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Volume 271, Number 52, Issue of December 27, 1996 pp. 33686-33692
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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NCp7 Activates HIV-1_Lai RNA Dimerization by Converting a Transient Loop-Loop Complex into a Stable Dimer

(Received for publication, May 28, 1996, and in revised form, September 18, 1996)

From Unité de Biochimie, URA 147 CNRS, 39 rue Camille Desmoulins, Institut Gustave Roussy, 94805 Villejuif, France and ^§ Département de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, 4 avenue de l'Observatoire, 75006 Paris, France

Nucleocapsid protein 7 (NCp7), the human immunodeficiency virus type 1 (HIV-1) nucleocapsid protein, was shown to strongly potentiate the dimerization of the retroviral genomic RNA. This process involves the interaction of two retroviral RNA monomer subunits near their 5-ends. A region located upstream from the splice donor site was recently identified as being responsible for the formation of dimeric HIV-1 RNA. This region appeared to be confined within a stem-loop structure, with an autocomplementary sequence in the loop. In an in vitro study of spontaneous dimer formation, we reported that the 77-402 RNA transcript forms two distinct dimers differing in their thermostability: D37 and D55. We identified D37 as a "kissing" complex structure, formed via a loop-loop interaction between the two monomers, and D55 as a double stranded structure involving all nucleotides of the stem-loop via canonical base pairing. In this report, we have characterized the role of NCp7 in the HIV-1_Lai RNA dimerization process by using in vitro dimerization assays with RNA transcripts of different lengths and dimer thermal dissociation. Our results show that the nucleocapsid protein NCp7 activates RNA dimerization very likely through interaction with the kissing complex and converts it into a stable dimer. Furthermore, this NCp7-promoted conversion only occurs if the 240-280 stem-loop structure is present in HIV-1_Lai RNA molecules and contains the autocomplementary G²⁵⁷CGCGC²⁶² sequence. This study suggests that, under physiological conditions, an NCp7-mediated RNA conformational change is involved in the maturation of the HIV-1 RNA dimer.

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