Richard V Farias

Rutgers, The State University of New Jersey, Нью-Брансуик, New Jersey, United States

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Publications (1)4.48 Total impact

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    ABSTRACT: A single polypeptide of the HIV-1 reverse transcriptase that reconstituted Mg2+-dependent RNase H activity has been made. Using molecular modeling, the construct was designed to encode the p51 subunit joined by a linker to the thumb (T), connection (C), and RNase H (R) domains of p66. This p51-G-TCR construct was purified from the soluble fraction of an Escherichia coli strain, MIC2067(DE3), lacking endogenous RNase HI and HII. The p51-G-TCR RNase H construct displayed Mg2+-dependent activity using a fluorescent nonspecific assay and showed the same cleavage pattern as HIV-1 reverse transcriptase (RT) on substrates that mimic the tRNA removal required for second-strand transfer reactions. The mutant E706Q (E478Q in RT) was purified under similar conditions and was not active. The RNase H of the p51-G-TCR RNase H construct and wild type HIV-1 RT had similar Kms for an RNA-DNA hybrid substrate and showed similar inhibition kinetics to two known inhibitors of the HIV-1 RT RNase H.
    Antimicrobial Agents and Chemotherapy 07/2011; 55(10):4735-41. DOI:10.1128/AAC.00658-11 · 4.48 Impact Factor

Publication Stats

4 Citations
4.48 Total Impact Points


  • 2011
    • Rutgers, The State University of New Jersey
      Нью-Брансуик, New Jersey, United States