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首页> 外文期刊>Journal of Molecular Biology >HPV oncoprotein E6 is a structure-dependent DNA-binding protein that recognizes four-way junctions.
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HPV oncoprotein E6 is a structure-dependent DNA-binding protein that recognizes four-way junctions.

机译：HPV癌蛋白E6是一种结构依赖性的DNA结合蛋白，可识别四向连接。

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摘要

E6 is an oncoprotein implicated in cervical cancers, produced by "high-risk" human papillomaviruses. E6 is thought to promote tumorigenesis by stimulating cellular degradation of the tumour suppressor p53, but it might display other activities. Sequence similarity was recently detected between E6 and endonuclease VII, a protein of phage T4 that recognizes and cleaves four-way DNA junctions. Here, we purified recombinant E6 proteins and demonstrated that high-risk E6 s bind selectively to four-way junctions in a structure-dependent manner. Several residues in the C-terminal zinc-binding domain, the region of E6 similar to endonuclease VII, are necessary for the junction-binding activity. E6 binds to the junction as a monomer. Comparative electrophoresis shows that E6-bound junctions migrate in an extended square conformation. Magnesium inhibits the electrophoretic migration of the complexes but does not seem to influence their formation at equilibrium. This work is the first demonstration of specific binding of purified active E6 to a well-characterized DNA ligand, and suggests new modes of action of E6 in oncogenesis. Copyright 2000 Academic Press.
机译：E6是一种与宫颈癌有关的癌蛋白，由“高危”人类乳头瘤病毒产生。 E6被认为通过刺激肿瘤抑制因子p53的细胞降解来促进肿瘤发生，但是它可能表现出其他活性。最近在E6和核酸内切酶VII（一种识别并切割四向DNA连接的噬菌体T4蛋白）之间检测到了序列相似性。在这里，我们纯化了重组E6蛋白，并证明了高危E6以结构依赖性方式选择性地结合到四向接头。 C-末端锌结合结构域中的几个残基，即E6与核酸内切酶VII相似的区域，对于结合结合活性是必需的。 E6以单体形式结合到连接处。比较电泳显示，E6结合的结以扩展的正方形构象迁移。镁抑制复合物的电泳迁移，但似乎不影响其在平衡时的形成。这项工作是首次证明纯化的活性E6与特征明确的DNA配体的特异性结合，并提出了E6在肿瘤发生中的新作用方式。版权所有2000学术出版社。

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