Genetic analysis of the E2 transactivation domain dimerization interface from bovine papillomavirus type 1

被引：7

作者：

Gagnon, David ^{[1
,2
]}

Senechal, Helene ^{[1
,2
]}

D'Abramo, Claudia M. ^{[1
,2
]}

Alvarez, Jennifer ^{[1
,2
]}

McBride, Alison A. ^{[3
]}

Archambault, Jacques ^{[1
,2
]}

机构：

[1] Inst Rech Clin Montreal, Mol Virol Lab, Montreal, PQ H2W 1R7, Canada

[2] Univ Montreal, Dept Biochem, Montreal, PQ H3C 3J7, Canada

[3] NIAID, Viral Dis Lab, NIH, Bethesda, MD 20892 USA

来源：

VIROLOGY | 2013年 / 439卷 / 02期

基金：

加拿大健康研究院;

关键词：

BPV1; E2; Transactivation; DNA replication; Transactivation domain; Dimer; Dimerization; Redox; High-throughput assay; Protein interface; TRANSCRIPTIONAL ACTIVATION; DNA-REPLICATION; CRYSTAL-STRUCTURE; VIRAL-DNA; PROTEIN; GENOME; BRD4; COMPLEX; BINDING; PATHOGENESIS;

D O I：

10.1016/j.virol.2013.02.012

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The bovine papillomavirus type 1 (BPV1) E2 protein binds as a dimer to the viral genome to promote its transcription, replication and maintenance in keratinocytes. Although BPV1 E2 dimerizes primarily through its DNA-binding domain, it was shown previously that its transactivation domain (TAD) can also dimerize in vitro through formation of a disulfide bond between cysteine 57 (C57) of adjacent monomers and of an ion pair between arginine 172 (R172) and aspartic acid 175 (D175). The function of this TAD dimerization interface in vivo remains unknown. Here, we report the effects of substituting C57, R172 and D175 by alanine on the transactivation activity of BPV E2 as well as on its ability to support viral DNA replication using a novel luciferase-based assay. Results for this mutational analysis suggest that the TAD dimerization interface is not essential for either process but may contribute to the DNA replication activity of BPV1 E2. (C) 2013 Elsevier Inc. All rights reserved.

引用

页码：132 / 139

页数：8

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