Low resolution structure and stability studies of human GrpE#2, a mitochondrial nucleotide exchange factor

dc.creatorOliveira, CLP
dc.creatorBorges, JC
dc.creatorTorriani, IL
dc.creatorRamos, CHI
dc.date2006
dc.dateMAY 15
dc.date2014-11-16T14:02:09Z
dc.date2015-11-26T16:23:24Z
dc.date2014-11-16T14:02:09Z
dc.date2015-11-26T16:23:24Z
dc.date.accessioned2018-03-28T23:04:40Z
dc.date.available2018-03-28T23:04:40Z
dc.identifierArchives Of Biochemistry And Biophysics. Elsevier Science Inc, v. 449, n. 41671, n. 77, n. 86, 2006.
dc.identifier0003-9861
dc.identifierWOS:000237674700009
dc.identifier10.1016/j.abb.2006.02.015
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/52745
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/52745
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/52745
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1268256
dc.descriptionGrpE acts as a nucleotide exchange factor for the Hsp70 chaperone system. Only one GrpE isoform is present in Escherichia coli, but for reasons not yet well understood, two GrpE isoforms have been found in mammalian mitochondria. Therefore, studies aimed at evaluating the physico-chemical characteristics of these proteins are important for the comprehension of the function of the Hsp70 chaperone system in different organisms. Here we report biophysical studies on human mitochondrial GrpE isoform 2. Small angle X-ray scattering measurements of human GrpE isoform 2 showed that this protein has a quaternary structure which is similar to those of human GrpE isoform I and E coli GrpE: a dimer with a cruciform elongated shape. However, mitochondrial isoforms differed from each other regarding chemical and thermal denaturation profiles. This fact, combined with results of distinct expression patterns previously reported, point out that these proteins may have different response to external stimuli. Our results also indicate that human GrpE isoform 2 is more similar to the GrpE from E coli than to human GrpE isoform 1. These results are relevant because differences in the conformation of Hsp70 co-chaperones are considered to be one of the reasons for functional diversity of this system. (c) 2006 Elsevier Inc. All rights reserved.
dc.description449
dc.description41671
dc.description77
dc.description86
dc.languageen
dc.publisherElsevier Science Inc
dc.publisherNew York
dc.publisherEUA
dc.relationArchives Of Biochemistry And Biophysics
dc.relationArch. Biochem. Biophys.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectGrpE
dc.subjectHsp70
dc.subjectsmall angle X-ray scattering
dc.subjectprotein stability
dc.subjectprotein folding
dc.subjectX-ray-scattering
dc.subjectSmall-angle Scattering
dc.subjectEscherichia-coli
dc.subjectHeat-shock
dc.subjectAnalytical Ultracentrifugation
dc.subjectMolecular Chaperones
dc.subjectAtp Hydrolysis
dc.subjectGrpe
dc.subjectDnak
dc.subjectProtein
dc.titleLow resolution structure and stability studies of human GrpE#2, a mitochondrial nucleotide exchange factor
dc.typeArtículos de revistas


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