Primary structure of myostracal prism soluble protein (MPSP) in oyster shell, Crassostrea gigas.
Soluble protein (MPSP, myostracal prism soluble protein) obtained from myostracum in oyster shell (Crassostrea gigas) was characterized using biochemical and molecular biological techniques. From an analysis of secondary protein structure, it was shown that beta-structure was predominant in MPSP. And via in vitro assays, the relation of MPSP to biomineral phase and morphology was studied. SDS-PAGE revealed one major protein band of 20 kDa. An amino acid sequence of 160 amino acids was deduced for myostracum by characterization of the complementary DNA encoding the protein. The deduced protein was composed of a high proportion of Gly and Asp, typifying a calcium-binding protein for shell formation, and a relatively high proportion of Val, Ala and Ile, typifying an adhesive protein. In contrast to prevailing expectations, (Gly-Asp)n-type sequence motifs exist in MPSP, demanding a revision of previous theories of protein-mineral interactions. The cDNA sequence of myostracum is elucidated for the first time.
Lee
Seung Woo
SW
Department of Chemical & Biomolecular Engineering, Sogang University, Seoul, 121-742, Korea.
Kim
Young Moon
YM
Choi
Hong Seok
HS
Yang
Jai Myung
JM
Choi
Cheong Song
CS
D000818:Animals; D049896:Crassostrea / Q000033:anatomy & histology* / Q000737:chemistry* / Q000235:genetics; D005786:Gene Expression Regulation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics; D012995:Solubility
D011506:Proteins; D012333:RNA, Messenger