dc.creatorSeeger, Michael
dc.creatorOsorio, Gonzalo
dc.creatorJerez, Carlos
dc.date.accessioned2018-12-20T15:24:47Z
dc.date.available2018-12-20T15:24:47Z
dc.date.created2018-12-20T15:24:47Z
dc.date.issued1996
dc.identifierFEMS Microbiology Letters, Volumen 138, Issue 2-3, 1996, Pages 129-134.
dc.identifier03781097
dc.identifier10.1016/0378-1097(96)00084-5
dc.identifierhttp://repositorio.uchile.cl/handle/2250/159098
dc.description.abstractThe levels of phosphorylation of the chaperones DnaK and GroEL and other proteins varied when cells of Thiobacillus ferrooxidans were subjected to phosphate starvation. The phosphorylated amino acid of GroEL was found to be threonine. Our results show that not only heat shock, but also a nutrient starvation stress leads to phosphorylation of chaperones and, in addition, support the possible role of phosphorylation of these proteins in the sensing and regulation of stress responses in bacteria.
dc.languageen
dc.publisherBlackwell Publishing Ltd
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceFEMS Microbiology Letters
dc.subjectChaperone phosphorylation
dc.subjectDnaK
dc.subjectGroEL
dc.subjectStress response and protein phosphorylation
dc.subjectThiobacillus ferrooxidans
dc.titlePhosphorylation of GroEL, DnaK and other proteins from Thiobacillus ferrooxidans grown under different conditions
dc.typeArtículos de revistas


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