Conservative Structure of the Plaque Matrix Protein of Mussels in the Genus Mytilus |
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Authors: | Koji Inoue Kei Kamino Futaba Sasaki Satoshi Odo Shigeaki Harayama |
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Institution: | Marine Biotechnology Institute, Kamaishi Laboratories, Heita, Kamaishi, Iwate 026-0001, Japan |
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Abstract: | : The complementary DNA encoding the byssal plaque matrix protein (fp-2) of the mussel Mytilus coruscus was isolated. The predicted amino acid sequence (474 amino acids) consists of four parts: the signal peptide, the amino-terminal nonrepetitive domain, the central repetitive domain containing 11 repeats of an epidermal growth factor?like motif, and the carboxy-terminal nonrepetitive domain. The amino acid sequence is 82.7%, similar to that of fp-2 of Mytilus galloprovincialis, and the basic structure including number and motif of repeats is highly conservative. Amino acid substitutions are less frequent in ``consensus positions' of the central repetitive domain (13.1%), and most of them are changes from irregular amino acids to regular ones. Thus, the structure of fp-2 was found to be conservative between species. It was presumed that the basic structure of fp-2 is unchangeable to maintain the flexible and durable matrix structure and that variation is not required because fp-2 is protected by other surface proteins. |
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