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莫洛尼鼠白血病病毒整合酶蛋白的一个中心半胱氨酸残基和HHCC结构域在功能性多聚化中的作用。

Implication of a central cysteine residue and the HHCC domain of Moloney murine leukemia virus integrase protein in functional multimerization.

作者信息

Donzella G A, Leon O, Roth M J

机构信息

Department of Biochemistry, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway 08854, USA.

出版信息

J Virol. 1998 Feb;72(2):1691-8. doi: 10.1128/JVI.72.2.1691-1698.1998.

Abstract

Moloney murine leukemia virus (M-MuLV) IN-IN protein interactions important for catalysis of strand transfer and unimolecular and bimolecular disintegration reactions were investigated by using a panel of chemically modified M-MuLV IN proteins. Functional complementation of an HHCC-deleted protein (Ndelta105) by an independent HHCC domain (Cdelta232) was severely compromised by NEM modification of either subunit. Productive Ndelta105 IN-DNA interactions with a disintegration substrate lacking a long terminal repeat 5'-single-stranded tail also required complementation by a functional HHCC domain. Virus encoding the C209A M-MuLV IN mutation exhibited delayed virion production and replication kinetics.

摘要

通过使用一组化学修饰的莫洛尼鼠白血病病毒(M-MuLV)整合酶(IN)蛋白,研究了对链转移催化以及单分子和双分子解体反应至关重要的M-MuLV IN-IN蛋白相互作用。独立的HHCC结构域(Cdelta232)对HHCC缺失蛋白(Ndelta105)的功能互补,因任一亚基的NEM修饰而严重受损。Ndelta105 IN与缺乏长末端重复序列5'-单链尾巴的解体底物之间有效的相互作用也需要功能性HHCC结构域的互补。编码C209A M-MuLV IN突变的病毒表现出延迟的病毒粒子产生和复制动力学。

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