Effect of tRNA on the Maturation of HIV-1 Reverse Transcriptase

JOURNAL OF MOLECULAR BIOLOGY

卷:430

Article

Ilina, Tatiana V.^1,2  Slack, Ryan L.¹  Elder, John H.³  Sarafianos, Stefan G.⁴  Parniak, Michael A.²  Ishima, Rieko¹ 

[1] Univ Pittsburgh, Sch Med, Dept Struct Biol, Room 1037,Biomed Sci Tower 3,3501 Fifth Ave, Pittsburgh, PA 15260 USA

[2] Univ Pittsburgh, Sch Med, Dept Microbiol & Mol Genet, Pittsburgh, PA 15219 USA

[3] Scripps Res Inst, Dept Immunol & Microbiol, La Jolla, CA 92037 USA

[4] Emory Univ, Sch Med, Dept Pediat, Lab Biochem Pharmacol, Atlanta, GA 30322 USA

关键词: HIV-1;    proteolysis;    maturation;    tRNA;    reverse transcriptase;    RNase H;   

DOI  :  10.1016/j.jmb.2018.02.027

来源: Elsevier

【 摘 要 】

The mature HIV-1 reverse transcriptase is a heterodimer that comprises 66 kDa (p66) and 51 kDa (p51) subunits. The latter is formed by HIV-1 protease-catalyzed removal of a C-terminal ribonuclease H domain from a p66 subunit. This proteolytic processing is a critical step in virus maturation and essential for viral infectivity. Here, we report that tRNA significantly enhances in vitro processing even at a substoichiometric tRNA:p66/p66 ratio. Other double-stranded RNAs have considerably less pronounced effect. Our data support a model where interaction of p66/p66 with tRNA introduces conformational asymmetry in the two subunits, permitting specific proteolytic processing of one p66 to provide the mature RT p66/p51 heterodimer. 2018 Elsevier Ltd. (C) All rights reserved.

【 授权许可】

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