Sea urchin collagen evolutionarily homologous to vertebrate pro-alpha 2(I) collagen.
We isolated several overlapping cDNA clones covering the 4242 nucleotides of a Strongylocentrotus purpuratus transcript that codes for a fibrillar procollagen chain. The sea urchin polypeptide includes a 124-amino acid long amino pre-propeptide, a 1064-amino acid alpha-chain inclusive of 338 uninterrupted Gly-X-Y repeats, and a 226-residue carboxyl-propeptide. The distribution of the highly conserved cysteines within the last domain together with the structural configuration of the amino-propeptide and the organization of the corresponding coding region, strongly suggest that the sea urchin gene is evolutionarily related to the vertebrate pro-alpha 2(I) collagen. This work, therefore, represents the first report of the complete primary structure of an invertebrate fibrillar procollagen chain. It also provides a new insight into the evolution of the amino-propeptide, the most divergent among the major protein domains of fibrillar procollagen chains.
Exposito
J Y
JY
Brookdale Center for Molecular Biology, Mt. Sinai School of Medicine, New York, New York 10029.
D'Alessio
M
M
Solursh
M
M
Ramirez
F
F
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D003001:Cloning, Molecular; D003094:Collagen / Q000235:genetics*; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D005091:Exons; D005775:Gastrula; D015723:Gene Library; D005796:Genes; D046911:Macromolecular Substances; D008297:Male; D008969:Molecular Sequence Data; D011347:Procollagen / Q000737:chemistry*; D011487:Protein Conformation; D015183:Restriction Mapping; D012617:Sea Urchins / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D013094:Spermatozoa / Q000502:physiology; D014714:Vertebrates / Q000235:genetics*
D046911:Macromolecular Substances; D011347:Procollagen; D003094:Collagen; D004247:DNA