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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleSmall-angle X-ray scattering and in silico modeling approaches for the accurate functional annotation of an LysR-type transcriptional regulatorpt_BR
dc.contributor.authorToledo, MASpt_BR
dc.contributor.authorSantos, CApt_BR
dc.contributor.authorMendes, JSpt_BR
dc.contributor.authorPelloso, ACpt_BR
dc.contributor.authorBeloti, LLpt_BR
dc.contributor.authorCrucello, Apt_BR
dc.contributor.authorFavaro, MTPpt_BR
dc.contributor.authorSantiago, ASpt_BR
dc.contributor.authorSchneider, DRSpt_BR
dc.contributor.authorSaraiva, AMpt_BR
dc.contributor.authorStach-Machado, DRpt_BR
dc.contributor.authorSouza, AApt_BR
dc.contributor.authorTrivella, DBBpt_BR
dc.contributor.authorAparicio, Rpt_BR
dc.contributor.authorTasic, Lpt_BR
dc.contributor.authorAzzoni, ARpt_BR
dc.contributor.authorSouza, APpt_BR
unicamp.authorToledo, M. A. S. Santos, C. A. Mendes, J. S. Pelloso, A. C. Beloti, L. L. Crucello, A. Favaro, M. T. P. Santiago, A. S. Schneider, D. R. S. Saraiva, A. M. Azzoni, A. R. Souza, A. P. Univ Estadual Campinas, Ctr Biol Mol & Engn Genet, Campinas, SP, Brazilpt_BR
unicamp.authorSaraiva, A. M. Inst Nacl Metrol Qualidade & Tecnol, Rio De Janeiro, Brazilpt_BR
unicamp.authorStach-Machado, D. R. Univ Estadual Campinas, Inst Biol, Dept Imunol, Campinas, SP, Brazilpt_BR
unicamp.authorSouza, A. A. IAC, Ctr APTA Citros Sylvio Moreira, Cordeiropolis, SP, Brazilpt_BR
unicamp.authorTrivella, D. B. B. Aparicio, R. Univ Estadual Campinas, Inst Quim, Lab Biol Estruct & Cristalog, Campinas, SP, Brazilpt_BR
unicamp.authorTasic, L. Univ Estadual Campinas, Inst Quim, Lab Quim Biol, Campinas, SP, Brazilpt_BR
unicamp.authorAzzoni, A. R. Univ Sao Paulo, Escola Politecn, Dept Engn Quim, Sao Paulo, Brazilpt_BR
unicamp.authorSouza, A. P. Univ Estadual Campinas, Dept Biol Vegetal, Inst Biol, Campinas, SP, Brazilpt_BR
dc.subjectLysR-like transcriptional regulator (LTTR)pt_BR
dc.subjectSmall-angle X-ray scattering (SAXS)pt_BR
dc.subjectCitrus variegated chlorosis (CVC)pt_BR
dc.subject.wosCitrus Variegated Chlorosispt_BR
dc.subject.wosPathogen Xylella-fastidiosapt_BR
dc.subject.wosAutomated Protein-structurept_BR
dc.subject.wosStructure Predictionpt_BR
dc.subject.wosBiofilm Formationpt_BR
dc.description.abstractXylella fastidiosa is a xylem-limited, Gram-negative phytopathogen responsible for economically relevant crop diseases. Its genome was thus sequenced in an effort to characterize and understand its metabolism and pathogenic mechanisms. However, the assignment of the proper functions to the identified open reading frames (ORFs) of this pathogen was impaired due to a lack of sequence similarity in the databases. In the present work, we used small-angle X-ray scattering and in silica modeling approaches to characterize and assign a function to a predicted LysR-type transcriptional regulator in the X. fastidiosa (XfLysRL) genome. XfLysRL was predicted to be a homologue of BenM, which is a transcriptional regulator involved in the degradation pathway of aromatic compounds. Further functional assays confirmed the structural prediction because we observed that XfLysRL interacts with benzoate and cis,cis-muconic acid (also known as 2E,4E-hexa-2,4-dienedioic acid; hereafter named muconate), both of which are co-factors of BenM. In addition, we showed that the XfLysRL protein is differentially expressed during the different stages of X.fastidiosa biofilm formation and planktonic cell growth, which indicates that its expression responds to a cellular signal that is likely related to the aromatic compound degradation pathway. The assignment of the proper function to a protein is a key step toward understanding the cellular metabolic pathways and pathogenic mechanisms. In the context of X. fastidiosa, the characterization of the predicted ORFs may lead to a better understanding of the cellular pathways that are linked to its bacterial pathogenicity. (C) 2012 Published by Elsevier
dc.relation.ispartofBiochimica Et Biophysica Acta-proteins And Proteomicspt_BR
dc.relation.ispartofabbreviationBBA-Proteins Proteomicspt_BR
dc.publisherElsevier Science Bvpt_BR
dc.identifier.citationBiochimica Et Biophysica Acta-proteins And Proteomics. Elsevier Science Bv, v. 1834, n. 3, n. 697, n. 707, 2013.pt_BR
dc.sourceWeb of Sciencept_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.description.sponsorship1Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorship1Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorship1Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.description.sponsordocumentnumberFAPESP [01/07533-7]pt
dc.description.provenanceMade available in DSpace on 2014-07-30T19:58:07Z (GMT). No. of bitstreams: 0 Previous issue date: 2013en
dc.description.provenanceMade available in DSpace on 2015-11-26T17:52:33Z (GMT). No. of bitstreams: 0 Previous issue date: 2013en
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