Volltext-Downloads (blau) und Frontdoor-Views (grau)

Bitte verwenden Sie diesen Link, wenn Sie dieses Dokument zitieren oder verlinken wollen: https://nbn-resolving.org/urn:nbn:de:gbv:9-opus-37621

The Involvement of the McsB Arginine Kinase in Clp-Dependent Degradation of the MgsR Regulator in Bacillus subtilis

  • Regulated ATP-dependent proteolysis is a common feature of developmental processes and plays also a crucial role during environmental perturbations such as stress and starvation. The Bacillus subtilis MgsR regulator controls a subregulon within the stress- and stationary phase σB regulon. After ethanol exposition and a short time-window of activity, MgsR is ClpXP-dependently degraded with a half-life of approximately 6 min. Surprisingly, a protein interaction analysis with MgsR revealed an association with the McsB arginine kinase and an in vivo degradation assay confirmed a strong impact of McsB on MgsR degradation. In vitro phosphorylation experiments with arginine (R) by lysine (K) substitutions in McsB and its activator McsA unraveled all R residues, which are essentially needed for the arginine kinase reaction. Subsequently, site directed mutagenesis of the MgsR substrate was used to substitute all arginine residues with glutamate (R-E) to mimic arginine phosphorylation and to test their influence on MgsR degradation in vivo. It turned out, that especially the R33E and R94/95E residues (RRPI motif), the latter are adjacently located to the two redox-sensitive cysteines in a 3D model, have the potential to accelerate MgsR degradation. These results imply that selective arginine phosphorylation may have favorable effects for Clp dependent degradation of short-living regulatory proteins. We speculate that in addition to its kinase activity and adaptor function for the ClpC ATPase, McsB might also serve as a proteolytic adaptor for the ClpX ATPase in the degradation mechanism of MgsR.

Download full text files

Export metadata

Additional Services

Search Google Scholar

Statistics

frontdoor_oas
Metadaten
Author: Lars Lilge, Alexander Reder, Frank Tippmann, Friedrich Morgenroth, Janice Grohmann, Dörte BecherORCiD, Katharina Riedel, Uwe VölkerORCiD, Michael Hecker, Ulf Gerth
URN:urn:nbn:de:gbv:9-opus-37621
DOI:https://doi.org/10.3389/fmicb.2020.00900
ISSN:1664-302X
Parent Title (English):Frontiers in Microbiology
Publisher:Frontiers Media S.A.
Document Type:Article
Language:English
Date of first Publication:2020/05/12
Release Date:2020/10/17
Tag:Clp proteolysis; McsB arginine kinase; MgsR activity; MgsR degradation; arginine phosphorylation
GND Keyword:-
Volume:11
Faculties:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Mikrobiologie - Abteilung für Genetik & Biochemie
Licence (German):License LogoCreative Commons - Namensnennung