THE LARGE SUBUNIT OF HIV-1 REVERSE-TRANSCRIPTASE INTERACTS WITH BETA-ACTIN

HIV-1 reverse transcriptase is a dimeric enzyme mainly involved in the replication of the viral genome. A filamentous phage cDNA expression library from human lymphocytes was used to select cellular proteins in teracting with HIV-1 reverse transcriptase. Affinity selections using the bacterially expressed monomeric large subunit of reverse transcrip tase (p66) yielded host beta-actin. This clone was expressed as glutat hione-S-transferase fusion protein which was identified by using a spe cific antibody against beta-actin. Furthermore we show that also the e ukaryotic beta-actin binds to either the large subunit of reverse tran scriptase or to the Pol precursor polyprotein in vitro. The reverse tr anscriptase/beta-actin interaction might be important for the secretio n of HIV-1 virions.