%0 Journal Article
%T HuR interacts with human immunodeficiency virus type 1 reverse transcriptase, and modulates reverse transcription in infected cells
%A Julie Lemay
%A Priscilla Maidou-Peindara
%A Thomas Bader
%A Eric Ennifar
%A Jean-Christophe Rain
%A Richard Benarous
%A Lang Liu
%J Retrovirology
%D 2008
%I BioMed Central
%R 10.1186/1742-4690-5-47
%X HIV-1 reverse transcriptase (RT) is a DNA- and RNA-dependent DNA polymerase responsible for converting the virion ssRNA genome into a dsDNA genome once the virus has entered the cell [1]. HIV-1 RT also displays RNA degradation activity (RNase H), independent of its polymerase activities. Both activities are essential for the reverse transcription process in vivo.HIV-1 reverse transcriptase is incorporated into virions, during their assembly, as part of the Gag-Pol precursor. It is processed into two subunits by the viral protease, during particle maturation, after budding. The p66 subunit includes domains responsible for the RNase H and DNA polymerase activities, whereas the p51 subunit bears only the polymerase domain. The two subunits dimerize within the viral particle, and form the p66/p51 heterodimer, the active form of the enzyme [2]. Reverse transcription occurs essentially in the cytoplasm once the virus has entered the cell. It is mediated by a complex formed by two copies of the viral RNA, associated viral proteins, including RT, and, presumably, cellular proteins that have yet to be characterized. This reverse transcription complex (RTC) is gradually transformed into the preintegration complex (PIC), during its progressive migration to the nucleus. The PIC is responsible for ensuring the integration of the proviral genomic DNA generated by reverse transcription into the host genome (recently reviewed in [3]).Recent studies point towards the importance of cellular co-factors for an efficient reverse transcription of HIV-1 in vivo [4,5]. However, the cellular factors involved in this reaction have not yet been identified. Moreover, there have been very few reports of cellular proteins interacting with HIV-1 RT. Hottiger et al. showed that the HIV-1 p66 monomer interacts directly with beta-actin [6]. Olova et al. have shown that eRF1 interacts directly with the reverse transcriptase of the murine retrovirus, M-MuLV [7], but not with HIV-1 RT. We searched for
%U http://www.retrovirology.com/content/5/1/47