| Literature DB >> 29751015 |
Tatiana V Ilina1, Ryan L Slack2, John H Elder3, Stefan G Sarafianos4, Michael A Parniak5, Rieko Ishima6.
Abstract
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.Entities:
Keywords: HIV-1; RNase H; maturation; proteolysis; reverse transcriptase; tRNA
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Year: 2018 PMID: 29751015 PMCID: PMC5988984 DOI: 10.1016/j.jmb.2018.02.027
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469