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Volumn 71, Issue 4, 1996, Pages 1914-1919

Intermolecular coupling between loop 38-52 and the C-terminus in actin filaments

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; COPPER; DEOXYRIBONUCLEASE I; ETHYLENEDIAMINE DERIVATIVE; F ACTIN; SUBTILISIN;

EID: 0029841187     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79390-6     Document Type: Article
Times cited : (40)

References (30)
  • 1
    • 0028595912 scopus 로고
    • Sequence 18-29 on actin: Antibody and spectroscopic probing of conformational changes
    • Adams, S. B., and E. Reisler. 1994. Sequence 18-29 on actin: antibody and spectroscopic probing of conformational changes. Biochemistry. 33: 14426-14433.
    • (1994) Biochemistry , vol.33 , pp. 14426-14433
    • Adams, S.B.1    Reisler, E.2
  • 2
    • 0027967683 scopus 로고
    • Structural connectivity in actin: Effect of C-terminal modifications on the properties of actin
    • Crosbie, R. H., C. Miller, P. Cheung, T. Goodnight, A. Muhlrad, and E. Reisler. 1994. Structural connectivity in actin: effect of C-terminal modifications on the properties of actin. Biophys. J. 67:1957-1964.
    • (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
  • 4
    • 0027497704 scopus 로고
    • Cooperative effects on filament stability in actin modified at the C-terminus by substitution or truncation
    • Drewes, G., and H. Faulstich. 1993. Cooperative effects on filament stability in actin modified at the C-terminus by substitution or truncation. Eur. J. Biochem. 212:247-253.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 247-253
    • Drewes, G.1    Faulstich, H.2
  • 5
    • 0026768578 scopus 로고
    • The binding of mutant actins to profilin, ATP and DNase I
    • Drummond, D. R., E. S. Hennessey, and J. C. Sparrow. 1992. The binding of mutant actins to profilin, ATP and DNase I. Eur. J. Biochem. 209:171-179.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 171-179
    • Drummond, D.R.1    Hennessey, E.S.2    Sparrow, J.C.3
  • 7
    • 0028988935 scopus 로고
    • New insights into actin filament dynamics
    • Egelman, E. H., and A. Orlova. 1995. New insights into actin filament dynamics. Curr. Opin. Struct. Biol. 5:172-180.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 172-180
    • Egelman, E.H.1    Orlova, A.2
  • 8
    • 0027389463 scopus 로고
    • Conformational changes in subdomain-2 of G-actin upon polymerization into F-actin and upon binding myosin subfragment-1
    • Fievez, S., and M. Carlier. 1993. Conformational changes in subdomain-2 of G-actin upon polymerization into F-actin and upon binding myosin subfragment-1. FEBS Lett. 316:186-190.
    • (1993) FEBS Lett. , vol.316 , pp. 186-190
    • Fievez, S.1    Carlier, M.2
  • 9
    • 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. 9:886-893.
    • (1970) Biochemistry , vol.9 , pp. 886-893
    • Godfrey, J.E.1    Harrington, W.F.2
  • 10
    • 0017071181 scopus 로고
    • ATP binding to a protease-resistant core of actin
    • Jacobson, G. R., and J. P. Rosenbusch. 1976. ATP binding to a protease-resistant core of actin. Proc. Natl. Acad. Sci. USA. 73:2742-2746.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2742-2746
    • Jacobson, G.R.1    Rosenbusch, J.P.2
  • 11
    • 0024286070 scopus 로고
    • Orientation of the actin monomer in the F-actin filament: Radial coordinate of glutamine-41 and the effect of myosin subfragment-1 binding on the monomer orientation
    • Kasprzak, A. A., R. Takashi, and M. F. Morales. 1988. Orientation of the actin monomer in the F-actin filament: Radial coordinate of glutamine-41 and the effect of myosin subfragment-1 binding on the monomer orientation. Biochemistry. 27:4512-4522.
    • (1988) Biochemistry , vol.27 , pp. 4512-4522
    • Kasprzak, A.A.1    Takashi, R.2    Morales, M.F.3
  • 12
    • 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., J. Moraczewska, and H. Strzelecka-Golaszewska. 1993. 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. 218:911-920.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 911-920
    • Khaitlina, S.Y.1    Moraczewska, J.2    Strzelecka-Golaszewska, H.3
  • 13
    • 0030048282 scopus 로고    scopus 로고
    • Myosin-induced changes in F-actin: Fluorescence probing of sub-domain 2 by dansyl ethylenediamine attached to Gin-41
    • Kim, E., C. J. Miller, M. Motoki, K. Seguro, A. Muhlrad, and E. Reisler. 1996. Myosin-induced changes in F-actin: fluorescence probing of sub-domain 2 by dansyl ethylenediamine attached to Gin-41. Biophys. J. 70:1439-1446.
    • (1996) Biophys. J. , vol.70 , pp. 1439-1446
    • Kim, E.1    Miller, C.J.2    Motoki, M.3    Seguro, K.4    Muhlrad, A.5    Reisler, E.6
  • 14
    • 0028871340 scopus 로고
    • Conformational changes in subdomain 2 of G-actin: Fluorescence probing by dansyl ethylenediamine attached to Gln-41
    • Kim, E., M. Motoki, K. Seguro, A. Muhlrad, and E. Reisler. 1995. Conformational changes in subdomain 2 of G-actin: fluorescence probing by dansyl ethylenediamine attached to Gln-41. Biophys. J. 69: 2024-2032.
    • (1995) Biophys. J. , vol.69 , pp. 2024-2032
    • Kim, E.1    Motoki, M.2    Seguro, K.3    Muhlrad, A.4    Reisler, E.5
  • 15
    • 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., and K. Mikashi. 1981. 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. 113:33-38.
    • (1981) Eur. J. Biochem. , vol.113 , pp. 33-38
    • Kouyama, T.1    Mikashi, K.2
  • 16
    • 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 trypto-phanto AEDANS
    • Kuznetsova, I., O. Antropova, K. Turoverov, and S. Khaitlina. 1996. Conformational changes in subdomain I of actin induced by proteolytic cleavage within the DNase I binding loop: energy transfer from trypto-phanto AEDANS. FEBS Lett. 383:105-108.
    • (1996) FEBS Lett. , vol.383 , pp. 105-108
    • Kuznetsova, I.1    Antropova, O.2    Turoverov, K.3    Khaitlina, S.4
  • 17
    • 0015337669 scopus 로고
    • 2+ to actin without loss of polymerizability: The involvement of the rapidly reacting -SH group
    • 2+ to actin without loss of polymerizability: the involvement of the rapidly reacting -SH group. Arch. Biochem. Biophys. 150:164-174.
    • (1972) Arch. Biochem. Biophys. , vol.150 , pp. 164-174
    • Lehrer, S.S.1    Nagy, B.2    Gergely, J.3
  • 18
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation alogarithm
    • Lorenz, M., D. Popp, and K. C. Holmes. 1993. Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation alogarithm. J. Mol. Biol. 234:826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 19
    • 0028228518 scopus 로고
    • Dynamic properties of actin: Structural changes induced by beryllium fluoride
    • Muhlrad, A., P. Cheung, B. C. Phan, C. Miller, and E. Reisler. 1994. Dynamic properties of actin: structural changes induced by beryllium fluoride. J. Biol. Chem. 269:11852- 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
  • 20
    • 0026437417 scopus 로고
    • Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysis
    • Orlova, A., and E. H. Egelman. 1992. Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysis. J. Mol. Biol. 227:1043-1053.
    • (1992) J. Mol. Biol. , vol.227 , pp. 1043-1053
    • Orlova, A.1    Egelman, E.H.2
  • 21
    • 0027328612 scopus 로고
    • A Conformational change in the actin subunit can change the flexibility of the actin filament
    • Orlova, A., and E. H. Egelman. 1993. A Conformational change in the actin subunit can change the flexibility of the actin filament. J. Mol. Biol. 232:334-341.
    • (1993) J. Mol. Biol. , vol.232 , pp. 334-341
    • Orlova, A.1    Egelman, E.H.2
  • 22
    • 0028907435 scopus 로고
    • Structural dynamics of F-actin. I. Changes in the C terminus
    • Orlova, A., and H. E. Egelman. 1995. Structural dynamics of F-actin. I. Changes in the C terminus. J. Mol. Biol. 245:582-597.
    • (1995) J. Mol. Biol. , vol.245 , pp. 582-597
    • Orlova, A.1    Egelman, H.E.2
  • 23
    • 0028920157 scopus 로고
    • Structural dynamics of F-actin: II. Cooperativity in structural transitions
    • Orlova, A., E. Prochniewicz, and E. H. Egelman̈. 1995. Structural dynamics of F-actin: II. Cooperativity in structural transitions. J. Mol. Biol. 245:598-607.
    • (1995) J. Mol. Biol. , vol.245 , pp. 598-607
    • Orlova, A.1    Prochniewicz, E.2    Egelman̈, E.H.3
  • 24
    • 0027340549 scopus 로고
    • A 13 Å map of the actin-scruin filament from the Limulus acrosomal process
    • Owen. C., and D. DeRosier. 1993. A 13 Å map of the actin-scruin filament from the Limulus acrosomal process. J. Cell Biol. 123:337-344.
    • (1993) J. Cell Biol. , vol.123 , pp. 337-344
    • Owen, C.1    DeRosier, D.2
  • 25
    • 0024316496 scopus 로고
    • Subtilisin-cleaved actin: Polymerization and interaction with myosin subfragment 1
    • Schwyter, D., M. Phillips, and E. Reisler. 1989. Subtilisin-cleaved actin: polymerization and interaction with myosin subfragment 1. Biochemistry. 28:5889-5895.
    • (1989) Biochemistry , vol.28 , pp. 5889-5895
    • Schwyter, D.1    Phillips, M.2    Reisler, E.3
  • 26
    • 0025359118 scopus 로고
    • Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin
    • Schwyter, D. H., S. J. Kron, Y. Y. Toyoshima, J. A. Spudich, and E. Reisler. 1990. Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin. J. Cell. Biol. 111:465-470.
    • (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
  • 27
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosintroponin 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, S.2
  • 28
    • 0027523454 scopus 로고
    • Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion
    • Strzelecka-Golaszewska, H., J. Moraczewska, S. Y. Khaitlina, and M. Mossakowska. 1993. Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion. Eur. J. Biochem. 221:731-742.
    • (1993) Eur. J. Biochem. , vol.221 , pp. 731-742
    • Strzelecka-Golaszewska, H.1    Moraczewska, J.2    Khaitlina, S.Y.3    Mossakowska, M.4
  • 29
    • 0028861589 scopus 로고
    • Normal modes as refinement parameters for the F-actin model
    • Tirion, M. M., D. Ben-Avraham, M. Lopez, and K. C. Holmes. 1995. Normal modes as refinement parameters for the F-actin model. Biophys. J. 68:5-12.
    • (1995) Biophys. J. , vol.68 , pp. 5-12
    • Tirion, M.M.1    Ben-Avraham, D.2    Lopez, M.3    Holmes, K.C.4
  • 30
    • 0017336444 scopus 로고
    • Studies of the chymotryptic digestion of myosin: Effects of divalent cations on proteolytic susceptibility
    • Weeds, A., and B. Pope. 1977. Studies of 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, B.2


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