Open AccessThe occurrence of tissue‐specific twitchin isoforms in the mussel Mytilus galloprovincialis
Author(s) -
KUSAKA Miho,
IKEDA Daisuke,
FUNABARA Daisuke,
HARTSHORNE David J,
WATABE Shugo
Publication year - 2008
Publication title -
fisheries science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.412
H-Index - 64
eISSN - 1444-2906
pISSN - 0919-9268
DOI - 10.1111/j.1444-2906.2008.01574.x
Subject(s) - mytilus , byssus , gene isoform , biology , mussel , biochemistry , phosphorylation , complementary dna , microbiology and biotechnology , gene , fishery
The catch state in Mytilus anterior byssus retractor muscle is regulated by phosphorylation and dephosphorylation of twitchin, a member of the titin/connectin superfamily, and involves two serine residues, Ser‐1075 (D1) and Ser‐4316 (D2). This study was undertaken to examine whether isoforms of twitchin were expressed in various muscles of the mussel Mytilus galloprovincialis by reverse transcription‐polymerase chain reaction. Mussel tissues, including both catch and non‐catch muscles, contained various twitchin isoforms that all contained the D2 site and the kinase domain. However, sequence alterations were detected around the D1 site, notably a potential deletion of the D1 site. All isoforms from catch muscles contained both the D1 and D2 sites, whereas those from non‐catch muscles also expressed the D2 site, but some of them lacked the D1 site. This suggests that the D1 site of twitchin is essential to the mechanism of catch. Genomic DNA analysis revealed that twitchin isoforms are produced by alternative splicing.