Catchin, a novel protein in molluscan catch muscles, is produced by alternative splicing from the myosin heavy chain gene.

Molluscan catch muscles contain polypeptides of 110-120 kDa in size which have the same partial amino acid sequences as those of the myosin heavy chain (MHC). Here we provide evidence that these polypeptides are major components only of the catch-type muscles (their estimated molar ratio to MHC is approximately 1:1) and they are alternative products of the MHC gene. Northern blot analysis of total RNA from Mytilus galloprovincialis catch muscles was carried out with fragments from the 3'-end of the MHC cDNA as probes. We detected two bands of 6.5 kb and 3.5 kb. The former corresponds to the MHC mRNA, and the latter is an mRNA coding for catchin, a novel myosin rod-like protein. By using a 5'-rapid amplification of cDNA ends (RACE) PCR method, the full-length cDNA of Mytilus catchin was cloned. It codes for a protein with a unique N-terminal domain of 156 residues (rich in serine, threonine, and proline), which includes a phosphorylatable peptide sequence. The rest of the sequence is identical with the C-terminal 830 residues of the MHC. We also analyzed Mytilus and scallop (Argopecten irradians) genomic DNAs and found that the 5'-end of the cDNA sequence was located in a large intron of the MHC gene in both species. Since catchin is abundantly expressed only in catch muscles and it is phosphorylatable, we suggest that it may play an important role in the catch contraction of molluscan smooth muscles. Copyright 2000 Academic Press.