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Originally published In Press as doi:10.1074/jbc.M001371200 on April 13, 2000

J. Biol. Chem., Vol. 275, Issue 25, 19210-19217, June 23, 2000
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The Gag-like Protein of the Yeast Ty1 Retrotransposon Contains a Nucleic Acid Chaperone Domain Analogous to Retroviral Nucleocapsid Proteins*

Gaël CristofariDagger , Damien Ficheux§, and Jean-Luc DarlixDagger

From the Dagger  LaboRetro, Unité de Virologie Humaine, INSERM (412), Ecole Normale Supérieure de Lyon, 46 Allée d'Italie, 69364 Lyon Cedex 07, France and the § Institut de Biologie et Chimie des Protéines, 7 Passage du Vercors, 69367 Lyon, France

The reverse transcription process for retroviruses and retrotransposons takes place in a nucleocore structure in the virus or virus-like particle. In retroviruses the major protein of the nucleocore is the nucleocapsid protein (NC protein), which derives from the C-terminal region of GAG. Retroviral NC proteins are formed of either one or two CCHC zinc finger(s) flanked by basic residues and have nucleic acid chaperone and match-maker properties essential for virus replication. Interestingly, the GAG protein of a number of retroelements including Spumaviruses does not possess the hallmarks of retroviral GAGs and in particular lacks a canonical NC protein. In an attempt to search for a nucleic acid chaperone activity in this class of retroelements we used the yeast Ty1 retrotransposon as a model system. Results shows that the C-terminal region of Ty1 GAG contains a nucleic acid chaperone domain capable of promoting the annealing of primer tRNAiMet to the multipartite primer binding site, Ty1 RNA dimerization and initiation of reverse transcription. Moreover Ty1 RNA dimerization, in a manner similar to Ty3 but unlike retroviral RNAs, appears to be mediated by tRNAiMet. These findings suggest that nucleic acid chaperone proteins probably are general co-factors for reverse transcriptases.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. E-mail: Jean-Luc.Darlix@ens-lyon.fr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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