Document Detail


Differential contributions of tacaribe arenavirus nucleoprotein N-terminal and C-terminal residues to nucleocapsid functional activity.
MedLine Citation:
PMID:  24696466     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
IMPORTANCE: The mechanism of arenavirus functional nucleocapsid assembly is still poorly understood. No detailed information is available on the nucleocapsid structure, and the regions of full-length NP involved in binding to viral RNA remain to be determined. In this report, novel findings are provided on critical interactions between the viral ribonucleoprotein components. We identify several amino acid residues in both the N-terminal and C-terminal domains of TCRV NP that differentially contribute to NP-NP and NP-RNA interactions and analyze their relevance for binding of NP to the L polymerase and for nucleocapsid activity. Our results provide insight into the contribution of NP self-interaction to RNP assembly and activity and reveal the involvement of the NP C-terminal domain in RNA binding.
Authors:
Alejandra D'Antuono; Maria Eugenia Loureiro; Sabrina Foscaldi; Cristina Marino-Buslje; Nora Lopez
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2014-04-02
Journal Detail:
Title:  Journal of virology     Volume:  88     ISSN:  1098-5514     ISO Abbreviation:  J. Virol.     Publication Date:  2014 Jun 
Date Detail:
Created Date:  2014-05-07     Completed Date:  2014-07-02     Revised Date:  2014-07-14    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6492-505     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Arenaviruses, New World / genetics,  metabolism*
Base Sequence
Blotting, Northern
Blotting, Western
Computational Biology
DNA-Directed RNA Polymerases / metabolism
Gene Expression Regulation, Viral / genetics*
Immunoprecipitation
Models, Molecular*
Molecular Sequence Data
Mutagenesis
Nucleocapsid / metabolism,  physiology*
Nucleoproteins / genetics,  metabolism*
Plasmids / genetics
RNA, Viral / biosynthesis,  metabolism*
Sequence Analysis, DNA
Virus Assembly / genetics,  physiology*
Chemical
Reg. No./Substance:
0/Nucleoproteins; 0/RNA, Viral; EC 2.7.7.6/DNA-Directed RNA Polymerases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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