Structural and functional repetition in a marine mussel adhesive protein.
The DOPA-rich polyphenolic protein secreted by the marine mussel Mytilus edulis establishes key chemical linkages in a water-resistant adhesive. Molecular cloning of the gene for this remarkable protein reveals its primary structure as one of the most repetitive proteins identified in the animal kingdom. Expression and purification of polyphenolic proteins from recombinant yeast have provided sufficient material to demonstrate adhesivity of these polypeptides in the laboratory. Adhesive tests reveal a water-resistant bonding capacity of the protein that is dependent on in vitro modification of tyrosine residues to DOPA and the subsequent oxidation to quinone.
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Genex Corporation, Gaithersburg, Maryland 20877.
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D049872:Bivalvia; D003001:Cloning, Molecular; D003432:Cross-Linking Reagents; D004247:DNA; D005091:Exons; D006900:Hydroxylation; D008969:Molecular Sequence Data; D014442:Monophenol Monooxygenase / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000235:genetics* / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000235:genetics; D013303:Streptomyces antibioticus / Q000201:enzymology; D014443:Tyrosine / Q000378:metabolism
D003432:Cross-Linking Reagents; D011506:Proteins; C037403:adhesive protein, mussel; D014443:Tyrosine; D004247:DNA; D014442:Monophenol Monooxygenase