The large subunit of HIV-1 reverse transcriptase interacts with beta-actin.
AUTOR(ES)
Hottiger, M
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=306752Documentos Relacionados
- HIV-1 reverse transcriptase specifically interacts with the anticodon domain of its cognate primer tRNA.
- Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase.
- Structures of HIV-1 reverse transcriptase with pre- and post-translocation AZTMP-terminated DNA
- HIV-1 Reverse Transcriptase: a potential target for marine products
- Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA