与CBP/p300相互作用使1型牛乳头瘤病毒E6癌蛋白能够下调由p53介导的CBP/p300依赖性反式激活作用。

Interaction with CBP/p300 enables the bovine papillomavirus type 1 E6 oncoprotein to downregulate CBP/p300-mediated transactivation by p53.

作者信息

Zimmermann Holger, Koh Choon-Heng, Degenkolbe Roland, O'Connor Mark J, Müller Andreas, Steger Gertrud, Chen Jason J, Lui Yun, Androphy Elliot, Bernard Hans-Ulrich

机构信息

Laboratory for Papillomavirus Biology, Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609, Republic of Singapore1.

Institut für Virologie der Universität zu Köln, Cologne, Germany2.

出版信息

J Gen Virol. 2000 Nov;81(Pt 11):2617-2623. doi: 10.1099/0022-1317-81-11-2617.

DOI:10.1099/0022-1317-81-11-2617

PMID:11038372

Abstract

The E6 oncoprotein of bovine papillomavirus type 1 (BPV-1) can transform cells independently of p53 degradation. The precise mechanisms underlying this transformation are not yet completely understood. Here it is shown that BPV-1 E6 interacts with CBP/p300 in the same way as described for the E6 proteins of oncogenic human papillomaviruses. This interaction results in an inhibition of the transcriptional coactivator function of CBP/p300 required by p53 and probably by other transcription factors. The comparison of the CBP/p300-binding properties of BPV-1 E6 mutants previously characterized in transcription and transformation studies suggests (i) that the E6-CBP/p300 interaction may be necessary, but not sufficient, for cell transformation, and (ii) that the transcriptional activator function, inherent to the E6 protein, is not derived from forming a complex with CBP/p300.

摘要

1型牛乳头瘤病毒（BPV-1）的E6癌蛋白可独立于p53降解而转化细胞。这种转化背后的确切机制尚未完全明了。本文表明，BPV-1 E6与CBP/p300相互作用的方式与致癌性人乳头瘤病毒的E6蛋白的相关描述相同。这种相互作用导致p53以及可能其他转录因子所需的CBP/p300转录共激活因子功能受到抑制。对先前在转录和转化研究中表征的BPV-1 E6突变体的CBP/p300结合特性进行比较表明：（i）E6-CBP/p300相互作用对于细胞转化可能是必要的，但并不充分；（ii）E6蛋白固有的转录激活功能并非源自与CBP/p300形成复合物。