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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
- Authors
Nishitsuji, Hironori; Yokoyama, Masaru; Sato, Hironori; Yamauchi, Suguru; Takaku, Hiroshi
- Abstract
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. Structured summary of protein interactions: RT and RT physically interact by cross-linking study (View interaction: 1, 2, 3). CK2 alpha phosphorylates RT by protein kinase assay (View interaction).
- Subjects
AMINO acids; REVERSE transcriptase; HIV; PROTEOLYTIC enzymes; DIMERIZATION; PROTEIN kinases
- Publication
FEBS Letters, 2011, Vol 585, Issue 21, p3372
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2011.09.034