Mutations in HIV-1 reverse transcriptase cause misfolding and miscleavage by the viral protease

Both subunits contribute to the stability of RT. In general, the differences in stability between the mutants and WT were greater if the mutation was in p51 rather than p66. Expressing the Pol polyprotein containing the RT mutants in Escherichia coli produced results similar to what was seen in virions; the mutant RTs were misfolded and/or degraded at 37 °C, but were better folded and processed at 30 °C.