ArticleProceedings of the National Academy of Sciences of the United States of America1994
Regulation of scallop myosin by the regulatory light chain depends on a single glycine residue.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 40 citations in OpenAlex.
- Amino Acid Composition in Different Tissues of Iceland Scallop from the Barents Sea.Animals : an open access journal from MDPI · 2024Article
- Myosin light chains: Teaching old dogs new tricks.Bioarchitecture · 2014Review
- Modification of interface between regulatory and essential light chains hampers phosphorylation-dependent activation of smooth muscle myosin.The Journal of biological chemistry · 2012Article
- Orientation of the N-terminal lobe of the myosin regulatory light chain in skeletal muscle fibers.Biophysical journal · 2012Article
- Insights derived from molecular dynamics simulation into the molecular motions of serine protease proteinase K.Journal of molecular modeling · 2010Article
- Analysis of tarantula skeletal muscle protein sequences and identification of transcriptional isoforms.BMC genomics · 2009Article
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- The early history of the biochemistry of muscle contraction.The Journal of general physiology · 2004Article
- Evaluation of the symmetric model for myosin-linked regulation: effect of site-directed mutations in the regulatory light chain on scallop myosin.The Biochemical journal · 2003Article
- Trifluoperazine inhibits the MgATPase activity and in vitro motility of conventional and unconventional myosins.Journal of muscle research and cell motility · 2003Article
- Primary structure of myosin from the striated adductor muscle of the Atlantic scallop, Pecten maximus, and expression of the regulatory domain.Journal of muscle research and cell motility · 2000Article
- Molecular dynamics simulations of protein-tyrosine phosphatase 1B. I. ligand-induced changes in the protein motions.Biophysical journal · 1999Article
- Regulation by molluscan myosins.Molecular and cellular biochemistry · 1999Review
- Microsecond rotational dynamics of spin-labeled myosin regulatory light chain induced by relaxation and contraction of scallop muscle.Biochemistry · 1998Article
- Essential and regulatory light chains of Placopecten striated and catch muscle myosins.Journal of muscle research and cell motility · 1996Article
- A fluorescent protein biosensor of myosin II regulatory light chain phosphorylation reports a gradient of phosphorylated myosin II in migrating cells.Molecular biology of the cell · 1995Article
- Role of essential light chain EF hand domains in calcium binding and regulation of scallop myosin.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Role of myosin light chains.Journal of muscle research and cell motility · 1994Review
- Regulatory domains of myosins: influence of heavy chain on Ca(2+)-binding.Journal of muscle research and cell motility · 1994Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Specific Ca2+ binding and Ca2+ activation of ATPase activity in scallop myosin require a regulatory light chain (RLC) from regulated (molluscan or vertebrate smooth) myosin; hybrids containing vertebrate skeletal RLCs do not bind Ca2+ and their ATPase activity is inhibited. Chimeras between scallop and chicken skeletal RLCs restore Ca2+ sensitivity to RLC-free myosin provided that residues 81-117 are derived from scallop. Six mutants (R90M, A94K, D98P, N105K, M116Q, and G117C) were generated by replacing amino acids of the scallop RLC with the corresponding skeletal RLC residues in positions conserved in either regulated or nonregulated myosins. Ca2+ binding was abolished by a G117C and a G117A mutation; however, these mutants have a decreased affinity for the heavy chain. None of the other mutations affected RLC function. Replacement of the respective cysteine with glycine in the skeletal RLC has markedly changed the regulatory properties of the molecule. The single cysteine to glycine mutation conferred to this light chain the ability to restore Ca2+ binding and regulated ATPase activity, although Ca2+ activation of the actin-activated ATPase was lower than with scallop RLC. The presence of amino acids other than glycine at this position in vertebrate skeletal myosin RLCs may explain why these are not fully functional in the scallop system. The results are in agreement with x-ray crystallography data showing the central role of G117 in stabilizing the Ca(2+)-binding site of scallop myosin.
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