UNASSIGNED: @entity16757 ( @entity16757 ) of @entity2858 ) is synthesized and packaged into the virion as a part of the GagPol polyprotein. Mature @entity16757 is released by the action of viral protease. However, unlike other viral proteins, @entity16757 is subject to an internal cleavage event leading to the formation of two subunits in the virion: a @entity19490 subunit and a @entity4206 subunit that lacks the RNase H domain. We have previously identified RNase H to be an @entity2858 protein that has the potential to be a substrate for the N-end rule pathway, which is an ubiquitin-dependent proteolytic system in which the identity of the N-terminal @entity535 determines the half-life of a protein. Here we examined the importance of the N-terminal @entity535 residue of RNase H in the early life cycle of @entity2858 . We show that changing this residue to an @entity535 structurally different from the conserved residue leads to the degradation of @entity16757 and, in some cases, integrase in the virus particle and this abolishes infectivity. Using intravirion complementation and in vitro protease cleavage assays, we show that degradation of @entity16757 in RNase H N-terminal mutants occurs in the absence of active viral protease in the virion. Our results also indicate the importance of the RNase H N-terminal residue in the dimerization of @entity16757 subunits. IMPORTANCE: @entity2858 proteins are initially made as part of a polyprotein that is cleaved by the viral protease into the proteins that form the virus particle. We were interested in one particular protein, RNase H, that is cleaved from reverse transcriptase. In particular, we found that the first @entity535 of RNase H never varied in over 1,850 isolates of @entity2858 that we compared. When we changed the first @entity535 , we found that the reverse transcriptase in the virus was degraded. While other studies have implied that the viral protease can degrade mutant @entity16757 proteins, we show here that this may not be the case for our mutants. Our results suggest that the presence of active viral protease is not required for the degradation of @entity16757 in RNase H N-terminal mutants, suggesting a role for a cellular protease in this process.

The Nature of the N-Terminal @entity535 Residue of XXXX RNase H Is Critical for the Stability of Reverse Transcriptase in Viral Particles.

@entity2858 :: ('11676', 'Species') :: ['human immunodeficiency virus type 1 (HIV-1', 'HIV-1'] @entity535 :: ('CHEBI:33704', 'Chemical') :: ['amino acid'] @entity4206 :: ('8626', 'Gene') :: ['p51'] @entity19490 :: ('10714', 'Gene') :: ['p66'] @entity16757 :: ('MESH:D054038', 'Disease') :: ['Reverse transcriptase', 'RT']
@entity2858 :: (11676,Species) :: ['HIV-1']
