|The adhesive protein cDNA of Mytilus galloprovincialis encodes decapeptide repeats but no hexapeptide motif|
Inoue, K.; Odo, S. (1994). The adhesive protein cDNA of Mytilus galloprovincialis encodes decapeptide repeats but no hexapeptide motif. Biol. Bull. 186(3): 349-355
In: Biological Bulletin. Marine Biological Laboratory: Lancaster, Pa. etc.. ISSN 0006-3185, more
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A mussel is attached to hard surfaces by its byssus, which consists of a bundle of threads, each with a fibrous collagenous core coated with adhesive proteins. We constructed a cDNA library from RNA isolated from the foot of the mussel Mytilus galloprovincialis sampled in Japan. The library was probed with a nucleotide sequence corresponding to a part of the decapeptide repeat motif in the major adhesive protein of the closely related species M. edulis, and a clone including the whole coding region of the same adhesive protein of M. galloprovincialis was isolated. The sequences of the signal and nonrepetitive regions of the protein of M. galloprovincialis were homologous to those of M. edulis, despite several substitutions and a deletion of 18 amino acids. The repetitive region included a tetradecapeptide sequence and 62 repeats of the same decapeptide motif as in M. edulis, but hexapeptide sequences present in M. edulis were absent in the protein of M. galloprovincialis. In the decapeptide motif, two tyrosine residues, two lysine residues, and one of the two proline residues were highly conserved, but other residues were frequently substituted. In some residues in the decapeptide motif, specific codon usages were observed, suggesting that the nucleotide sequence itself has a function.