Chemical and thermal influence of the [4Fe-4S](2+) cluster of A/G-specific adenine glycosylase from Corynebacterium pseudotuberculosis

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade Federal de São João del-Rei (UFSJ)
dc.contributorUniversidade Federal de Minas Gerais (UFMG)
dc.creatorEberle, Raphael Joseph [UNESP]
dc.creatorCoronado, Monika Aparecida [UNESP]
dc.creatorCaruso, Ícaro Putinhon [UNESP]
dc.creatorLopes, Debora de Oliveira
dc.creatorMiyoshi, Anderson
dc.creatorAzevedo, Vasco
dc.creatorArni, Raghuvir Krishnaswamy [UNESP]
dc.date2015-10-21T13:14:18Z
dc.date2015-10-21T13:14:18Z
dc.date2015-02-01
dc.date.accessioned2023-09-12T06:41:47Z
dc.date.available2023-09-12T06:41:47Z
dc.identifierhttp://www.sciencedirect.com/science/article/pii/S0304416514003912
dc.identifierBiochimica Et Biophysica Acta-general Subjects. Amsterdam: Elsevier Science Bv, v. 1850, n. 2, p. 393-400, 2015.
dc.identifier0304-4165
dc.identifierhttp://hdl.handle.net/11449/128841
dc.identifier10.1016/j.bbagen.2014.11.014
dc.identifierWOS:000348256800015
dc.identifier9162508978945887
dc.identifier0000-0003-2460-1145
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8778186
dc.descriptionThe gram-positive bacteria Corynebacterium pseudotuberculosis, the causative agent of caseous lymphadenitis in livestock significantly reduces productivity and often causes death. The adenine/guanine-specific DNA glycosylase (MutY) prevents mutations in the DNA of the pathogen and a unique feature of the MutY protein family is the [4Fe-4S](2+) cluster that interlinks two protein subdomains. MutY from C. pseudotuberculosis was expressed in E. coli and purified, the CD experiments indicate a high content of alpha-helices and random coiled secondary structure and a typical near-UV CD fingerprint for the [4Fe-4S](2+) cluster. EDTA and copper sulfate possess a strong destabilizing effect on the [4Fe-4S](2+) cluster. UV-vis and fluorescence spectroscopy results demonstrate that between pH 3.0 and 4.0 the integrity of the [4Fe-4S](2+) cluster is destroyed. To investigate the thermal stability of the protein differential scanning calorimetry and fluorescence spectroscopy were used and the T-m was determined to be 45 degrees C. The analysis presented provides information concerning the protein stability under different physio-chemical conditions.
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionFundação de Amparo à Pesquisa do Estado de Minas Gerais (FAPEMIG)
dc.descriptionUniversidade Federal de São João del-Rei, Laboratório de Biologia Molecular, Câmpus Centro-Oeste
dc.descriptionUniversidade Federal de Minas Gerais, Laboratório de Genética Celular e Molecular, Instituto de Ciências Biológicas
dc.descriptionUniversidade Estadual Paulista, Departamento de Física, Instituto de Biociências, Letras e Ciências Exatas de São José do Rio Preto
dc.format393-400
dc.languageeng
dc.publisherElsevier B.V.
dc.relationBiochimica Et Biophysica Acta-general Subjects
dc.relation3.679
dc.relation1,671
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectC. pseudotuberculosis
dc.subjectMutY
dc.subject[4Fe-4S](2+) cluster
dc.subjectDNA repair
dc.subjectSpectroscopic method
dc.subjectSecondary and tertiary structure
dc.titleChemical and thermal influence of the [4Fe-4S](2+) cluster of A/G-specific adenine glycosylase from Corynebacterium pseudotuberculosis
dc.typeArtigo


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