vol.307 , pp. 739-744
    • Lehman, W.1    Rosol, M.2    Tobacman, L.S.3    Craig, R.4
  • 25
    • 0032540229 scopus 로고    scopus 로고
    • The muscle thin filament as a classical cooperative/allosteric regulatory system
    • Lehrer, S. S., and M. A. Geeves. 1998. The muscle thin filament as a classical cooperative/allosteric regulatory system. J. Mol. Biol. 277:1081-1089.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1081-1089
    • Lehrer, S.S.1    Geeves, M.A.2
  • 26
    • 0023970297 scopus 로고
    • The interaction of troponin-I with the N-terminal region of actin
    • Levine, B. A., A. J. G. Moir, and S. V. Perry. 1988. The interaction of troponin-I with the N-terminal region of actin. Eur. J. Biochem. 172:389-397.
    • (1988) Eur. J. Biochem. , vol.172 , pp. 389-397
    • Levine, B.A.1    Moir, A.J.G.2    Perry, S.V.3
  • 27
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop, D. F., and M. A. Geeves. 1993. Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament. Biophys. J. 65:693-701.
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 28
    • 0028906383 scopus 로고
    • Role of charged amino acid pairs in subdomain-1 of actin in interactions with myosin
    • Miller, C. J., and E. Reisler. 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
  • 29
    • 0030449743 scopus 로고    scopus 로고
    • Mutational analysis of the role of the N-terminus of actin in actomyosin interactions. Comparison with other mutant actins and implications for the cross-bridge cycle
    • Miller, C. J., W. W. Wong, E. Bobkova, P. A. Rubenstein, and E. Reisler. 1996. Mutational analysis of the role of the N-terminus of actin in actomyosin interactions. Comparison with other mutant actins and implications for the cross-bridge cycle. Biochemistry. 35:16557-16565.
    • (1996) Biochemistry , vol.35 , pp. 16557-16565
    • Miller, C.J.1    Wong, W.W.2    Bobkova, E.3    Rubenstein, P.A.4    Reisler, E.5
  • 30
    • 0035827552 scopus 로고    scopus 로고
    • Modulation of contractile activation in skeletal muscle by a calcium-insensitive troponin C mutant
    • Morris, C. A., L. S. Tobacman, and E. Homsher. 2001. Modulation of contractile activation in skeletal muscle by a calcium-insensitive troponin C mutant. J. Biol. Chem. 276:20245-20251.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20245-20251
    • Morris, C.A.1    Tobacman, L.S.2    Homsher, E.3
  • 32
    • 0009353304 scopus 로고
    • Isolation and sequence of the gene for actin in S. cerevisiae
    • Ng, R., and J. Abelson. 1980. Isolation and sequence of the gene for actin in S. cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 77:3912-3916,
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 3912-3916
    • Ng, R.1    Abelson, J.2
  • 33
    • 0033044797 scopus 로고    scopus 로고
    • Troponin I: Inhibitor or facilitator
    • Perry, S. V. 1999. Troponin I: Inhibitor or facilitator. Mol. Cell. Biochem. 190:9-32.
    • (1999) Mol. Cell. Biochem. , vol.190 , pp. 9-32
    • Perry, S.V.1
  • 34
    • 0016213363 scopus 로고
    • 2+ regulation of muscle contraction
    • 2+ regulation of muscle contraction. Biochemistry. 13:2697-2703.
    • (1974) Biochemistry , vol.13 , pp. 2697-2703
    • Potter, J.D.1    Gergely, J.2
  • 35
    • 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 W. Watt. 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, W.2
  • 36
    • 0031777885 scopus 로고    scopus 로고
    • A new look at thin filament regulation in vertebrate skeletal muscle
    • Squire, J. M., and E. P. Morris. 1998. A new look at thin filament regulation in vertebrate skeletal muscle. FASEB J. 12:761-771.
    • (1998) FASEB J. , vol.12 , pp. 761-771
    • Squire, J.M.1    Morris, E.P.2
  • 37
    • 0019474543 scopus 로고
    • Synthetic studies on the inhibitory region of rabbit skeletal troponin I. Relationship of amino acid sequence to biological activity
    • Talbot, J. A., and R. S. Hodges. 1981. Synthetic studies on the inhibitory region of rabbit skeletal troponin I. Relationship of amino acid sequence to biological activity. J. Biol. Chem. 254:2798-2802.
    • (1981) J. Biol. Chem. , vol.254 , pp. 2798-2802
    • Talbot, J.A.1    Hodges, R.S.2
  • 38
    • 0025356099 scopus 로고
    • Calcium-induced movement of troponin-I relative to actin in skeletal muscle thin filaments
    • Tao, T., B.-J. Gong, and P. C. Leavis. 1990. Calcium-induced movement of troponin-I relative to actin in skeletal muscle thin filaments. Science. 247:1339-1341.
    • (1990) Science , vol.247 , pp. 1339-1341
    • Tao, T.1    Gong, B.-J.2    Leavis, P.C.3
  • 39
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • Tobacman, L. S. 1996. Thin filament-mediated regulation of cardiac contraction. Annu. Rev. Physiol. 58:447-481.
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 41
    • 0023930339 scopus 로고
    • The biological importance of each amino acid residue of the troponin I inhibitory sequence 104-115 in the interaction with troponin C and tropomyosin-actin
    • Van Eyk, J. E., and R. S. Hodges. 1988. The biological importance of each amino acid residue of the troponin I inhibitory sequence 104-115 in the interaction with troponin C and tropomyosin-actin. J. Biol. Chem. 263:1726-1732.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1726-1732
    • Van Eyk, J.E.1    Hodges, R.S.2
  • 42
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility
    • Weeds, A., and A. B. Pope. 1977. Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111:129-157.
    • (1977) J. Mol. Biol. , vol.111 , pp. 129-157
    • Weeds, A.1    Pope, A.B.2
  • 43
    • 0026737363 scopus 로고
    • Systematic mutational analysis of the yeast ACTI gene
    • Wertman, K. F., D. G. Drubin, and D. Botstein. 1992. Systematic mutational analysis of the yeast ACTI gene. Genetics. 132:337-350.
    • (1992) Genetics , vol.132 , pp. 337-350
    • Wertman, K.F.1    Drubin, D.G.2    Botstein, D.3
  • 44
    • 0033604852 scopus 로고    scopus 로고
    • Nonspecific weak actomyosin interactions: Relocation of charged residues in subdomain I of actin does not alter actomyosin function
    • Wong, W. W., T. C. Doyle, and E. Reisler. 1999. Nonspecific weak actomyosin interactions: Relocation of charged residues in subdomain I of actin does not alter actomyosin function. Biochemistry. 38:1365-1370.
    • (1999) Biochemistry , vol.38 , pp. 1365-1370
    • Wong, W.W.1    Doyle, T.C.2    Reisler, E.3
  • 45
    • 0035816548 scopus 로고    scopus 로고
    • F-actin-like ATPase activity in a polymerization-defective mutant yeast actin (V266G/L267G)
    • Yao, X., and P. A. Rubenstein. 2001. F-actin-like ATPase activity in a polymerization-defective mutant yeast actin (V266G/L267G). J. Biol. Chem. 276:25598-25604.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25598-25604
    • Yao, X.1    Rubenstein, P.A.2
  • 46
    • 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., E. P. Morris, and S. S. Lehrer. 2000. Binding of troponin I and the troponin I-troponin C complex to actin-tropomyosin. Dissociation by myosin subfragment 1. Biochemistry. 39:1128-1132.
    • (2000) Biochemistry , vol.39 , pp. 1128-1132
    • Zhou, X.1    Morris, E.P.2    Lehrer, S.S.3
  • 47
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • Zot, A. S., and J. D. Potter. 1987. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Annu. Rev. Biophys. Chem. 16:535-559.
    • (1987) Annu. Rev. Biophys. Chem. , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.