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爱泼斯坦-巴尔病毒核蛋白2至少有两个介导自身缔合的N端结构域。

Epstein-Barr virus nuclear protein 2 has at least two N-terminal domains that mediate self-association.

作者信息

Harada S, Yalamanchili R, Kieff E

机构信息

Program in Virology and Department of Medicine, Channing Laboratory, Brigham and Women's Hospital and Harvard University, Boston, Massachusetts 02115, USA.

出版信息

J Virol. 2001 Mar;75(5):2482-7. doi: 10.1128/JVI.75.5.2482-2487.2001.

Abstract

Previous genetic and biochemical analyses have indicated that the Epstein-Barr virus EBNA-2 amino terminus is important for primary B-lymphocyte growth transformation and may be involved in self-association. We now report that EBNA-2 has at least two domains, amino acids 1 to 60 and 96 to 210, which independently mediate homotypic association, 1 to 60 with 1 to 60 and 96 to 210 with 96 to 210. EBNA-2 self-association is likely to be critical to the ability of EBNA-2 to interact simultaneously with multiple cellular transcription factors, coactivators, and histone acetyltransferases through its RBPJkappa binding and acidic activating domains.

摘要

先前的遗传学和生物化学分析表明,爱泼斯坦-巴尔病毒EBNA-2氨基末端对原发性B淋巴细胞生长转化很重要,可能参与自我缔合。我们现在报告EBNA-2至少有两个结构域,即氨基酸1至60和96至210,它们分别介导同型缔合,1至60与1至60缔合,96至210与96至210缔合。EBNA-2自我缔合可能对EBNA-2通过其RBPJκ结合域和酸性激活域同时与多种细胞转录因子、共激活因子和组蛋白乙酰转移酶相互作用的能力至关重要。

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