Identification of amino acid residues in HIV-1 reverse transcriptase that are critical for the proteolytic processing of Gag-Pol precursors

Hironori Nishitsuji, Masaru Yokoyama, Hironori Sato, Suguru Yamauchi, Hiroshi Takaku

Research output: Contribution to journalArticle

4 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)3372-3377
Number of pages6
JournalFEBS Letters
Volume585
Issue number21
DOIs
Publication statusPublished - 04-11-2011
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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