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. 1995 Mar 11;23(5):736–741. doi: 10.1093/nar/23.5.736

The large subunit of HIV-1 reverse transcriptase interacts with beta-actin.

M Hottiger 1, K Gramatikoff 1, O Georgiev 1, C Chaponnier 1, W Schaffner 1, U Hübscher 1
PMCID: PMC306752  PMID: 7535922

Abstract

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 interacting with HIV-1 reverse transcriptase Affinity selections using the bacterially expressed monomeric large subunit of reverse transcriptase (p66) yielded host beta-actin. This clone was expressed as glutathione-S-transferase fusion protein which was identified by using a specific antibody against beta-actin. Furthermore we show that also the eukaryotic beta-actin binds to either the large subunit of reverse transcriptase or to the Pol precursor polyprotein in vitro. The reverse transcriptase/beta-actin interaction might be important for the secretion of HIV-1 virions.

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