Biophysical and Structural Characterization of the Recombinant Human eIF3L

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dc.contributor.authorMorais, Ana T. S. [UNESP]
dc.contributor.authorMeza, Andreia N.
dc.contributor.authorAraujo, Gabriela C. [UNESP]
dc.contributor.authorVidotto, Alessandra
dc.contributor.authorSouza, Fatima P. [UNESP]
dc.contributor.authorFossey, Marcelo A. [UNESP]
dc.contributor.authorMurakami, Mario T.
dc.contributor.authorNogueira, Mauricio L.
dc.contributor.institutionFaculdade de Medicina de São José do Rio Preto (FAMERP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionCNPEM
dc.contributor.institutionUniv Texas Med Branch
dc.date.accessioned2014-12-03T13:11:06Z
dc.date.available2014-12-03T13:11:06Z
dc.date.issued2014-01-01
dc.description.abstractThe eukaryotic translation initiation factor 3, subunit L (eIF3L) is one of the subunits of the eIF3 complex, an accessory protein of the Polymerase I enzyme and may have an important role in the Flavivirus replication by interaction with a viral non-structural 5 protein. Considering the importance of eIF3L in a diversity of cellular functions, we have produced the recombinant full-length eIF3L protein in Escherichia coli and performed spectroscopic and in silico analyses to gain insights into its hydrodynamic behavior and structure. Dynamic light scattering showed that eIF3L behaves as monomer when it is not interacting with other molecular partners. Circular dichroism experiments showed a typical spectrum of alpha-helical protein for eIF3L, which is supported by sequence-based predictions of secondary structure and the 3D in silico model. The molecular docking with the K subunit of the eIF3 complex revealed a strong interaction. It was also predicted several potential interaction sites in eIF3L, indicating that the protein is likely capable of interacting with other molecules as experimentally shown in other functional studies. Moreover, bioinformatics analyses showed approximately 8 putative phosphorylation sites and one possible N-glycosylation site, suggesting its regulation by post-translational modifications. The production of the eIF3L protein in E. coli and structural information gained in this study can be instrumental for target-based drug design and inhibitors against Flavivirus replication and to shed light on the molecular mechanisms involved in the eukaryotic translation initiation.en
dc.description.affiliationFac Med Sao Jose do Rio Preto FAMERP, Dept Doencas Dermat Infecciosas & Parasitarias, Lab Pesquisas Virol, BR-15090000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUniv Estadual Paulista, Dept Biol, IBILCE UNESP, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationCNPEM, LNBio, Lab Nacl Biociencias, BR-13083970 Campinas, SP, Brazil
dc.description.affiliationUniv Estadual Paulista, Dept Fis, IBILCE UNESP, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUniv Estadual Paulista, Lab Multiusuario Inovacao Bio Mol, Sao Jose de Rio Preto IBILCE UNESP, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUniv Texas Med Branch, Ctr Trop Dis, Galveston, TX 77555 USA
dc.description.affiliationUnespUniv Estadual Paulista, Dept Biol, IBILCE UNESP, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Dept Fis, IBILCE UNESP, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Lab Multiusuario Inovacao Bio Mol, Sao Jose de Rio Preto IBILCE UNESP, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipIdFAPESP: 10/05043-1
dc.description.sponsorshipIdFAPESP: 09/01400-7
dc.description.sponsorshipIdCNPq: 566289/2008-3
dc.format.extent56-62
dc.identifierhttp://dx.doi.org/10.2174/09298665113209990084
dc.identifier.citationProtein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 21, n. 1, p. 56-62, 2014.
dc.identifier.issn0929-8665
dc.identifier.urihttp://hdl.handle.net/11449/112862
dc.identifier.wosWOS:000329022400010
dc.language.isoeng
dc.publisherBentham Science Publ Ltd
dc.relation.ispartofProtein and Peptide Letters
dc.relation.ispartofjcr1.039
dc.relation.ispartofsjr0,429
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectCircular dichroismen
dc.subjectDynamic light scatteringen
dc.subjecteukaryotic translation initiation factor 3en
dc.subjectsubunit Len
dc.subjectMolecular modelingen
dc.titleBiophysical and Structural Characterization of the Recombinant Human eIF3Len
dc.typeArtigo
dcterms.rightsHolderBentham Science Publ Ltd
unesp.author.orcid0000-0002-2012-388X[6]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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