Exposito J Y, D'Alessio M, Solursh M, Ramirez F
Brookdale Center for Molecular Biology, Mt. Sinai School of Medicine, New York, New York 10029.
J Biol Chem. 1992 Aug 5;267(22):15559-62.
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.
我们分离出了几个重叠的cDNA克隆，它们覆盖了紫球海胆转录本的4242个核苷酸，该转录本编码一种纤维状前胶原链。海胆多肽包括一个124个氨基酸长的氨基前原肽、一个包含338个不间断Gly-X-Y重复序列的1064个氨基酸的α链，以及一个226个残基的羧基前肽。最后一个结构域内高度保守的半胱氨酸分布，连同氨基前肽的结构构型和相应编码区的组织，强烈表明海胆基因在进化上与脊椎动物的前α2（I）型胶原相关。因此，这项工作代表了无脊椎动物纤维状前胶原链完整一级结构的首次报道。它还为氨基前肽的进化提供了新的见解，氨基前肽是纤维状前胶原链主要蛋白质结构域中差异最大的。
