scholarly journals Structure of the Periplasmic Stress Response Protein CpxP

2011 ◽  
Vol 193 (9) ◽  
pp. 2149-2157 ◽  
Author(s):  
G. L. Thede ◽  
D. C. Arthur ◽  
R. A. Edwards ◽  
D. R. Buelow ◽  
J. L. Wong ◽  
...  
Keyword(s):  
Stress Response ◽  
Periplasmic Stress

scholarly journals A Suppressor Mutation That Creates a Faster and More Robust σE Envelope Stress Response

2016 ◽  
Vol 198 (17) ◽  
pp. 2345-2351 ◽  
Author(s):  
Anna Konovalova ◽  
Jaclyn A. Schwalm ◽  
Thomas J. Silhavy
Keyword(s):  
Stress Response ◽  
Stress Responses ◽  
Novel Mutation ◽  
Signal Transduction Pathway ◽  
Normal Growth ◽  
Internal Stresses ◽  
Content Type ◽  
Envelope Stress ◽  
Genetic Perturbations ◽  
Periplasmic Stress

ABSTRACTThe σE envelope stress response is an essential signal transduction pathway which detects and removes mistargeted outer membrane (OM) β-barrel proteins (OMPs) in the periplasm ofEscherichia coli. It relies on σE, an alternative sigma factor encoded by therpoEgene. Here we report a novel mutation, a nucleotide change of C to A in the third base of the second codon, which increases levels of σE (rpoE_S2R). TherpoE_S2Rmutation does not lead to the induction of the stress response during normal growth but instead changes the dynamics of induction upon periplasmic stress, resulting in a faster and more robust response. This allows cells to adapt faster to the periplasmic stress, avoiding lethal accumulation of unfolded OMPs in the periplasm caused by severe defects in the OMP assembly pathway.IMPORTANCESurvival of bacteria under conditions of external or internal stresses depends on timely induction of stress response signaling pathways to regulate expression of appropriate genes that function to maintain cellular homeostasis. Previous studies have shown that strong preinduction of envelope stress responses can allow bacteria to survive a number of lethal genetic perturbations. In our paper, we describe a unique mutation that enhances kinetics of the σE envelope stress response pathway rather than preinducing the response. This allows bacteria to quickly adapt to sudden and severe periplasmic stress.

The Structure of RseB: A Sensor in Periplasmic Stress Response of E. coli

2007 ◽  
Vol 372 (4) ◽  
pp. 927-941 ◽  
Author(s):  
Petra Wollmann ◽  
Kornelius Zeth
Keyword(s):  
Stress Response ◽  
E Coli ◽  
Periplasmic Stress

scholarly journals The chlamydial periplasmic stress response serine protease cHtrA is secreted into host cell cytosol

2011 ◽  
Vol 11 (1) ◽  
pp. 87 ◽  
Author(s):  
Xiang Wu ◽  
Lei Lei ◽  
Siqi Gong ◽  
Ding Chen ◽  
Rhonda Flores ◽  
...  
Keyword(s):  
Stress Response ◽  
Host Cell ◽  
Serine Protease ◽  
Cell Cytosol ◽  
Host Cell Cytosol ◽  
Periplasmic Stress

CarR, a MarR-family regulator from Corynebacterium glutamicum, modulated antibiotic and aromatic compound resistance

2019 ◽  
Vol 476 (21) ◽  
pp. 3141-3159 ◽  
Author(s):  
Meiru Si ◽  
Can Chen ◽  
Zengfan Wei ◽  
Zhijin Gong ◽  
GuiZhi Li ◽  
...  
Keyword(s):  
Stress Response ◽  
Ligand Binding ◽  
Corynebacterium Glutamicum ◽  
Conformational Changes ◽  
Cysteine Oxidation ◽  
Transcriptional Regulatory ◽  
Ligand Free ◽  
Redox Sensing

Abstract MarR (multiple antibiotic resistance regulator) proteins are a family of transcriptional regulators that is prevalent in Corynebacterium glutamicum. Understanding the physiological and biochemical function of MarR homologs in C. glutamicum has focused on cysteine oxidation-based redox-sensing and substrate metabolism-involving regulators. In this study, we characterized the stress-related ligand-binding functions of the C. glutamicum MarR-type regulator CarR (C. glutamicum antibiotic-responding regulator). We demonstrate that CarR negatively regulates the expression of the carR (ncgl2886)–uspA (ncgl2887) operon and the adjacent, oppositely oriented gene ncgl2885, encoding the hypothetical deacylase DecE. We also show that CarR directly activates transcription of the ncgl2882–ncgl2884 operon, encoding the peptidoglycan synthesis operon (PSO) located upstream of carR in the opposite orientation. The addition of stress-associated ligands such as penicillin and streptomycin induced carR, uspA, decE, and PSO expression in vivo, as well as attenuated binding of CarR to operator DNA in vitro. Importantly, stress response-induced up-regulation of carR, uspA, and PSO gene expression correlated with cell resistance to β-lactam antibiotics and aromatic compounds. Six highly conserved residues in CarR were found to strongly influence its ligand binding and transcriptional regulatory properties. Collectively, the results indicate that the ligand binding of CarR induces its dissociation from the carR–uspA promoter to derepress carR and uspA transcription. Ligand-free CarR also activates PSO expression, which in turn contributes to C. glutamicum stress resistance. The outcomes indicate that the stress response mechanism of CarR in C. glutamicum occurs via ligand-induced conformational changes to the protein, not via cysteine oxidation-based thiol modifications.

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