TY - JOUR
T1 - Identification of amino acid residues in HIV-1 reverse transcriptase that are critical for the proteolytic processing of Gag-Pol precursors
AU - Nishitsuji, Hironori
AU - Yokoyama, Masaru
AU - Sato, Hironori
AU - Yamauchi, Suguru
AU - Takaku, Hiroshi
N1 - Funding Information:
We thank Dr. I.S.Y. Chen for providing pNL4-3lucΔenv and Dr. H. Miyoshi for providing pMD.G-VSV-G. This work was supported by a Grant-in-Aid for AIDS research from the Ministry of Health, Labor, and Welfare, Japan, a Grant-in-Aid for High Technology Research (HTR) from the Ministry of Education, Science, Sports, and Culture , Japan, and a Grant from the Strategic Research Foundation Grant-aided Project for Private Universities from the Ministry of Education, Culture, Sport, Science, and Technology , Japan (MEXT).
PY - 2011/11/4
Y1 - 2011/11/4
N2 - 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.
AB - 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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U2 - 10.1016/j.febslet.2011.09.034
DO - 10.1016/j.febslet.2011.09.034
M3 - Article
C2 - 22004763
AN - SCOPUS:80255129389
SN - 0014-5793
VL - 585
SP - 3372
EP - 3377
JO - FEBS Letters
JF - FEBS Letters
IS - 21
ER -
