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dc.contributor.author
El Mekdad, Hala  
dc.contributor.author
Boutant, Emmanuel  
dc.contributor.author
Karnib, Hassan  
dc.contributor.author
Biedma, Marina Elizabeth  
dc.contributor.author
Sharma, Kamal Kant  
dc.contributor.author
Malytska, Iuliia  
dc.contributor.author
Laumond, Géraldine  
dc.contributor.author
Roy, Marion  
dc.contributor.author
Réal, Eléonore  
dc.contributor.author
Paillart, Jean Christophe  
dc.contributor.author
Moog, Christiane  
dc.contributor.author
Darlix, Jean Luc  
dc.contributor.author
Mély, Yves  
dc.contributor.author
de Rocquigny, Hugues  
dc.date.available
2018-08-30T23:58:38Z  
dc.date.issued
2016-07  
dc.identifier.citation
El Mekdad, Hala; Boutant, Emmanuel; Karnib, Hassan; Biedma, Marina Elizabeth; Sharma, Kamal Kant; et al.; Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling; BioMed Central; Retrovirology; 13; 1; 7-2016; 1-14  
dc.identifier.issn
1742-4690  
dc.identifier.uri
http://hdl.handle.net/11336/57847  
dc.description.abstract
Background: In HIV-1 infected cells, the integrated viral DNA is transcribed by the host cell machinery to generate the full length HIV-1 RNA (FL RNA) that serves as mRNA encoding for the Gag and GagPol precursors. Virion formation is orchestrated by Gag, and the current view is that a specific interaction between newly made Gag molecules and FL RNA initiates the process. This in turn would cause FL RNA dimerization by the NC domain of Gag (GagNC). However the RNA chaperoning activity of unprocessed Gag is low as compared to the mature NC protein. This prompted us to search for GagNC co-factors. Results: Here we report that RPL7, a major ribosomal protein involved in translation regulation, is a partner of Gag via its interaction with the NC domain. This interaction is mediated by the NC zinc fingers and the N- and C-termini of RPL7, respectively, but seems independent of RNA binding, Gag oligomerization and its interaction with the plasma membrane. Interestingly, RPL7 is shown for the first time to exhibit a potent DNA/RNA chaperone activity higher than that of Gag. In addition, Gag and RPL7 can function in concert to drive rapid nucleic acid hybridization. Conclusions: Our results show that GagNC interacts with the ribosomal protein RPL7 endowed with nucleic acid chaperone activity, favoring the notion that RPL7 could be a Gag helper chaperoning factor possibly contributing to the start of Gag assembly.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
BioMed Central  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/  
dc.subject
Chaperone Activity  
dc.subject
Gag  
dc.subject
Hiv  
dc.subject
Interaction  
dc.subject
Nucleocapsid  
dc.subject
Rpl7  
dc.subject.classification
Otras Ciencias Biológicas  
dc.subject.classification
Ciencias Biológicas  
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS  
dc.title
Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2018-08-28T18:42:19Z  
dc.journal.volume
13  
dc.journal.number
1  
dc.journal.pagination
1-14  
dc.journal.pais
Reino Unido  
dc.journal.ciudad
Londres  
dc.description.fil
Fil: El Mekdad, Hala. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia  
dc.description.fil
Fil: Boutant, Emmanuel. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia  
dc.description.fil
Fil: Karnib, Hassan. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia  
dc.description.fil
Fil: Biedma, Marina Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Estudios Inmunológicos y Fisiopatológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Estudios Inmunológicos y Fisiopatológicos; Argentina. Université de Strasbourg; Francia. Inserm; Francia  
dc.description.fil
Fil: Sharma, Kamal Kant. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia  
dc.description.fil
Fil: Malytska, Iuliia. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia  
dc.description.fil
Fil: Laumond, Géraldine. Université de Strasbourg; Francia. Inserm; Francia  
dc.description.fil
Fil: Roy, Marion. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia  
dc.description.fil
Fil: Réal, Eléonore. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia  
dc.description.fil
Fil: Paillart, Jean Christophe. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia  
dc.description.fil
Fil: Moog, Christiane. Université de Strasbourg; Francia. Inserm; Francia  
dc.description.fil
Fil: Darlix, Jean Luc. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia  
dc.description.fil
Fil: Mély, Yves. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia  
dc.description.fil
Fil: de Rocquigny, Hugues. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia  
dc.journal.title
Retrovirology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4982112/  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://retrovirology.biomedcentral.com/articles/10.1186/s12977-016-0287-4  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1186/s12977-016-0287-4