Light-chain movement and regulation in scallop myosin
- 1 February 1983
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 301 (5900), 478-482
- https://doi.org/10.1038/301478a0
Abstract
Photo-cross-linking techniques show that when scallop myosin or myofibrils are subjected to experimental conditions that cause relaxed muscles to go into rigor, the N-terminal portion of the regulatory light chain of myosin moves towards the essential light chain while the C-terminal portion stays in place. These changes occur on the myosin before combination with actin. Cross-linking of the N-terminal region to the essential light chain in rigor locks the myosin into a conformation such that calcium sensitivity of the actin-activated Mg-ATPase is lost.This publication has 27 references indexed in Scilit:
- The role of myosin light chains in regulating actin-myosin interactionBiochimie, 1981
- Hybrid formation between scallop myofibrils and foreign regulatory light-chainsJournal of Molecular Biology, 1980
- Control of tension development in scallop muscle fibres with foreign regulatory light chainsNature, 1980
- Regulatory light-chains and scallop myosin: Full dissociation, reversibility and co-operative effectsJournal of Molecular Biology, 1980
- Interaction of skeletal myosin light chains with calcium ionsBiochemistry, 1978
- Reversible loss of calcium control of tension in scallop striated muscle associated with the removal of regulatory light chainsNature, 1978
- Physical characterization of myosin light chainsBiochemistry, 1978
- Regulatory light chains in myosinsJournal of Molecular Biology, 1976
- The light chains of scallop myosin as regulatory subunitsJournal of Molecular Biology, 1973
- Regulation in molluscan musclesJournal of Molecular Biology, 1970