Heat causes oligomeric disassembly and increases the chaperone activity of small heat shock proteins from sugarcane

dc.creatorTiroli-Cepeda, AO
dc.creatorRamos, CHI
dc.date2010
dc.dateFEB-MAR
dc.date2014-11-19T20:57:31Z
dc.date2015-11-26T16:29:34Z
dc.date2014-11-19T20:57:31Z
dc.date2015-11-26T16:29:34Z
dc.date.accessioned2018-03-28T23:10:36Z
dc.date.available2018-03-28T23:10:36Z
dc.identifierPlant Physiology And Biochemistry. Elsevier France-editions Scientifiques Medicales Elsevier, v. 48, n. 41700, n. 108, n. 116, 2010.
dc.identifier0981-9428
dc.identifierWOS:000276720900005
dc.identifier10.1016/j.plaphy.2010.01.001
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/68177
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/68177
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/68177
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1269754
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionSmall heat shock proteins (sHsp) constitute an important chaperone family linked to conformational diseases. In plants, sHsps prevent protein aggregation by acting as thermosensors and to enhance cell stress tolerance. SsHsp17.2 and SsHsp17.9 are the most highly expressed class I sHsps in sugarcane. They exist as dodecamers at 20 degrees C and have distinct substrate specificities. Therefore, they are useful models to study how class I SHsps work. Here we present data on the effects of heat on the oligomerization and chaperone activity of SsHsp17.2 and SsHsp17.9. Using several biophysical and biochemical probes, we show that the effects of heat are completely reversible, an important property for proteins that act at heat shock temperatures. SsHsp17.2 and SsHsp17.9 dodecamers dissociated to dimers at temperatures ranging from 40 to 45 degrees C and this dissociation was followed by enhanced chaperone activity. We conclude that high temperature affects the oligomeric state of these chaperones, resulting in enhanced chaperone activity. (C) 2010 Elsevier Masson SAS. All rights reserved.
dc.description48
dc.description41700
dc.description108
dc.description116
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFogarty International Center [NIH-R03TW007437]
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFogarty International Center [NIH-R03TW007437]
dc.languageen
dc.publisherElsevier France-editions Scientifiques Medicales Elsevier
dc.publisherParis
dc.publisherFrança
dc.relationPlant Physiology And Biochemistry
dc.relationPlant Physiol. Biochem.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectSmall heat shock protein
dc.subjectChaperone activity
dc.subjectOligomerization
dc.subjectThermosensor
dc.subjectSugarcane
dc.subjectMolecular Chaperones
dc.subjectAlpha-crystallin
dc.subjectIn-vitro
dc.subjectExpression
dc.subjectStress
dc.subjectDependence
dc.subjectResistance
dc.subjectSubstrate
dc.subjectPlants
dc.subjectHsp26
dc.titleHeat causes oligomeric disassembly and increases the chaperone activity of small heat shock proteins from sugarcane
dc.typeArtículos de revistas


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