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Volumn 86, Issue 2-3, 2000, Pages 191-201

Intermolecular dynamics and function in actin filaments

Author keywords

Actin filaments; Cross linking; Excimer fluorescence; Intermolecular dynamics; Intermolecular interface; Pyrene fluorescence

Indexed keywords

F ACTIN; PYRENE; SUBTILISIN;

EID: 0034734274     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(00)00143-5     Document Type: Conference Paper
Times cited : (24)

References (34)
  • 2
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz M., Popp D., Holmes K.C. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:1993;826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 4
    • 0008711922 scopus 로고
    • Axial period of actin filaments
    • Hanson J. Axial period of actin filaments. Nature. 213:1967;353-356.
    • (1967) Nature , vol.213 , pp. 353-356
    • Hanson, J.1
  • 5
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • McGough A., Pope B., Chiu W., Weeds A. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138:1997;771-781.
    • (1997) J. Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 6
    • 0026437417 scopus 로고
    • Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysis
    • Orlova A., Egelman E.H. Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysis. J. Mol. Biol. 227:1992;1043-1053.
    • (1992) J. Mol. Biol. , vol.227 , pp. 1043-1053
    • Orlova, A.1    Egelman, E.H.2
  • 7
    • 0027328612 scopus 로고
    • A conformational change in the actin subunit can change the flexibility of the actin filament
    • Orlova A., Egelman E.H. A conformational change in the actin subunit can change the flexibility of the actin filament. J. Mol. Biol. 232:1993;334-341.
    • (1993) J. Mol. Biol. , vol.232 , pp. 334-341
    • Orlova, A.1    Egelman, E.H.2
  • 8
    • 0028907435 scopus 로고
    • Structural dynamics of F-actin.1. Changes in the C-terminus
    • Orlova A., Egelman E.H. Structural dynamics of F-actin.1. Changes in the C-terminus. J. Mol. Biol. 245:1995;582-597.
    • (1995) J. Mol. Biol. , vol.245 , pp. 582-597
    • Orlova, A.1    Egelman, E.H.2
  • 9
    • 0025359118 scopus 로고
    • Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin
    • Schwyter D.H., Kron S.J., Toyoshima Y.Y., Spudich J.A., Reisler E. Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin. J. Cell Biol. 111:1990;465-470.
    • (1990) J. Cell Biol. , vol.111 , pp. 465-470
    • Schwyter, D.H.1    Kron, S.J.2    Toyoshima, Y.Y.3    Spudich, J.A.4    Reisler, E.5
  • 10
    • 0027134594 scopus 로고
    • The actin/actin interactions involving the N-terminus of the DNase-I-binding loop are crucial for stabilization of the actin filament
    • Khaitlina S.Y., Moraczewska J., Strzelecka-Golaszewska H. The actin/actin interactions involving the N-terminus of the DNase-I-binding loop are crucial for stabilization of the actin filament. Eur. J. Biochem. 218:1993;911-920.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 911-920
    • Khaitlina, S.Y.1    Moraczewska, J.2    Strzelecka-Golaszewska, H.3
  • 11
    • 0028228518 scopus 로고
    • Dynamic properties of actin - structural changes induced by beryllium fluoride
    • Muhlrad A., Cheung P., Phan B.C., Miller C., Reisler E. Dynamic properties of actin - structural changes induced by beryllium fluoride. J. Biol. Chem. 269:1994;11852-11858.
    • (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
  • 12
    • 0031777885 scopus 로고    scopus 로고
    • A new look at thin filament regulation in vertebrate skeletal muscle
    • Squire J.M., Morris E.P. A new look at thin filament regulation in vertebrate skeletal muscle. Fed. Am. Soc. Exp. Biol. J. 12:1998;761-771.
    • (1998) Fed. Am. Soc. Exp. Biol. J. , vol.12 , pp. 761-771
    • Squire, J.M.1    Morris, E.P.2
  • 13
    • 0026558989 scopus 로고
    • Removing the 2 C-terminal residues of actin affects the filament structure
    • O'Donoghue S.I., Miki M., dos Remedios C.G. Removing the 2 C-terminal residues of actin affects the filament structure. Arch. Biochem. Biophys. 293:1992;110-116.
    • (1992) Arch. Biochem. Biophys. , vol.293 , pp. 110-116
    • O'Donoghue, S.I.1    Miki, M.2    Dos Remedios, C.G.3
  • 14
    • 0027452835 scopus 로고
    • Proteolytic removal of 3 C-terminal residues of actin alters the monomer-monomer interactions
    • Mossakowska M., Moraczewska J., Khaitlina S., Strzelecka-Golaszewska H. Proteolytic removal of 3 C-terminal residues of actin alters the monomer-monomer interactions. Biochem. J. 289:1993;897-902.
    • (1993) Biochem. J. , vol.289 , pp. 897-902
    • Mossakowska, M.1    Moraczewska, J.2    Khaitlina, S.3    Strzelecka-Golaszewska, H.4
  • 15
    • 0027497704 scopus 로고
    • Cooperative effects on filament stability in actin modified at the C-terminus by substitution or truncation
    • Drewes G., Faulstich H. Cooperative effects on filament stability in actin modified at the C-terminus by substitution or truncation. Eur. J. Biochem. 212:1993;247-253.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 247-253
    • Drewes, G.1    Faulstich, H.2
  • 16
    • 0027967683 scopus 로고
    • Structural connectivity in actin-Effect of C-terminal modifications on the properties of actin
    • Crosbie R.H., Miller C., Cheung P., Goodnight T., Muhlrad A., Reisler E. Structural connectivity in actin-Effect of C-terminal modifications on the properties of actin. Biophys. J. 67:1994;1957-1964.
    • (1994) Biophys. J. , vol.67 , pp. 1957-1964
    • Crosbie, R.H.1    Miller, C.2    Cheung, P.3    Goodnight, T.4    Muhlrad, A.5    Reisler, E.6
  • 17
    • 0030012195 scopus 로고    scopus 로고
    • Conformational changes in subdomain I of actin induced by proteolytic cleavage within the DNase I-binding loop-energy transfer from tryptophan to AEDANS
    • Kuznetsova I., Antropova O., Turoverov K., Khaitlina S. Conformational changes in subdomain I of actin induced by proteolytic cleavage within the DNase I-binding loop-energy transfer from tryptophan to AEDANS. FEBS Lett. 383:1996;105-108.
    • (1996) FEBS Lett. , vol.383 , pp. 105-108
    • Kuznetsova, I.1    Antropova, O.2    Turoverov, K.3    Khaitlina, S.4
  • 18
    • 0029841187 scopus 로고    scopus 로고
    • Intermolecular coupling between loop 38-52 and the C-terminus in actin filaments
    • Kim E., Reisler E. Intermolecular coupling between loop 38-52 and the C-terminus in actin filaments. Biophys. J. 71:1996;1914-1919.
    • (1996) Biophys. J. , vol.71 , pp. 1914-1919
    • Kim, E.1    Reisler, E.2
  • 20
    • 0031556946 scopus 로고    scopus 로고
    • Cooperative rigor binding of myosin to actin is a function of F-actin structure
    • Orlova A., Egelman E.H. Cooperative rigor binding of myosin to actin is a function of F-actin structure. J. Mol. Biol. 265:1997;469-474.
    • (1997) J. Mol. Biol. , vol.265 , pp. 469-474
    • Orlova, A.1    Egelman, E.H.2
  • 21
    • 0027340549 scopus 로고
    • A 13-A map of the actin-scruin filament from the limulus acrosomal process
    • Owen C., DeRosier D. A 13-A map of the actin-scruin filament from the limulus acrosomal process. J. Cell Biol. 123:1993;337-344.
    • (1993) J. Cell Biol. , vol.123 , pp. 337-344
    • Owen, C.1    Derosier, D.2
  • 22
    • 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., Botstein D., Reisler E. Mutational analysis of the role of hydrophobic residues in the 338-348 helix on actin in actomyosin interactions. Biochemistry. 35:1996;3670-3676.
    • (1996) Biochemistry , vol.35 , pp. 3670-3676
    • Miller, C.J.1    Doyle, T.C.2    Bobkova, E.3    Botstein, D.4    Reisler, E.5
  • 23
    • 0028910876 scopus 로고
    • Allele shuffling: Conjugational transfer, plasmid shuffling and suppressor analysis in Saccharomyces cerevisiae
    • Sikorski R.S.M., William A., Tugendreich S., Hieter P. Allele shuffling: conjugational transfer, plasmid shuffling and suppressor analysis in Saccharomyces cerevisiae. Gene. 155:1995;51-59.
    • (1995) Gene , vol.155 , pp. 51-59
    • Sikorski, R.S.M.1    William, A.2    Tugendreich, S.3    Hieter, P.4
  • 24
    • 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., 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
  • 25
    • 0024316496 scopus 로고
    • Subtilisin-cleaved actin - polymerization and interaction with myosin subfragment-1
    • Schwyter D., Phillips M., Reisler E. Subtilisin-cleaved actin - polymerization and interaction with myosin subfragment-1. Biochemistry. 28:1989;5889-5895.
    • (1989) Biochemistry , vol.28 , pp. 5889-5895
    • Schwyter, D.1    Phillips, M.2    Reisler, E.3
  • 27
    • 0032558437 scopus 로고    scopus 로고
    • Kinetic studies on the effect of yeast cofilin on yeast actin polymerization
    • Du J.F., Frieden C. Kinetic studies on the effect of yeast cofilin on yeast actin polymerization. Biochemistry. 37:1998;13276-13284.
    • (1998) Biochemistry , vol.37 , pp. 13276-13284
    • Du, J.F.1    Frieden, C.2
  • 28
    • 0030794505 scopus 로고    scopus 로고
    • Fluorescence probing of yeast actin subdomain 3/4 hydrophobic loop 262-274-Actin-actin and actin-myosin interactions in actin filaments
    • Feng L., Kim E., Lee W.L. et al. Fluorescence probing of yeast actin subdomain 3/4 hydrophobic loop 262-274-Actin-actin and actin-myosin interactions in actin filaments. J. Biol. Chem. 272:1997;16829-16837.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16829-16837
    • Feng, L.1    Kim, E.2    Lee, W.L.3
  • 29
    • 0032558990 scopus 로고    scopus 로고
    • Intrastrand cross-linked actin between Gln-41 and Cys-374. I. Mapping of sites cross-linked in F-actin by N-(4-azido-2-nitrophenyl) putrescine
    • Hegyi G., Mak M., Kim E., Elzinga M., Muhlrad A., Reisler E. Intrastrand cross-linked actin between Gln-41 and Cys-374. I. Mapping of sites cross-linked in F-actin by N-(4-azido-2-nitrophenyl) putrescine. Biochemistry. 37:1998;17784-17792.
    • (1998) Biochemistry , vol.37 , pp. 17784-17792
    • Hegyi, G.1    Mak, M.2    Kim, E.3    Elzinga, M.4    Muhlrad, A.5    Reisler, E.6
  • 30
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labeled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • Kouyama T., Mihashi K. Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labeled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur. J. Biochem. 114:1981;33-38.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 31
    • 0029202621 scopus 로고
    • Pyrene excimer fluorescence as a probe of protein conformational change
    • B.B. Biswas, Roy S. New York: Plenum Press
    • Lehrer S.S. Pyrene excimer fluorescence as a probe of protein conformational change. Biswas B.B., Roy S. Subcellular Biochemistry, Proteins: Structure, Function, and Engineering. 24:1995;115-131 Plenum Press, New York.
    • (1995) Subcellular Biochemistry, Proteins: Structure, Function, and Engineering , vol.24 , pp. 115-131
    • Lehrer, S.S.1
  • 32
    • 0032558975 scopus 로고    scopus 로고
    • Intrastrand cross-linked actin between Gln-41 and Cys-374. III. Inhibition of motion and force generation with myosin
    • Kim E., Bobkova E., Miller C.J. et al. Intrastrand cross-linked actin between Gln-41 and Cys-374. III. Inhibition of motion and force generation with myosin. Biochemistry. 37:1998;17801-17809.
    • (1998) Biochemistry , vol.37 , pp. 17801-17809
    • Kim, E.1    Bobkova, E.2    Miller, C.J.3
  • 33
    • 0030804033 scopus 로고    scopus 로고
    • A correlative analysis of actin filament assembly, structure, and dynamics
    • Steinmetz M., Goldie K., Aebi U. A correlative analysis of actin filament assembly, structure, and dynamics. J. Cell Biol. 138:1997;559-574.
    • (1997) J. Cell Biol. , vol.138 , pp. 559-574
    • Steinmetz, M.1    Goldie, K.2    Aebi, U.3
  • 34
    • 0025685506 scopus 로고
    • Inhibition of sliding movement of F-actin by cross-linking emphasizes the role of actin structure in the mechanism of motility
    • Prochniewicz E., Yanagida T. Inhibition of sliding movement of F-actin by cross-linking 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


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