与SUMO结合酶Ubc9相互作用存在缺陷的乳头瘤病毒E1解旋酶突变体的特征分析
Characterization of papillomavirus E1 helicase mutants defective for interaction with the SUMO-conjugating enzyme Ubc9.
作者信息
Fradet-Turcotte Amélie, Brault Karine, Titolo Steve, Howley Peter M, Archambault Jacques
机构信息
Laboratory of Molecular Virology, Institut de Recherches Cliniques de Montréal and Department of Biochemistry, University of Montreal, 110 Pine Avenue West, Montreal, Quebec, Canada H2W 1R7.
出版信息
Virology. 2009 Dec 20;395(2):190-201. doi: 10.1016/j.virol.2009.09.020.
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 E1 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 E1 are not essential for nuclear accumulation of E1. These results suggest that the interaction of E1 with Ubc9 is not essential for its nuclear accumulation but, rather, depends on its oligomerization and binding to DNA and ATP.
来自牛乳头瘤病毒（BPV）和人乳头瘤病毒16型（HPV16）的E1解旋酶与Ubc9相互作用，以促进病毒基因组复制。我们报告称，HPV11 E1在体外和酵母双杂交系统中也与Ubc9相互作用。E1中参与寡聚化的残基（353 - 435）在体外足以与Ubc9结合，但在酵母中还需要起始点结合域和ATP酶结构域。先前已表明，BPV E1的核积累取决于其与Ubc9的相互作用以及赖氨酸514上的SUMO化修饰。相比之下，即使SUMO途径受到抑制，对Ubc9结合有缺陷的HPV11和HPV16 E1突变体仍保留在细胞核中。此外，我们发现BPV E1中的K514和HPV11 E1中的类似物K559对于E1的核积累并非必不可少。这些结果表明，E1与Ubc9的相互作用对于其核积累并非必不可少，而是取决于其寡聚化以及与DNA和ATP的结合。
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