Nucleic Acids Research Advance Access originally published online on July 26, 2007
Nucleic Acids Research 2007 35(15):5141-5153; doi:10.1093/nar/gkm542
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Nucleic Acids Research, 2007, Vol. 35, No. 15 5141-5153
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription
1Architecture et Réactivité de l’ARN, Université Louis Pasteur, CNRS, IBMC, 15 rue René Descartes, 67084, Strasbourg cedex, France and 2AIDS Vaccine Program, SAIC-Frederick Inc., NCI-Frederick, P.O. Box B, Frederick, MD, USA
*To whom correspondence should be addressed. Tel: +33 0 3 88 41 70 35; Fax: +33 0 3 88 60 22 18; Email: jc.paillart{at}ibmc.u-strasbg.fr Correspondence may also be addressed to Roland Marquet. Tel: +33 0 3 88 41 70 54; Fax: +33 0 3 88 60 22 18; Email: r.marquet{at}ibmc.u-strasbg.fr
Received June 7, 2007. Revised July 2, 2007. Accepted July 3, 2007.
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 tRNALys3 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 tRNALys3, 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.
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