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Structural and Functional Repetition in a Marine Mussel Adhesive Protein
Author(s) -
Filpula David R.,
Lee ShwuMaan,
Link Rebecca P.,
Strausberg Susan L.,
Strausberg Robert L.
Publication year - 1990
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp00003a001
Subject(s) - mussel , mytilus , recombinant dna , biochemistry , yeast , tyrosine , chemistry , adhesive , cloning (programming) , biology , gene , ecology , organic chemistry , layer (electronics) , computer science , programming language
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.