Regulatory light chain influences alterations of myosin head induced by actin
- 16 December 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 295 (1) , 55-58
- https://doi.org/10.1016/0014-5793(91)81383-j
Abstract
The effect of magnesium-for-calcium exchange and phosphorylation of regulatory light chain (LC 2 ) on structural organization of rabbit skeletal myosin head was studied by limited tryptic digestion. In the presence of actin, exchange of magnesium bound to LC 2 by calcium in dephosphorylated myosin accelerates the digestion of myosin and heavy meromysin heavy chain and increases the accumulation of a 50 kDa fragment. This effect is significantly diminished in the case of phosphorylated myosin. Thus, both phosphorylation and cation exchange influences the effect of actin binding on the structural organization of myosin head.Keywords
This publication has 37 references indexed in Scilit:
- On the origin and transmission of force in actomyosin subfragment 1.Proceedings of the National Academy of Sciences, 1989
- Functional sequences of the myosin headJournal of Muscle Research and Cell Motility, 1989
- Domains, motions and regulation in the myosin headJournal of Muscle Research and Cell Motility, 1988
- Movement of myosin fragments in vitro: Domains involved in force productionCell, 1987
- The Mechanism of Muscle ContractioCritical Reviews in Biochemistry, 1986
- Crossbridge behaviour during muscle contractionJournal of Muscle Research and Cell Motility, 1985
- Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibilityJournal of Molecular Biology, 1977
- Actin-Induced Local Conformational Change in the Myosin MoleculeThe Journal of Biochemistry, 1977
- Studies on the Helical Segment of the Myosin MoleculePublished by Cold Spring Harbor Laboratory ,1973
- Sulfhydryl Groups Involved in the Active Site of Myosin A Adenosine Triphosphatase*The Journal of Biochemistry, 1966