Expression of multiple forms of an adhesive plaque protein in an individual mussel, Mytilus edulis |
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Authors: | S C Warner J H Waite |
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Institution: | (1) College of Marine Studies, University of Delaware, Newark, Delaware 19716, USA, US;(2) Department of Molecular, Cell and Developmental Biology, University of California, Santa Barbara, California 93106, USA, US |
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Abstract: | Individual blue mussels, Mytilus edulis L., can express at least 20 variants of a small protein known as M. edulis foot protein 3 or Mefp3. Mefp3 has been shown to be a component of the adhesive plaque of the byssus, the structure securing
mussels to solid substrata. The cDNAs and deduced fp3 protein sequences display more variation at the carboxy-terminus than
at the N-terminus, although there is some variation present throughout the protein. This indicates that there most likely
are multiple copies of the gene encoding this protein. Each protein sequence contains a signal peptide, 24 to 25 residues
in length, and a mature protein sequence of 44 to 54 residues. Gly is the most common amino acid in the mature protein at
20 to 25 mol%. Tyr and Arg follow closely at 20 to 23 and 16 to 21 mol%, respectively. Both of these amino acids were previously
shown to be post-translationally modified to 3,4-dihydroxyphenylalanine (Dopa) and 4-hydroxyarginine, respectively, in this
protein. MALDI-TOF (matrix-assisted laser desorption ionization with time-of-flight) mass spectrometric analysis of the underside
of adhesive plaques reveals the presence of Mefp3-like proteins. Curiously, only four or five out of 20 possible fp3 variants
are detectable in plaques deposited on glass or plastic. This would suggest that selection of protein variants for deposition
onto surfaces is determined at the level of translation.
Received: 11 August 1998 / Accepted: 15 April 1999 |
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