Characterization of papillomavirus E1 helicase mutants defective for interaction with the SUMO-conjugating enzyme Ubc9

被引：12

作者：

Fradet-Turcotte, Amelie ^{[1
,2
]}

Brault, Karine ^{[3
]}

Titolo, Steve ^{[3
]}

Howley, Peter M. ^{[4
]}

Archambault, Jacques ^{[1
,2
]}

机构：

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

[2] Univ Montreal, Dept Biochem, Montreal, PQ H2W 1R7, Canada

[3] Boehringer Ingelheim Canada Ltd, Dept Biol Sci, Laval, PQ H7S 2G5, Canada

[4] Harvard Univ, Sch Med, Dept Pathol, Boston, MA 02115 USA

来源：

VIROLOGY | 2009年 / 395卷 / 02期

关键词：

Papillomavirus; E1; Ubc9; Yeast two-hybrid; Sumoylation; DNA replication; Oligomerization; DNA-binding; ATPase; Gam1; ADENOASSOCIATED VIRUS TYPE-2; POLYMERASE ALPHA-PRIMASE; LARGE T-ANTIGEN; DNA-REPLICATION; BINDING DOMAIN; FLUORESCENCE ANISOTROPY; PROTEIN BINDS; NUCLEAR-BODY; UBIQUITIN; IDENTIFICATION;

D O I：

10.1016/j.virol.2009.09.020

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The E1 helicase from BPV and HPV16 interacts with Ubc9 to facilitate viral genome replication. We report that HPV11 E1 also interacts with Ubc9 in vitro and in the yeast two-hybrid system. Residues in E1 involved in oligomerization (353-435) were sufficient for binding to Ubc9 in vitro, but the origin-binding and ATPase domains were additionally required in yeast. Nuclear accumulation of BPV El was shown previously to depend on its interaction with Ubc9 and sumoylation on lysine 514. In contrast, HPV11 and HPV16 E1 mutants defective for Ubc9 binding remained nuclear even when the SUMO pathway was inhibited. Furthermore, we found that K514 in BPV E1 and the analogous K559 in HPV11 El are not essential for nuclear accumulation of El. These results suggest that the interaction of El with Ubc9 is not essential for its nuclear accumulation but, rather, depends on its oligomerization and binding to DNA and ATP. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：190 / 201

页数：12

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