{"title":"A Major Substrate for MPF: cDNA Cloning and Expression of Polypeptide Chain Elongation Factor 1γ from Goldfish ( Carassius auratus )","authors":"M. Tokumoto, Y. Nagahama, T. Tokumoto","doi":"10.1080/10425170290019865","DOIUrl":null,"url":null,"abstract":"One of the eukaryotic polypeptide chain elongation factors, EF-1 g n i complex, is involved in polypeptide chain elongation via the GDP/GTP exchange activity of EF-1 f. In the complex, EF-1 n has been reported to be a major substrate for maturation promoting factor (MPF). Here, we present the cloning, sequencing and expression analysis of goldfish, Carassius auratus, EF-1 n from the goldfish ovary. The cloned cDNA was 1490 u bp in length and encoded 442 amino acids. The deduced amino acid sequence was highly homologous to EF-1 n from other species. Although, the phosphorylation site identified in Xenopus EF-1 n was not conserved in the goldfish homologue, phosphorylation analysis showed that the goldfish EF-1 n was phosphorylated by MPF. We concluded that EF-1 n is a substrate for MPF during oocyte maturation in goldfish.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"1 1","pages":"27 - 31"},"PeriodicalIF":0.0000,"publicationDate":"2002-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"15","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"DNA Sequence","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/10425170290019865","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 15
Abstract
One of the eukaryotic polypeptide chain elongation factors, EF-1 g n i complex, is involved in polypeptide chain elongation via the GDP/GTP exchange activity of EF-1 f. In the complex, EF-1 n has been reported to be a major substrate for maturation promoting factor (MPF). Here, we present the cloning, sequencing and expression analysis of goldfish, Carassius auratus, EF-1 n from the goldfish ovary. The cloned cDNA was 1490 u bp in length and encoded 442 amino acids. The deduced amino acid sequence was highly homologous to EF-1 n from other species. Although, the phosphorylation site identified in Xenopus EF-1 n was not conserved in the goldfish homologue, phosphorylation analysis showed that the goldfish EF-1 n was phosphorylated by MPF. We concluded that EF-1 n is a substrate for MPF during oocyte maturation in goldfish.