PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1. - Institut Albert Bonniot Accéder directement au contenu
Article Dans Une Revue Comptes Rendus Biologies Année : 2002

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

Résumé

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 mimices 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.
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Dates et versions

hal-02328820 , version 1 (23-10-2019)

Identifiants

  • HAL Id : hal-02328820 , version 1
  • PUBMED : 11862616

Citer

Edmund A. Derrington, Caroline Gabus, Pascal Leblanc, Jonas Chnaidermann, Linda Grave, et al.. PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1.. Comptes Rendus Biologies, 2002, 325 (1), pp.17-23. ⟨hal-02328820⟩
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