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  • Title: Identification of amino acid residues in HIV-1 reverse transcriptase that are critical for the proteolytic processing of Gag-Pol precursors.
    Author: Nishitsuji H, Yokoyama M, Sato H, Yamauchi S, Takaku H.
    Journal: FEBS Lett; 2011 Nov 04; 585(21):3372-7. PubMed ID: 22004763.
    Abstract:
    The efficient processing of human immunodeficiency virus type 1 Gag-Pol requires not only protease activity but also specific reverse transcriptase (RT) and integrase sequences. However, the critical amino acid residues of the HIV-1 Pol gene involved in protease-mediated Gag-Pol processing have not been precisely defined. Here, we found that the substitution of Thr-128 or Tyr-146 with Ala markedly impaired the proteolytic processing of the MA/CA, p66/p51 and RT/IN sites but did not affect the normal processing of other sites. Moreover, a Thr-128 or Tyr-146 mutation in RT abolished RT dimerization in vitro. These results suggest that Thr-128 and Tyr-146 within the RT region play important roles in protease-mediated Gag-Pol processing.
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