Proteome analysis of Streptomyces coelicolor mutants affected in the proteasome system reveals changes in stress-responsive proteins.
Prokaryotic 20S proteasomes are confined to archaebacteria and actinomycetes. Bacterial targets of this compartmentalized multi-subunit protease have not yet been identified and its physiological function in prokaryotes remains unknown. In this study, intracellular and extracellular proteomes of Streptomyces coelicolor A3(2) mutants affected in the structural genes of the 20S proteasome, in the gene encoding the presumed proteasome-accessory AAA ATPase ARC, or in two putative proteasome-associated actinomycete-specific genes (sco1646, sco1647) were analysed, revealing modified patterns of stress-responsive proteins. In addition, the extracellular protease profile of the sco1647 mutant was significantly altered. The most prominent change, common to the four mutants, was a strongly increased level of the non-heme chloroperoxidase SCO0465, coinciding with an increased resistance to cumene hydroperoxide.
De Mot
René
R
Centre of Microbial and Plant Genetics, Department of Microbial and Molecular Systems, Faculty of Bioscience Engineering, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, 3001 Leuven, Belgium. rene.demot@biw.kuleuven.be
Schoofs
Geert
G
Nagy
István
I
D001426:Bacterial Proteins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D016254:Mutagenesis, Insertional; D046988:Proteasome Endopeptidase Complex / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D048372:Streptomyces coelicolor / Q000201:enzymology* / Q000235:genetics* / Q000378:metabolism
D001426:Bacterial Proteins; D046988:Proteasome Endopeptidase Complex