Active site mutagenesis of the AIDS virus protease and its alleviation by trans complementation.

摘要: Replacement of the putative active site Asp residue cloned HIV-1 protease with Ala yields a molecule incapable autocatalytic processing. Similarly, protease/reverse transcriptase and transcriptase/endonuclease polyproteins containing same mutation accumulate as enzymatically inert polyproteins. Introduction second, wild-type, copy in trans alleviates this defect, leading case individually to cleavage mutant protein, polyprotein mutants release reverse endonuclease polypeptides, former which recover enzymatic activity. In related experiments, similar inhibition trans-complementation genetically engineered gag--protease fusion protein was observed.