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

Hottiger, M.
Gramatikoff, K.
Georgiev, O.
Schaffner, W.
Hubscher, U.
Published in Nucleic Acids Research. 1995, vol. 23, no. 5, p. 736-741
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.
Keywords Actins/ metabolismAnimalsBase SequenceCattleDNA PrimersDNA, ComplementaryGene Products, gag/metabolismGlutathione Transferase/metabolismHIV Reverse TranscriptaseHIV-1/ enzymologyHumansMolecular Sequence DataProtein BindingProtein Precursors/metabolismProtein Processing, Post-TranslationalRNA-Directed DNA Polymerase/ metabolismRecombinant Fusion Proteins/metabolismgag Gene Products, Human Immunodeficiency Viruspol Gene Products, Human Immunodeficiency Virus
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PMID: 7535922
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