Mostrar el registro sencillo del ítem

dc.contributor.author
Álvarez Paggi, Damián Jorge
dc.contributor.author
Esperante, Sebastian
dc.contributor.author
Salgueiro, Mariano
dc.contributor.author
Camporeale, Gabriela
dc.contributor.author
Oliveira, G.A.
dc.contributor.author
de Prat Gay, Gonzalo
dc.date.available
2019-12-27T20:03:43Z
dc.date.issued
2019-08
dc.identifier.citation
Álvarez Paggi, Damián Jorge; Esperante, Sebastian; Salgueiro, Mariano; Camporeale, Gabriela; Oliveira, G.A.; et al.; A conformational switch balances viral RNA accessibility and protection in a nucleocapsid ring model; Elsevier Science Inc; Archives of Biochemistry and Biophysics; 671; 8-2019; 77-86
dc.identifier.issn
0003-9861
dc.identifier.uri
http://hdl.handle.net/11336/93162
dc.description.abstract
Virus from the Mononegavirales order share common features ranging from virion structure arrangement to mechanisms of replication and transcription. One of them is the way the nucleoprotein (N) wraps and protects the RNA genome from degradation by forming a highly ordered helical nucleocapsid. However, crystal structures from numerous Mononegavirales reveal that binding to the nucleoprotein results in occluded nucleotides that hinder base pairing necessary for transcription and replication. This hints at the existence of alternative conformations of the N protein that would impact on the protein-RNA interface, allowing for transient exposure of the nucleotides without complete RNA release. Moreover, the regulation between the alternative conformations should be finely tuned. Recombinant expression of N from the respiratory syncytial virus form regular N/RNA common among all Mononegavirales, and these constitute an ideal minimal unit for investigating the mechanisms through which these structures protect RNA so efficiently while allowing for partial accessibility during transcription and replication. Neither pH nor high ionic strength could dissociate the RNA but led to irreversible aggregation of the nucleoprotein. Low concentrations of guanidine chloride dissociated the RNA moiety but leading to irreversible aggregation of the protein moiety. On the other hand, high concentrations of urea and long incubation periods were required to remove bound RNA. Both denaturants eventually led to unfolding but converged in the formation of an RNA-free β-enriched intermediate species that remained decameric even at high denaturant concentrations. Although the N-RNA rings interact with the phosphoprotein P, the scaffold of the RNA polymerase complex, this interaction did not lead to RNA dissociation from the rings in vitro. Thus, we have uncovered complex equilibria involving changes in secondary structure of N and RNA loosening, processes that must take place in the context of RNA transcription and replication, whose detailed mechanisms and cellular and viral participants need to be established.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science Inc
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
NUCLEOPROTEIN
dc.subject
OLIGOMERIZATION
dc.subject
PROTEIN-RNA INTERACTION
dc.subject
RSV
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
A conformational switch balances viral RNA accessibility and protection in a nucleocapsid ring model
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-12-11T20:21:31Z
dc.journal.volume
671
dc.journal.pagination
77-86
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Álvarez Paggi, Damián Jorge. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Esperante, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Fundación Instituto Leloir; Argentina
dc.description.fil
Fil: Salgueiro, Mariano. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Camporeale, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Fundación Instituto Leloir; Argentina
dc.description.fil
Fil: Oliveira, G.A.. University of Virginia; Estados Unidos. Universidade Federal do Rio de Janeiro; Brasil
dc.description.fil
Fil: de Prat Gay, Gonzalo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Fundación Instituto Leloir; Argentina
dc.journal.title
Archives of Biochemistry and Biophysics
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0003986119302899
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.abb.2019.06.005