Protease-mediated maturation of M-PMV reverse transcriptase into a functional heterodimer.

ABSTRACT: Reverse transcriptase (RT) of retroviruses orchestrates viral replication, yet its structural diversity remains poorly understood. Well-studied RTs, such as those from HIV-1, murine leukemia virus, and avian myeloblastosis virus, were characterized decades ago, but less prominent retroviruses have escaped detailed analysis. Despite being discovered alongside HIV-1, the RT of Mason-Pfizer monkey virus (M-PMV) has resisted recombinant expression, leaving its properties unresolved. Here, we report the first detailed analysis of M-PMV RT, a betaretroviral enzyme previously thought challenging to obtain recombinantly. Using baculovirus-based expression in insect cells, we produced soluble full-length RT that, upon proteolytic maturation by the M-PMV protease, yielded a heterodimer composed of p

SUBMITTER: Kapisheva M 

PROVIDER: S-EPMC12817477 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature