Thermal stressed human immunodeficiency virus type 1 nucleocapsid protein NCp7 maintains nucleic acid-binding activity
Thermal stressed human immunodeficiency virus type 1 nucleocapsid protein NCp7 maintains nucleic acid-binding activity
复制标题
热应激人类免疫缺陷病毒1型核衣壳蛋白NCp7保持核酸结合活性
DOI：
10.1016/j.bbrc.2020.03.167
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发表时间：
2020-06-04
影响因子：
3.1
通讯作者：
Wang, Ying
中科院分区：
文献类型：
--
作者：
Guo, Chao;Han, Jingwen;Wang, Ying
人类免疫缺陷病毒1型（HIV-1）的核衣壳蛋白（NC）是一种小的、高度碱性的核酸（NA）结合蛋白，具有两个CCHC锌指基序。在这项研究中，我们首次报告，据我们所知，热应激HIV-1 NCp 7保持NA结合活性。在100 ℃孵育60 min后，约41.3%的NCp 7保持可溶性，并且热处理的NCp 7保持其与HIV-1包装信号（Psi）和Psi的茎环3结合的能力。在高或非常高程度的序列占有率，NCp 7抑制第一链cDNA合成催化纯化的HIV-1逆转录酶，热处理NCp 7保持抑制。此外，EDTA处理和H23 K + H44 K双突变体的NCp 7抑制第一链cDNA的合成，表明在高NC：NA比的NCp 7的NA结合活性是独立于其锌指。这些结果可能有助于进一步研究NCp 7的结构稳定性和在病毒复制中的功能。(C)2020爱思唯尔公司All rights reserved.
The nucleocapsid protein (NC) of human immunodeficiency virus type 1 (HIV-1) is a small, highly basic nucleic acid (NA)-binding protein with two CCHC zinc-finger motifs. In this study, we report for the first time, to our knowledge, that thermal stressed HIV-1 NCp7 maintained NA-binding activity. About 41.3% of NCp7 remained soluble after incubated at 100 degrees C for 60 min, and heat-treated NCp7 maintained its abilities to bind to HIV-1 packaging signal (Psi) and the stem-loop 3 of the Psi. At high or very high degrees of sequence occupancy, NCp7 inhibited first-strand cDNA synthesis catalyzed by purified HIV-1 reverse transcriptase, and heat-treated NCp7 maintained the inhibition. Moreover, both EDTA-treated and H23K + H44K double mutant of NCp7 inhibited first-strand cDNA synthesis, demonstrating that the NA-binding activity of NCp7 at high NC:NA ratios is independent on its zinc-fingers. These results may benefit further investigations of the structural stability and function of NCp7 in viral replication. (C) 2020 Elsevier Inc. All rights reserved.