Suppr超能文献

腺病毒2/5 E1a蛋白C末端的一个区域对于与一种细胞磷蛋白的结合是必需的,并且对于T24-ras介导的转化、肿瘤发生和转移的负调控很重要。

A region in the C-terminus of adenovirus 2/5 E1a protein is required for association with a cellular phosphoprotein and important for the negative modulation of T24-ras mediated transformation, tumorigenesis and metastasis.

作者信息

Boyd J M, Subramanian T, Schaeper U, La Regina M, Bayley S, Chinnadurai G

机构信息

Institute for Molecular Virology, St Louis University Medical Center, MO 63110.

出版信息

EMBO J. 1993 Feb;12(2):469-78. doi: 10.1002/j.1460-2075.1993.tb05679.x.

Abstract

We have examined a series of small deletion mutants within exon 2 of the adenovirus 2/5 E1A oncogene product, the 243R protein, for immortalization, ras cooperative transformation, tumorigenesis and metastasis. Compared with wild-type 243R, various deletion mutants located between residues 193 and 243 cooperated more efficiently with ras to induce large transformed foci of less adherent cells that were tumorigenic and metastatic. However, the greatest enhancement of transformation (comparable to that obtained with a deletion of the C-terminal 67 amino acids) was observed with a mutant carrying a deletion of residues 225-238. This mutant was also more defective in immortalization. These results suggest that this 14 amino acid region may contain a function that is important for immortalization and negative modulation of tumorigenesis and metastasis. To identify cellular proteins that may associate with the exon 2-coded region of E1A (C-terminal half) and modulate its transformation potential, we constructed a chimeric gene coding for the C-terminal 68 amino acids of E1a fused to bacterial glutathione-S-transferase (GST). This fusion protein was used to purify cellular proteins that bind to the C-terminal region of E1a. A 48 kDa cellular protein doublet (designated CtBP) was found to bind specifically to the GST-E1a C-terminal fusion protein as well as to bacterially expressed full-length E1a (243R) protein. It also co-immunoprecipitated specifically with E1a. Analysis of a panel of GST-E1a C-terminal mutant proteins indicates that residues 225-238 are required for the association of E1a and CtBP, suggesting a correlation between the association of CtBP and the immortalization and transformation modulating activities of exon 2. CtBP is a phosphoprotein and the level of phosphorylation of CtBP appears to be regulated during the cell cycle, suggesting that it may play an important role during cellular proliferation.

摘要

我们检测了腺病毒2/5 E1A癌基因产物(243R蛋白)外显子2内的一系列小缺失突变体,以研究其永生化、ras协同转化、肿瘤发生和转移情况。与野生型243R相比,位于第193至243位残基之间的各种缺失突变体与ras协同作用时,能更有效地诱导形成大量转化灶,这些转化灶中的细胞贴壁性较差,具有致瘤性和转移性。然而,在携带第225 - 238位残基缺失的突变体中观察到了最大程度的转化增强(与C末端67个氨基酸缺失时相当)。该突变体在永生化方面也存在更大缺陷。这些结果表明,这个14个氨基酸的区域可能包含对永生化以及肿瘤发生和转移的负调控很重要的功能。为了鉴定可能与E1A外显子2编码区(C末端一半)相互作用并调节其转化潜能的细胞蛋白,我们构建了一个嵌合基因,该基因编码与细菌谷胱甘肽 - S - 转移酶(GST)融合的E1a的C末端68个氨基酸。这种融合蛋白用于纯化与E1a C末端区域结合的细胞蛋白。发现一种48 kDa的细胞蛋白双峰(命名为CtBP)能特异性地与GST - E1a C末端融合蛋白以及细菌表达的全长E1a(243R)蛋白结合。它也能与E1a特异性地共免疫沉淀。对一组GST - E1a C末端突变蛋白的分析表明,E1a与CtBP的结合需要第

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d7/413230/3ed826f703b2/emboj00074-0105-a.jpg

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验