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Defense against Protein Carbonylation by DnaK/DnaJ and Proteases of the Heat Shock Regulon

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dc.creator Fredriksson, Åsa
dc.creator Ballesteros, Manuel
dc.creator Dukan, Sam
dc.creator Nyström, Thomas
dc.date 2008-03-31T07:29:59Z
dc.date 2008-03-31T07:29:59Z
dc.date 2005-06
dc.date.accessioned 2017-01-31T01:01:21Z
dc.date.available 2017-01-31T01:01:21Z
dc.identifier Journal Bacteriology 187(12): 4207–4213 (2005)
dc.identifier 1098-5530
dc.identifier http://hdl.handle.net/10261/3378
dc.identifier 10.1128/JB.187.12.4207–4213.2005
dc.identifier.uri http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3378
dc.description Protein carbonylation is an irreversible oxidative modification that increases during organism aging and bacterial growth arrest. We analyzed whether the heat shock regulon has a role in defending Escherichia coli cells against this deleterious modification upon entry into stationary phase. Providing the cell with ectopically elevated levels of the heat shock transcription factor, 32, effectively reduced stasis-induced carbonylation. Separate overproduction of the major chaperone systems, DnaK/DnaJ and GroEL/GroES, established that the former of these is more important in counteracting protein carbonylation. Deletion of the heat shock proteases Lon and HslVU enhanced carbonylation whereas a clpP deletion alone had no effect. However, ClpP appears to have a role in reducing protein carbonyls in cells lacking Lon and HslVU. Proteomic immunodetection of carbonylated proteins in the wild-type, lon, and hslVU strains demonstrated that the same spectrum of proteins displayed a higher load of carbonyl groups in the lon and hslVU mutants. These proteins included the -subunit of RNA polymerase, elongation factors Tu and G, the E1 subunit of the pyruvate dehydrogenase complex, isocitrate dehydrogenase, 6-phosphogluconate dehydrogenase, and serine hydroxymethyltranferase.
dc.description This work was sponsored by grants from the Swedish Natural Research Council and the Foundation for Strategic Research in Sweden and an award from the Go¨ran Gustafsson Foundation for Scientific Research in Molecular Biology.
dc.description Peer reviewed
dc.format 242551 bytes
dc.format application/pdf
dc.language eng
dc.publisher American Society for Microbiology
dc.relation http://dx.doi.org/10.1128/JB.187.12.4207-4213.2005
dc.rights closedAccess
dc.title Defense against Protein Carbonylation by DnaK/DnaJ and Proteases of the Heat Shock Regulon
dc.type Artículo


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