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dc.contributor.author
Incicco, Juan Jeremías
dc.contributor.author
Gebhard, Leopoldo German
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dc.contributor.author
González Lebrero, Rodolfo M.
dc.contributor.author
Gamarnik, Andrea V.
dc.contributor.author
Sergio B. Kaufman
dc.date.available
2015-05-26T19:07:10Z
dc.date.issued
2013-03-19
dc.identifier.citation
Incicco, Juan Jeremías; Gebhard, Leopoldo German; González Lebrero, Rodolfo M. ; Andrea V. Gamarnik; Sergio B. Kaufman; Steady-State NTPase Activity of Dengue Virus NS3: Number of Catalytic Sites, Nucleotide Specificity and Activation by sRNA; Public Library Science; Plos One; 8; 3; 19-3-2013; 1-12;
dc.identifier.issn
1932-6203
dc.identifier.uri
http://hdl.handle.net/11336/565
dc.description.abstract
Dengue virus nonstructural protein 3 (NS3) unwinds double stranded RNA driven by the free energy derived from the hydrolysis of nucleoside triphosphates. This paper presents the first systematic and quantitative characterization of the steady-state NTPase activity of DENV NS3 and their interaction with ssRNA. Substrate curves for ATP, GTP, CTP and UTP were obtained, and the specificity order for these nucleotides -evaluated as the ratio (kcat/KM)- was GTP=ATP=CTP > UTP, which showed that NS3 have poor ability to discriminate between different NTPs. Competition experiments between the four substrates indicated that all of them are hydrolyzed in one and the same catalytic site of the enzyme. The effect of ssRNA on the ATPase activity of NS3 was studied using poly(A) and poly(C). Both RNA molecules produced a 10 fold increase in the turnover rate constant (kcat) and a 100 fold decrease in the apparent affinity (KM) for ATP. When the ratio [RNA bases]/[NS3] was between 0 and *20 the ATPase activity was inhibited by increasing both poly(A) and poly(C). Using the theory of binding of large ligands (NS3) to a one-dimensional homogeneous lattice of infinite length (RNA) we tested the hypothesis that inhibition is the result of crowding of NS3 molecules along the RNA lattices. Finally, we discuss why this hypothesis is consistent with the idea that the ATPase catalytic cycle is tightly coupled to the movement of NS3 helicase along the RNA.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Public Library Science
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Rna Helicase
dc.subject
Nonstructural Protein 3
dc.subject
Dengue Virus
dc.subject.classification
Ciencias Naturales y Exactas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
Bioquímica y Biología Molecular (ídem 3.1.10)
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dc.title
Steady-State NTPase Activity of Dengue Virus NS3: Number of Catalytic Sites, Nucleotide Specificity and Activation by sRNA
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-03-30 10:35:44.97925-03
dc.journal.volume
8
dc.journal.number
3
dc.journal.pagination
1-12
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
San Francisco
dc.description.fil
Fil: Incicco, Juan Jeremías. DTO.DE QUIMICA BIOLOGICA; INST.DE QUIMICA Y FISICO-QUIMICA BIOLOGICAS;
dc.description.fil
Fil: Gebhard, Leopoldo German. INST.DE INVEST.BIOQUIMICAS DE BS.AS(I); FUND.INSTITUTO LELOIR;
dc.description.fil
Fil: González Lebrero, Rodolfo M.. DTO.DE QUIMICA BIOLOGICA; INST.DE QUIMICA Y FISICO-QUIMICA BIOLOGICAS;
dc.description.fil
Fil: Andrea V. Gamarnik. INST.DE INVEST.BIOQUIMICAS DE BS.AS(I); FUND.INSTITUTO LELOIR;
dc.description.fil
Fil: Sergio B. Kaufman. INST.DE QUIMICA Y FISICO-QUIMICA BIOLOGICAS; DTO.DE QUIMICA BIOLOGICA;
dc.journal.title
Plos One
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://dx.plos.org/10.1371/journal.pone.0058508
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