{"title":"鸡真核翻译起始因子-2β cDNA编码的鉴定","authors":"Kyra J. Sneesby, D. Crane, W. Murrell","doi":"10.3109/10425170109042051","DOIUrl":null,"url":null,"abstract":"A full length cDNA for the β subunit of chick (Gallus gallus) eukaryotic translation initiation factor-2 is described. This cDNA was isolated by screening a chick cDNA library with a probe derived via differential display of developing chick heart tissue. Up-regulated expression of eIF-2β mRNA was confirmed by reverse Northern dot blot analysis. eIF-2β, together with eIF-2α and eIF-2γ, comprise subunits of a complex that promotes the binding of methionyl-tRNA to ribosomes during the initiation of protein translation. The nucleotide sequence of the chick eIF-2β cDNA predicts a protein of 334 amino acids that has 95%, 93%, 56% and 37% sequence identity with rabbit, human, drosophila and yeast eIF-2β, respectively. The deduced eIF-2p protein contains a number of functional motifs and domains consistent with the putative function of this protein; these include a potential C2-C2 zinc-finger binding domain, three polylysine regions, and three acidic regions.","PeriodicalId":11381,"journal":{"name":"DNA Sequence","volume":"261 1","pages":"59 - 65"},"PeriodicalIF":0.0000,"publicationDate":"2001-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"Characterisation of a cDNA Encoding Chick Eukaryotic Translation Initiation Factor-2β\",\"authors\":\"Kyra J. Sneesby, D. Crane, W. Murrell\",\"doi\":\"10.3109/10425170109042051\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"A full length cDNA for the β subunit of chick (Gallus gallus) eukaryotic translation initiation factor-2 is described. This cDNA was isolated by screening a chick cDNA library with a probe derived via differential display of developing chick heart tissue. Up-regulated expression of eIF-2β mRNA was confirmed by reverse Northern dot blot analysis. eIF-2β, together with eIF-2α and eIF-2γ, comprise subunits of a complex that promotes the binding of methionyl-tRNA to ribosomes during the initiation of protein translation. The nucleotide sequence of the chick eIF-2β cDNA predicts a protein of 334 amino acids that has 95%, 93%, 56% and 37% sequence identity with rabbit, human, drosophila and yeast eIF-2β, respectively. The deduced eIF-2p protein contains a number of functional motifs and domains consistent with the putative function of this protein; these include a potential C2-C2 zinc-finger binding domain, three polylysine regions, and three acidic regions.\",\"PeriodicalId\":11381,\"journal\":{\"name\":\"DNA Sequence\",\"volume\":\"261 1\",\"pages\":\"59 - 65\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2001-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"DNA Sequence\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3109/10425170109042051\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"DNA Sequence","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3109/10425170109042051","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Characterisation of a cDNA Encoding Chick Eukaryotic Translation Initiation Factor-2β
A full length cDNA for the β subunit of chick (Gallus gallus) eukaryotic translation initiation factor-2 is described. This cDNA was isolated by screening a chick cDNA library with a probe derived via differential display of developing chick heart tissue. Up-regulated expression of eIF-2β mRNA was confirmed by reverse Northern dot blot analysis. eIF-2β, together with eIF-2α and eIF-2γ, comprise subunits of a complex that promotes the binding of methionyl-tRNA to ribosomes during the initiation of protein translation. The nucleotide sequence of the chick eIF-2β cDNA predicts a protein of 334 amino acids that has 95%, 93%, 56% and 37% sequence identity with rabbit, human, drosophila and yeast eIF-2β, respectively. The deduced eIF-2p protein contains a number of functional motifs and domains consistent with the putative function of this protein; these include a potential C2-C2 zinc-finger binding domain, three polylysine regions, and three acidic regions.