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Nucleic Acids Research Advance Access originally published online on October 13, 2006
Nucleic Acids Research 2006 34(20):5764-5777; doi:10.1093/nar/gkl722
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Nucleic Acids Research, 2006, Vol. 34, No. 20 5764-5777
© 2006 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.

RNA

Characterization of a nucleocapsid-like region and of two distinct primer tRNALys,2 binding sites in the endogenous retrovirus Gypsy

Caroline Gabus, Roland Ivanyi-Nagy, Julien Depollier1, Alain Bucheton1, Alain Pelisson1 and Jean-Luc Darlix*

LaboRetro, Unité de Virologie Humaine INSERM, IFR 128, Ecole Normale Supérieure de Lyon, 46 Allée d'Italie, 69364 LYON Cedex 07, France 1 Institut de Génétique Humaine 141, rue de la Cardonille, 34396 MONTPELLIER Cedex 5, France

*To whom correspondence should be addressed. Tel: +33 4 72 72 81 69; Fax: +33 4 72 72 87 77; Email: Jean-Luc.Darlix{at}ens-lyon.fr

Received August 28, 2006. Revised September 18, 2006. Accepted September 18, 2006.

Mobile LTR-retroelements comprising retroviruses and LTR-retrotransposons form a large part of eukaryotic genomes. Their mode of replication and abundance favour the notion that they are major actors in eukaryote evolution. The Gypsy retroelement can spread in the germ line of the fruit fly Drosophila melanogaster via both env-independent and env-dependent processes. Thus, Gypsy is both an active retrotransposon and an infectious retrovirus resembling the gammaretrovirus MuLV. However, unlike gammaretroviruses, the Gypsy Gag structural precursor is not processed into Matrix, Capsid and Nucleocapsid (NC) proteins. In contrast, it has features in common with Gag of the ancient yeast TY1 retroelement. These characteristics of Gypsy make it a very interesting model to study replication of a retroelement at the frontier between ancient retrotransposons and retroviruses. We investigated Gypsy replication using an in vitro model system and transfection of insect cells. Results show that an unstructured domain of Gypsy Gag has all the properties of a retroviral NC. This NC-like peptide forms ribonucleoparticle-like complexes upon binding Gypsy RNA and directs the annealing of primer tRNALys,2 to two distinct primer binding sites (PBS) at the genome 5' and 3' ends. Only the 5' PBS is indispensable for cDNA synthesis in vitro and in Drosophila cells.


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