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Titolo:
THE EFFECTS OF SMOOTH-MUSCLE CALPONIN ON THE STRONG AND WEAK MYOSIN BINDING-SITES OF F-ACTIN
Autore:
ELMEZGUELDI M; MARSTON SB;
Indirizzi:
NATL HEART & LUNG INST,UNIV LONDON IMPERIAL COLL SCI TECHNOL & MED,SCH MED,DEPT CARDIAC MED LONDON SW3 6LY ENGLAND
Titolo Testata:
The Journal of biological chemistry
fascicolo: 45, volume: 271, anno: 1996,
pagine: 28161 - 28167
SICI:
0021-9258(1996)271:45<28161:TEOSCO>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
VITRO MOTILITY ANALYSIS; ATPASE ACTIVITY; TROPONIN-TROPOMYOSIN; HEAVY-MEROMYOSIN; SKELETAL-MUSCLE; IN-VITRO; ACTOMYOSIN MGATPASE; THIN-FILAMENTS; CALDESMON; INHIBITION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
M. Elmezgueldi e S.B. Marston, "THE EFFECTS OF SMOOTH-MUSCLE CALPONIN ON THE STRONG AND WEAK MYOSIN BINDING-SITES OF F-ACTIN", The Journal of biological chemistry, 271(45), 1996, pp. 28161-28167

Abstract

We have investigated the mechanism of inhibition of the actomyosin MgATPase by the smooth muscle protein calponin. We have shown previouslythe specific interaction of calponin with Glu(334) of actin (EL-Mezgueldi, M., Fattoum, A., Derancourt, J., and Hassab, R. (1992) J. Biol. Chem. 267, 15943-15951). This residue is within the sequence 332-334, which has been proposed to be an important part of the strong myosin binding site (Rayment, L., Holden, H. M., Whittaker, M., Yohn, C. B., Lorenz, M., Holmes, K. C., and Milligan, R. A. (1993) Science 261, 58-65), Therefore, we suggested that calponin will affect the strong binding actin-myosin interaction, To test this hypothesis we have investigated the effect of calponin on the strong binding of S-1 . MgAMP-PNP (5'-adenylyl imidodiphosphate) and on the weak binding of S-1 . MgADP . P-i to actin, We found that an inhibitory concentration of calponin decreased the binding of S-1 . MgAMP-PNP to actin but had no effect on the binding of S-1 . MgADP . P-i. Similar results were obtained with skeletal muscle and smooth muscle S-1. In competition experiments calponin was found to displace S-1 . MgAMP-PNP and S-1 . MgADP but not S-1 . MgADP . P-i from the actin filament, S-1 displaced calponin from actin in the rigor state, in the presence of MgADP, and in the presence ofMgAMP-PNP. We conclude that calponin inhibits the actin activated S-1ATPase by blocking a strong S-1 binding site on actin and does not block the weak binding site.

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Documento generato il 13/08/20 alle ore 14:38:30