Publications
2008
Lemay J, Maidou-Peindara P, Cancio R, Ennifar E, Coadou G, Maga G, Rain J C, Benarous R, Liu L X
AKAP149 binds to HIV-1 reverse transcriptase and is involved in the reverse transcription Journal Article
In: J Mol Biol, vol. 383, no. 4, pp. 783-796, 2008, ISBN: 18786546, (1089-8638 (Electronic) Journal Article Research Support, Non-U.S. Gov't).
Abstract | Links | BibTeX | Tags: DUMAS A Kinase Anchor Proteins/chemistry/genetics/*metabolism Amino Acid Sequence Animals Binding Sites Cell Line HIV Reverse Transcriptase/chemistry/genetics/*metabolism HIV-1/enzymology/genetics Humans Models, ENNIFAR, Molecular Molecular Sequence Data Mutagenesis Protein Binding Protein Structure, Tertiary RNA Interference Recombinant Fusion Proteins/genetics/metabolism Reverse Transcription/*physiology Two-Hybrid System Techniques Virion/metabolism Virus Replication/physiology, Unité ARN
@article{,
title = {AKAP149 binds to HIV-1 reverse transcriptase and is involved in the reverse transcription},
author = {J Lemay and P Maidou-Peindara and R Cancio and E Ennifar and G Coadou and G Maga and J C Rain and R Benarous and L X Liu},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18786546},
isbn = {18786546},
year = {2008},
date = {2008-01-01},
journal = {J Mol Biol},
volume = {383},
number = {4},
pages = {783-796},
abstract = {Like all retroviruses, human immunodeficiency virus type 1 (HIV-1) undergoes reverse transcription during its replication cycle. The cellular cofactors potentially involved in this process still remain to be identified. We show here that A-kinase anchoring protein 149 (AKAP149) interacts with HIV-1 reverse transcriptase (RT) in both the yeast two-hybrid system and human cells. The AKAP149 binding site has been mapped to the RNase H domain of HIV-1 RT. AKAP149 silencing by RNA interference in HIV-1-infected cells inhibited viral replication at the reverse transcription step. We selected single-point mutants of RT defective for AKAP149 binding and demonstrated that mutant G462R, despite retaining significant intrinsic RT activity in vitro, failed to carry out HIV-1 reverse transcription correctly in infected cells. This suggests that the interaction between RT and AKAP149 in infected cells may play an important role in HIV-1 reverse transcription.},
note = {1089-8638 (Electronic)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {DUMAS A Kinase Anchor Proteins/chemistry/genetics/*metabolism Amino Acid Sequence Animals Binding Sites Cell Line HIV Reverse Transcriptase/chemistry/genetics/*metabolism HIV-1/enzymology/genetics Humans Models, ENNIFAR, Molecular Molecular Sequence Data Mutagenesis Protein Binding Protein Structure, Tertiary RNA Interference Recombinant Fusion Proteins/genetics/metabolism Reverse Transcription/*physiology Two-Hybrid System Techniques Virion/metabolism Virus Replication/physiology, Unité ARN},
pubstate = {published},
tppubtype = {article}
}