Worm Breeder's Gazette 15(2): 47 (February 1, 1998)
These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.
|1||Faculty of Agriculture, Department of Agricultural Chemistry, Tottori University, Minami 4-101, Koyama-cho, Tottori city, Tottori 680, Japan|
|2||Suntory Institute for Bioorganic Research, Wakayamadai 1-1-1, Shimamoto-cho, Mishima-gun, Osaka 618, Japan|
When we searched a peptide homologous with A-chain of Bombyxin a silkworm insulin-like peptide on the C. elegans genome project, we found two species of putativ e peptides that share four cystein residues with Bombyxin A-chain. Then we carried out RACE to obtain the full-length cDNA sequences. The predicted precursor proteins consist of 95 and 108 amino acid residues and contain a signal peptide, B-cahin, C-peptide, and A-chain in the order like those of Bombyxin and human insulin. The deduced mature peptides consist of 50 and 49 residues (named Ceinsulin-1 and Ceinsulin-2) and include six cystein residues identical with those of Bombyxin and human insulin. Ceinsulin-1 A-chain: QLQTICCQVGCNVEDLLAYCAPI B-chain: QQADGRMKMCPPGGSTFTMAWSMSCSM Ceinsulin-2 A-chain: TMNMCCETGCEFTDIFAICNPFG B-chain: AKHGSLKLCPPGGASFLDAFNLICPM Now we try to elicit three dimensional structures of the C. elegans insulin-like peptides using computer chemistry to compare with Bombyxin and human insulin. The GFP fusion proteins will reveal when and where the C. elegans genes encoding insulin-like peptides are expressed