Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: dissociation by the Rev response element.

Détails

Ressource 1Télécharger: BIB_2EF551320B8B.P001.pdf (2395.78 [Ko])
Etat: Public
Version: Final published version
ID Serval
serval:BIB_2EF551320B8B
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: dissociation by the Rev response element.
Périodique
Molecular and Cellular Biology
Auteur⸱e⸱s
Fankhauser C., Izaurralde E., Adachi Y., Wingfield P., Laemmli U.K.
ISSN
0270-7306 (Print)
ISSN-L
0270-7306
Statut éditorial
Publié
Date de publication
1991
Volume
11
Numéro
5
Pages
2567-2575
Langue
anglais
Résumé
The human immunodeficiency virus type 1 (HIV) Rev protein is thought to be involved in the export of unspliced or singly spliced viral mRNAs from the nucleus to the cytoplasm. This function is mediated by a sequence-specific interaction with a cis-acting RNA element, the Rev response element (RRE), present in these intron-containing RNAs. To identify possible host proteins involved in Rev function, we fractionated nuclear cell extracts with a Rev affinity column. A single, tightly associated Rev-binding protein was identified; this protein is the mammalian nucleolar protein B23. The interaction between HIV Rev and B23 is very specific, as it was observed in complex cell extracts. The complex is also very stable toward dissociation by high salt concentrations. Despite the stability of the Rev-B23 protein complex, the addition of RRE, but not control RNA, led to the displacement of B23 and the formation of a specific Rev-RRE complex. The mammalian nucleolar protein B23 or its amphibian counterpart No38 is believed to function as a shuttle receptor for the nuclear import of ribosomal proteins. B23 may also serve as a shuttle for the import of HIV Rev from the cytoplasm into the nucleus or nucleolus to allow further rounds of export of RRE-containing viral RNAs.
Mots-clé
Binding Sites, Cell Nucleus/metabolism, Centrifugation, Density Gradient, Chromatography, Affinity, DNA, Viral/genetics, DNA, Viral/isolation & purification, Gene Products, rev/isolation & purification, Gene Products, rev/metabolism, Genes, rev, HIV-1/genetics, HIV-1/metabolism, HeLa Cells/metabolism, Humans, Nuclear Proteins/isolation & purification, Nuclear Proteins/metabolism, Plasmids, Protein Binding, Transcription, Genetic, rev Gene Products, Human Immunodeficiency Virus
Pubmed
Web of science
Création de la notice
13/12/2012 13:20
Dernière modification de la notice
20/08/2019 14:13
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