2024-03-28T15:09:14Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/33782020-01-22T13:54:21Zcom_10261_128com_10261_1col_10261_381
Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon
Fredriksson, Åsa
Ballesteros, Manuel
Dukan, Sam
Nyström, Thomas
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.
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 Goran Gustafsson Foundation for Scientific Research in Molecular Biology.
Peer reviewed
2008-03-31T07:29:59Z
2008-03-31T07:29:59Z
2005-06
artículo
http://purl.org/coar/resource_type/c_6501
Journal Bacteriology 187(12): 4207–4213 (2005)
1098-5530
http://hdl.handle.net/10261/3378
10.1128/JB.187.12.4207–4213.2005
15937182
en
http://dx.doi.org/10.1128/JB.187.12.4207-4213.2005
none
242551 bytes
application/pdf
American Society for Microbiology