Abstract
Human immunodeficiency virus 1 reverse transcriptase (RT) purified from virions is composed of a similar to 51,000 M sub(r) polypeptide and a similar to 66,000 M sub(r) polypeptide. We prepared individual bacterial-recombinant RTs as the similar to 66,000 M sub(r) polypeptide (p66) or as the similar to 51,000 M sub(r) polypeptide (p51) and then conducted various in vitro protein-protein binding experiments. The results indicate that purified individual RT peptides p51 and p66 are capable of binding to form a 1:1 heterodimer and suggest that the central region of p66 is required for this subunit binding.