Dispensable PDZ domain of Escherichia coli YaeL essential protease.

Détails

ID Serval
serval:BIB_DEF89B3633E3
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Dispensable PDZ domain of Escherichia coli YaeL essential protease.
Périodique
Molecular Microbiology
Auteur⸱e⸱s
Bohn C., Collier J., Bouloc P.
ISSN
0950-382X
Statut éditorial
Publié
Date de publication
2004
Peer-reviewed
Oui
Volume
52
Numéro
2
Pages
427-435
Langue
anglais
Résumé
In Escherichia coli, adaptation to extra-cytoplasmic stress relies on sigma(E) activation to induce a rescue pathway. Under non-stressed conditions, sigma(E) is sequestered by the inner membrane protein RseA. Extra-cytoplasmic stress activates DegS-dependent cleavage of RseA, rendering RseA sensitive to further degradation by the YaeL protease. YaeL contains two motifs characteristic of a family of metallo-proteases, as well as a periplasmic PDZ domain. We report results of mutational analyses of the YaeL domains. Surprisingly, expression in a strain depleted for wild-type YaeL or YaeL variants having a 40 amino acid deletion of the PDZ domain or amino acid substitutions of conserved amino acids of the YaeL PDZ domain did not affect cell viability. The proteolytic activity against RseA of these YaeL variants became independent of DegS. These observations suggest that the YaeL PDZ domain exerts a negative control on YaeL activity. Rather than being involved in substrate recognition, the PDZ domain of YaeL is likely to act as an inhibitor of proteolytic activity.
Mots-clé
Amino Acid Motifs, Amino Acid Sequence, Bacterial Proteins, Binding Sites, Cloning, Molecular, DNA Mutational Analysis, Endopeptidases, Escherichia coli, Escherichia coli Proteins, Gene Expression Regulation, Bacterial, Membrane Proteins, Molecular Sequence Data, Mutagenesis, Mutation, Plasmids, Recombinant Proteins, Sequence Homology, Amino Acid, Transcription Factors
Pubmed
Web of science
Création de la notice
27/02/2009 15:46
Dernière modification de la notice
20/08/2019 16:03
Données d'usage