| Literature DB >> 8794372 |
N Almog1, R Roller, G Arad, L Passi-Even, M A Wainberg, M Kotler.
Abstract
Human immunodeficiency virus type 1 (HIV-1) protease (PR) and p6(Pol) are translated as part of the Gag-Pol polyprotein after a ribosomal frameshift. PR is essential to virus replication and is responsible for cleaving Gag and Gag-Pol precursors, but the role of p6(Pol) in HIV-1 infection is poorly understood. Here, we report that (i) PR is present in mature HIV-1 virions primarily as a p6(Pol)-PR fusion protein; (ii) HIV-1 PR cleaves viral precursor proteins expressed in bacterial cells at the Phe-Leu bond (positions 1639 to 1642) located at the junction of the NC and p6(Pol) proteins, releasing the p6(Pol)-PR fusion protein; and (iii) purified p6(Pol)-PR fusion protein undergoes autocleavage in vitro at at least three sites.Entities:
Mesh:
Substances:
Year: 1996 PMID: 8794372 PMCID: PMC190778
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103