Anticodon-like binding of the HIV-1 tRNA-like element to human lysyl-tRNA synthetase.

ABSTRACT: A critical step in the HIV-1 lifecycle involves reverse transcription of the viral genomic RNA (gRNA). Human tRNA^Lys3 serves as a primer for transcription initiation and is selectively enriched in virus particles. Human lysyl-tRNA synthetase (hLysRS) is also packaged into virions. Recently, a tRNA-like element (TLE) within the HIV-1 gRNA was shown to mimic the global tRNA fold and bind competitively to hLysRS, suggesting a mechanism of tRNA targeting to the primer binding site (PBS) and release from the synthetase. Here, we use NMR to investigate hLysRS anticodon-binding domain (ACB) binding to six RNA oligonucleotides, including a hairpin derived from the HIV-1 gRNA TLE. We show that ACB interacts with submicromolar affinity to U-rich RNA oligonucleotides-the tRNA^Lys3

SUBMITTER: Liu S 

PROVIDER: S-EPMC5113203 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature