Retroviral nucleocapsid proteins display nonequivalent levels of nucleic acid chaperone activity期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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Retroviral nucleocapsid proteins display nonequivalent levels of nucleic acid chaperone activity

Authors:	Stewart-Maynard Kristen M Cruceanu Margareta Wang Fei Vo My-Nuong Gorelick Robert J Williams Mark C Rouzina Ioulia Musier-Forsyth Karin

Institution:	Department of Chemistry, The Ohio State University, 100 W 18th Ave., Columbus, OH 43210, USA.

Abstract:	Human immunodeficiency virus type 1 (HIV-1) nucleocapsid protein (NC) is a nucleic acid chaperone that facilitates the remodeling of nucleic acids during various steps of the viral life cycle. Two main features of NC's chaperone activity are its abilities to aggregate and to destabilize nucleic acids. These functions are associated with NC's highly basic character and with its zinc finger domains, respectively. While the chaperone activity of HIV-1 NC has been extensively studied, less is known about the chaperone activities of other retroviral NCs. In this work, complementary experimental approaches were used to characterize and compare the chaperone activities of NC proteins from four different retroviruses: HIV-1, Moloney murine leukemia virus (MLV), Rous sarcoma virus (RSV), and human T-cell lymphotropic virus type 1 (HTLV-1). The different NCs exhibited significant differences in their overall chaperone activities, as demonstrated by gel shift annealing assays, decreasing in the order HIV-1 ~ RSV > MLV
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