Publications
2007
Henriet S, Sinck L, Bec G, Gorelick R J, Marquet R, Paillart J C
Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription Article de journal
Dans: Nucleic Acids Res, vol. 35, no. 15, p. 5141-5153, 2007, ISBN: 17660191, (1362-4962 (Electronic) Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't).
Résumé | Liens | BibTeX | Étiquettes: Amino Acyl/metabolism RNA, Capsid Proteins/metabolism DNA, gag/metabolism Gene Products, Human Immunodeficiency Virus, Human Immunodeficiency Virus vif Gene Products, MARQUET, PAILLART, Single-Stranded/biosynthesis Dimerization Gene Products, Transfer, Unité ARN, vif/*metabolism HIV-1/*genetics Molecular Chaperones/*metabolism RNA, Viral/*metabolism *Reverse Transcription Viral Proteins/metabolism gag Gene Products
@article{,
title = {Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription},
author = {S Henriet and L Sinck and G Bec and R J Gorelick and R Marquet and J C Paillart},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17660191},
isbn = {17660191},
year = {2007},
date = {2007-01-01},
journal = {Nucleic Acids Res},
volume = {35},
number = {15},
pages = {5141-5153},
abstract = {HIV-1 Vif (viral infectivity factor) is associated with the assembly complexes and packaged at low level into the viral particles, and is essential for viral replication in non-permissive cells. Viral particles produced in the absence of Vif exhibit structural defects and are defective in the early steps of reverse transcription. Here, we show that Vif is able to anneal primer tRNA(Lys3) to the viral RNA, to decrease pausing of reverse transcriptase during (-) strand strong-stop DNA synthesis, and to promote the first strand transfer. Vif also stimulates formation of loose HIV-1 genomic RNA dimers. These results indicate that Vif is a bona fide RNA chaperone. We next studied the effects of Vif in the presence of HIV-1 NCp, which is a well-established RNA chaperone. Vif inhibits NCp-mediated formation of tight RNA dimers and hybridization of tRNA(Lys3), while it has little effects on NCp-mediated strand transfer and it collaborates with nucleocapsid (NC) to increase RT processivity. Thus, Vif might negatively regulate NC-assisted maturation of the RNA dimer and early steps of reverse transcription in the assembly complexes, but these inhibitory effects would be relieved after viral budding, thanks to the limited packaging of Vif in the virions.},
note = {1362-4962 (Electronic)
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't},
keywords = {Amino Acyl/metabolism RNA, Capsid Proteins/metabolism DNA, gag/metabolism Gene Products, Human Immunodeficiency Virus, Human Immunodeficiency Virus vif Gene Products, MARQUET, PAILLART, Single-Stranded/biosynthesis Dimerization Gene Products, Transfer, Unité ARN, vif/*metabolism HIV-1/*genetics Molecular Chaperones/*metabolism RNA, Viral/*metabolism *Reverse Transcription Viral Proteins/metabolism gag Gene Products},
pubstate = {published},
tppubtype = {article}
}
1997
Rudinger J, Felden B, Florentz C, Giege R
Strategy for RNA recognition by yeast histidyl-tRNA synthetase Article de journal
Dans: Bioorg Med Chem, vol. 5, no. 6, p. 1001-1009, 1997, ISBN: 9222493, (0968-0896 Journal Article Review Review, Tutorial).
Résumé | Liens | BibTeX | Étiquettes: Amino Acyl/metabolism RNA, Base Sequence Histidine-tRNA Ligase/*metabolism Molecular Sequence Data RNA, FLORENTZ, Fungal/*metabolism RNA, Non-U.S. Gov't, Transfer, Unité ARN, Viral/metabolism Saccharomyces cerevisiae/*enzymology Substrate Specificity Support
@article{,
title = {Strategy for RNA recognition by yeast histidyl-tRNA synthetase},
author = {J Rudinger and B Felden and C Florentz and R Giege},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9222493},
isbn = {9222493},
year = {1997},
date = {1997-01-01},
journal = {Bioorg Med Chem},
volume = {5},
number = {6},
pages = {1001-1009},
abstract = {Histidine aminoacylation systems are of interest because of the structural diversity of the RNA substrates recognized by histidyl-tRNA synthetases. Among tRNAs participating in protein synthesis, those specific for histidine all share an additional residue at their 5'-extremities. On the other hand, tRNA-like domains at the 3'--termini of some plant viruses can also be charged by histidyl-tRNA synthetases, although they are not actors in protein synthesis. This is the case for the RNAs from tobacco mosaic virus and its satellite virus but also those of turnip yellow and brome mosaic viruses. All these RNAs have intricate foldings at their 3'-termini differing from that of canonical tRNAs and share a pseudoknotted domain which is the prerequisite for their folding into structures mimicking the overall L-shape of tRNAs. This paper gives an overview on tRNA identity and rationalizes the apparently contradictory structural and aminoacylation features of histidine-specific tRNAs and tRNA-like structures. The discussion mainly relies on histidylation data obtained with the yeast synthetase, but the conclusions are of a more universal nature. In canonical tRNA(His), the major histidine identity element is the 'minus' 1 residue, since its removal impairs histidylation and conversely its addition to a non-cognate tRNA(Asp) confers histidine identity to the transplanted molecule. Optimal expression of histidine identity depends on the chemical nature of the -1 residue and is further increased and/or modulated by the discriminator base N73 and by residues in the anticodon. In the viral tRNA-like domains, the major identity determinant -1 is mimicked by a residue from the single-stranded L1 regions of the different pseudoknots. The consequences of this mimicry for the function of minimalist RNAs derived from tRNA-like domains are discussed. The characteristics of the histidine systems illustrate well the view that the core of the amino acid accepting RNAs is a scaffold that allows proper presentation of identity nucleotides to their amino acid identity counterparts in the synthetase and that different types of scaffoldings are possible.},
note = {0968-0896
Journal Article
Review
Review, Tutorial},
keywords = {Amino Acyl/metabolism RNA, Base Sequence Histidine-tRNA Ligase/*metabolism Molecular Sequence Data RNA, FLORENTZ, Fungal/*metabolism RNA, Non-U.S. Gov't, Transfer, Unité ARN, Viral/metabolism Saccharomyces cerevisiae/*enzymology Substrate Specificity Support},
pubstate = {published},
tppubtype = {article}
}