Flexible Nature and Specific Functions of the HIV-1 Nucleocapsid Protein

被引：124

作者：

Darlix, Jean-Luc ^{[1
]}

Godet, Julien ^{[2
,3
]}

Ivanyi-Nagy, Roland ^{[4
]}

Fosse, Philippe ^{[5
]}

Mauffret, Olivier ^{[5
]}

Mely, Yves ^{[2
]}

机构：

[1] ENS Lyon, INSERM 758, LaboRetro, F-69364 Lyon, France

[2] CNRS, Fac Pharm, Lab Biophoton & Pharmacol, UMR 7213, F-67401 Illkirch Graffenstaden, France

[3] Strasbourg Univ Hosp, Med Informat & Biostat Dept, F-67000 Strasbourg, France

[4] Univ Oxford, Mol Parasitol Grp, Weatherall Inst Mol Med, Oxford OX3 9DS, England

[5] ENS Cachan, CNRS UMR8113 LBPA, F-94235 Cachan, France

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2011年 / 410卷 / 04期

关键词：

HIV-1; nucleocapsid protein; zinc fingers; intrinsic disorder; virus replication; IMMUNODEFICIENCY-VIRUS TYPE-1; DEPENDENT DNA POLYMERASE; FLUORESCENCE CORRELATION SPECTROSCOPY; RNA CHAPERONE PROTEINS; HIGH-AFFINITY BINDING; PACKAGING SIGNAL-PSI; ROUS SARCOMA VIRUS; REVERSE TRANSCRIPTION; STRAND TRANSFER; IN-VITRO;

D O I：

10.1016/j.jmb.2011.03.037

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

One salient feature of reverse transcription in retroviruses, notably in the human immunodeficiency virus type 1, is that it requires the homologous nucleocapsid (NC) protein acting as a chaperoning partner of the genomic RNA template and the reverse transcriptase, from the initiation to the completion of viral DNA synthesis. This short review on the NC protein of human immunodeficiency virus type 1 aims at briefly presenting the flexible nature of NC protein, how it interacts with nucleic acids via its invariant zinc fingers and flanking basic residues, and the possible mechanisms that account for its multiple functions in the early steps of virus replication, notably in the obligatory strand transfer reactions during viral DNA synthesis by the reverse transcriptase enzyme. (C) 2011 Elsevier Ltd. All rights reserved.

引用

页码：565 / 581

页数：17

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