PMID: 6404300Mar 15, 1983Paper

Calcium-sensitive binding of heavy meromyosin to regulated actin requires light chain 2 and the head-tail junction

Biochemistry
P D Wagner, D B Stone

Abstract

Sedimentation in a preparative ultracentrifuge was used to determine the affinity of heavy meromyosin, HMM, for regulated actin, F-actin plus troponin-tropomyosin, in the presence of MgATP at pH 7.0, 20 degrees C, and mu = 18 mM. HMM was prepared from vertebrate striated muscle myosin by a mild chymotryptic digestion. This HMM contained 85-90% intact 19 000-dalton light chains, LC2. In the presence of calcium, 90% of the HMM bound to regulated actin with an association constant of (2-4) X 10(4) M-1. In the absence of calcium, while one-third of the HMM bound with an affinity similar to that observed in the presence of calcium, the rest bound much more weakly. It was not possible to accurately determine the association constant for this weakly binding HMM, but a 20-fold reduction in affinity is consistent with the binding data. The binding of single-headed heavy meromyosin to regulated actin was similarly sensitive to the calcium concentration. Since removal of calcium inhibits the regulated actin-activated ATPase of HMM greater than 20-fold, troponin-tropomyosin must be capable of inhibiting both the binding of HMM to regulated actin and a step which occurs after binding but prior to product release. Removal of LC2 increased th...Continue Reading

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Citations

Nov 1, 1992·The International Journal of Biochemistry·H Kajiyama
Jan 1, 1992·Pharmacology & Therapeutics·J M Chalovich
Sep 26, 1986·Biochimica Et Biophysica Acta·U TollemarJ W Shriver
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Jul 20, 1990·Journal of Molecular Biology·T Arata
Sep 24, 2015·The Journal of Head Trauma Rehabilitation·Bojana BudisinRobin E Green
Feb 20, 1990·Biochemistry·A Bonet-KerracheD Mornet
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Jul 1, 1994·Current Biology : CB·M K ReedyF Schachat
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Dec 1, 1985·Journal of Muscle Research and Cell Motility·J Seymour, E J O'Brien
Jan 1, 1986·CRC Critical Reviews in Biochemistry·R Cooke

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