摘要
泛素介导的泛素-蛋白酶体通路(Ubiquitin_proteasomepathway,UPP)是真核细胞内依赖ATP的非溶酶体蛋白质降解途径,该途径对细胞内蛋白的选择性降解起着重要作用。设计一对简并引物,从棉铃虫Helicoverpaarmigera卵巢细胞Ha831中克隆了泛素基因的编码区,GenBank登录号AY456195。序列分析表明,该编码区的长度为228bp,编码76个氨基酸、其编码蛋白的相对分子质量为8560,等电点为6 56。同源性比较发现,棉铃虫泛素基因与其他真核生物泛素基因在氨基酸水平上具有96%以上的相似性,而与棉铃虫核多角体病毒泛素的相似性为76%,所有已知的泛素关键功能位点在该泛素蛋白中均保守存在。
Ubiquitin plays a very important role in regulated non_lysosomal ATP dependent protein degradation. The coding sequence of Helicoverpa armigera ubiquitin gene was isolated (GenBank Accession No.AY456195). The length of this ORF is 228 bp, encoding a protein with Mr of 8 560 and isoelectric point of 6.56. Multiple sequence alignment indicated that H. armigera ubiquitin is very similar to the homologous proteins of other eukaryotic species and it has more than 96% identity with other eukaryotic ubiquitins and 76% with Helicoverpa armigera single nucleopolyhedrovirus (HaSPV) ubiquitin at amino acid level. All known key_functional sites are still existed in H.armigera ubiquitin.
出处
《中山大学学报(自然科学版)》
CAS
CSCD
北大核心
2005年第1期61-64,共4页
Acta Scientiarum Naturalium Universitatis Sunyatseni
基金
国家重点基础规划"973"资助项目(G2000016209)
中山大学青年教师启动基金资助项目