The V protein of the paramyxovirus SV5 interacts with damage-specific DNA binding protein
The V protein of the paramyxovirus SV5 interacts with damage-specific DNA binding protein
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DOI：
10.1006/viro.1998.9317
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发表时间：
1998-09-15
期刊：
影响因子：
3.7
通讯作者：
Lamb, RA
中科院分区：
文献类型：
--
作者：
Lin, GY;Paterson, RG;Lamb, RA
猴副流感病毒5型（SV 5）V/P基因编码两种蛋白：V和磷蛋白P。V和P蛋白的氨基共末端为164个残基，但它们具有独特的羧基末端。V的独特羧基末端含有七个半胱氨酸残基，类似于锌指，并结合两个锌原子。在谷胱甘肽-S-转移酶（GST）-融合蛋白选择细胞裂解物试验中，发现GST-V蛋白与损伤特异性DNA结合蛋白（DDB）的127-kDa亚基（DDB 1）[也称为UV损伤DNA结合蛋白（UV-DDB）、着色性干皮病E组结合因子（XPE-BF）和B型肝炎病毒X相关蛋白1（XAP-1）]相互作用。一个互惠的GST-DDB 1融合蛋白的选择试验表明，SV 5感染的细胞裂解物的DDB 1和V相互作用，并发现，V和DDB 1可以从SV 5感染的细胞或从细胞表达V和DDB 1使用牛痘病毒T7表达系统免疫共沉淀。V和DDB 1的相互作用涉及V的羧基末端结构域，因为V羧基末端结构域的缺失或锌结合结构域中的半胱氨酸残基（C189、C193、C205、C207、C210、C214和C217）被丙氨酸取代能够破坏与DDB 1的结合。在使用体外转录和翻译的DDB 1的GST融合蛋白选择试验中，还发现腮腺炎病毒、人副流感病毒2型（hPIV 2）和麻疹病毒的V蛋白与DDB 1相互作用。(C)北京：科学出版社.
The simian parainfluenza virus 5 (SV5) V/P gene encodes two proteins: V and the phosphoprotein P. The V and P proteins are amino coterminal for 164 residues, but they have unique carboxyl termini. The unique carboxyl terminus of V contains seven cysteine residues, resembles a zinc finger, and binds two atoms of zinc. In a glutathione-S-transferase (GST)-fusion protein selection of cell lysate assay, the GST-V protein was found to interact with the 127-kDa subunit (DDB1) of the damage-specific DNA binding protein (DDB) [also known as UV-damaged DNA binding protein (UV-DDB), xeroderma pigmentosum group E binding factor (XPE-BF), and the hepatitis B virus X-associated protein 1 (XAP-1)]. A reciprocal GST-DDB1 fusion protein selection assay of SVS-infected cell lysates showed that DDB1 and V interact, and it was found that V and DDB1 could be coimmunoprecipitated from SV5-infected cells or from cells expressing V and DDB1 using the vaccinia virus T7 expression system. The interaction of V and DDB1 involves the carboxyl-terminal domain of V in that either deletion of the V carboxyl-terminal domain or substitution of the cysteine residues (C189, C193, C205, C207, C210, C214, and C217) in the zinc-binding domain with alanine was able to disrupt binding to DDB1. The V proteins of the mumps virus, human parainfluenza virus 2 (hPIV2), and measles virus have also been found to interact with DDB1 in GST-fusion protein selection assays using in vitro transcribed and translated DDB1. (C) 1998 Academic Press.