The extracellular proteome of Bacillus subtilis under secretion stress conditions.

Détails

ID Serval
serval:BIB_E419DA51E09B
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The extracellular proteome of Bacillus subtilis under secretion stress conditions.
Périodique
Molecular Microbiology
Auteur(s)
Antelmann H., Darmon E., Noone D., Veening J.W., Westers H., Bron S., Kuipers O.P., Devine K.M., Hecker M., van Dijl J.M.
ISSN
0950-382X (Print)
ISSN-L
0950-382X
Statut éditorial
Publié
Date de publication
2003
Volume
49
Numéro
1
Pages
143-156
Langue
anglais
Résumé
The accumulation of malfolded proteins in the cell envelope of the Gram-positive eubacterium Bacillus subtilis was previously shown to provoke a so-called secretion stress response. In the present studies, proteomic approaches were employed to identify changes in the extracellular proteome of B. subtilis in response to secretion stress. The data shows that, irrespective of the way in which secretion stress is imposed on the cells, the levels of only two extracellular proteins, HtrA and YqxI, display major variations in a parallel manner. Whereas the extracellular level of the HtrA protease is determined through transcriptional regulation, the level of YqxI in the growth medium is determined post-transcriptionally in an HtrA-dependent manner. In the absence of secretion stress, the extracellular levels of HtrA and YqxI are low because of extracytoplasmic proteolysis. Finally, the protease active site of HtrA is dispensable for post-transcriptional YqxI regulation. It is known that Escherichia coli HtrA has combined protease and chaperone-like activities. As this protein shares a high degree of similarity with B. subtilis HtrA, it can be hypothesized that both activities are conserved in B. subtilis HtrA. Thus, a chaperone-like activity of B. subtilis HtrA could be involved in the appearance of YqxI on the extracellular proteome.
Mots-clé
Acyltransferases, Bacillus subtilis/genetics, Bacillus subtilis/metabolism, Bacterial Proteins/genetics, Bacterial Proteins/metabolism, Culture Media/chemistry, Culture Media/metabolism, Escherichia coli Proteins/metabolism, Gene Expression Regulation, Bacterial, Heat-Shock Proteins/genetics, Heat-Shock Proteins/metabolism, Periplasmic Proteins/genetics, Periplasmic Proteins/metabolism, Protein Folding, Proteome/analysis, Recombinant Fusion Proteins/metabolism, Serine Endopeptidases/genetics, Serine Endopeptidases/metabolism, Transcription, Genetic
Pubmed
Web of science
Open Access
Oui
Création de la notice
11/10/2016 15:23
Dernière modification de la notice
20/08/2019 16:07
Données d'usage