PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1

Derrington, E; Gabus, C; Leblanc, P; Chnaidermann, J; Grave, L; Dormont, D; Swietnicki, W; Morillas, M; Marck, D; Nandi, P; Darlix, JL

Abstract

The function of the cellular prion protein (PrPC) remains obscure. Studies suggest that PrPC functions in several processes including signal transduction and Cu2+ metabolism. PrPC has also been established to bind nucleic acids. Therefore we investigated the properties of PrPC as a putative nucleic acid chaperone. Surprisingly, PrPC possesses all the nucleic acid chaperoning properties previously specific to retroviral nucleocapsid proteins. PrPC appears to be a molecular mimic of NCP7, the nucleocapsid protein of HIV-1. Thus PrPC, like NCP7, chaperones the annealing of tRNA(Lys) to the HIV-1 primer binding site, the initial step of retrovirus replication. PrPC also chaperones the two DNA strand transfers required for production of a complete proviral DNA with LTRs. Concerning the functions of NCP7 during budding, PrPC also mimics NCP7 by dimerizing the HIV-1 genomic RNA. These data are unprecedented because, although many cellular proteins have been identified as nucleic acid chaperones, none have the properties of retroviral nucleocapsid proteins. To cite this article: E. Derrington et al., C. R. Biologies 325 (2002) 17-23. (C) 2002 Academie des Sciences/Editions scientifiques et medicales Elsevier SAS.

Más información

Título según WOS: ID WOS:000175291900004 Not found in local WOS DB
Título de la Revista: COMPTES RENDUS BIOLOGIES
Volumen: 325
Número: 1
Editorial: ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
Fecha de publicación: 2002
Página de inicio: 17
Página final: 23
DOI:

10.1016/S1631-0691(02)01388-4

Notas: ISI