ArticleProceedings of the National Academy of Sciences of the United States of America1994
Scallop striated and smooth muscle myosin heavy-chain isoforms are produced by alternative RNA splicing from a single gene.
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 16 papers.
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Who cites it
16 citing papers in PubMed, 49 citations in OpenAlex.
- Genome-Wide Identification and Expression Profiles of Myosin Genes in the Pacific White Shrimp,Frontiers in physiology · 2019Article
- Differences between fast and slow muscles in scallops revealed through proteomics and transcriptomics.BMC genomics · 2018Article
- Scallop genome reveals molecular adaptations to semi-sessile life and neurotoxins.Nature communications · 2017Article
- Article
- An invertebrate smooth muscle with striated muscle myosin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Shared gene structures and clusters of mutually exclusive spliced exons within the metazoan muscle myosin heavy chain genes.PloS one · 2014Article
- Independent specialisation of myosin II paralogues in muscle vs. non-muscle functions during early animal evolution: a ctenophore perspective.BMC evolutionary biology · 2012Article
- Muscular tissues of the squid Doryteuthis pealeii express identical myosin heavy chain isoforms: an alternative mechanism for tuning contractile speed.The Journal of experimental biology · 2012Article
- Development of a Pacific oyster (Crassostrea gigas) 31,918-feature microarray: identification of reference genes and tissue-enriched expression patterns.BMC genomics · 2011Article
- Alternative S2 hinge regions of the myosin rod affect myofibrillar structure and myosin kinetics.Biophysical journal · 2009Article
- Alternative S2 hinge regions of the myosin rod differentially affect muscle function, myofibril dimensions and myosin tail length.Journal of molecular biology · 2007Article
- An in vitro assay reveals essential protein components for the "catch" state of invertebrate smooth muscle.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Variable surface loops and myosin activity: accessories to a motor.Journal of muscle research and cell motility · 2000Review
- Regulation by molluscan myosins.Molecular and cellular biochemistry · 1999Review
- Amino-acid sequence of squid myosin heavy chain.Journal of muscle research and cell motility · 1998Article
- Sequence variations in the surface loop near the nucleotide binding site modulate the ATP turnover rates of molluscan myosins.Journal of muscle research and cell motility · 1996Article
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
We report here that the catch and striated adductor muscle myosin heavy-chain (MHC) isoforms of scallop (Argopecten irradians, previously Aequipecten irradians) are generated by alternative RNA splicing from a single gene. Scallop catch muscle cDNA and genomic DNA were amplified by PCR using primers based on the previously sequenced scallop striated muscle MHC cDNA. Mapping of the exon/intron borders and sequencing of a full-length catch muscle MHC in overlapping fragments revealed that the 24-kb gene encodes the MHC polypeptide in 27 exons and that four sets of tandem exon pairs are alternatively spliced into a striated and a catch MHC isoform. An additional alternative exon was identified in catch cDNA and is apparently spliced into a minor MHC isoform. The striated muscle-specific isoform is not expressed in other tissues, whereas the catch-type isoforms were also detected in various smooth muscles, but not in the striated one. Of the alternative exons, exons 5 and 6 encode part of the ATP-binding region and the 25-kDa/50-kDa proteolytic junction; exon 13 encodes part of one of the actin-binding regions and extends to the active site; exon 20 encodes the middle of the rod hinge region; exon 26 in the striated-specific sequence starts with the stop codon, whereas the catch-specific exon codes for an additional 10 residues. Differences between the alternative exons presumably determine the lower ATPase activity of smooth muscle myosin, contribute to the different structure of the striated and smooth muscle thick filaments, and may also be important for the molecular mechanism of the catch phenomenon.
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