scholarly journals Protein acetylation affects acetate metabolism, motility and acid stress response in Escherichia coli

2014 ◽  
Vol 10 (11) ◽  
pp. 762 ◽  
Author(s):  
Sara Castaño‐Cerezo ◽  
Vicente Bernal ◽  
Harm Post ◽  
Tobias Fuhrer ◽  
Salvatore Cappadona ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Stress Response ◽  
Acid Stress ◽  
Acetate Metabolism ◽  
Protein Acetylation ◽  
Acid Stress Response

scholarly journals Inactivation of PadR, the Repressor of the Phenolic Acid Stress Response, by Molecular Interaction with Usp1, a Universal Stress Protein from Lactobacillus plantarum, in Escherichia coli

2009 ◽  
Vol 75 (16) ◽  
pp. 5273-5283 ◽  
Author(s):  
Jérôme Gury ◽  
Hélène Seraut ◽  
Ngoc Phuong Tran ◽  
Lise Barthelmebs ◽  
Stéphanie Weidmann ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Stress Response ◽  
Lactobacillus Plantarum ◽  
Phenolic Acid ◽  
Stress Protein ◽  
Acid Stress ◽  
Universal Stress Protein ◽  
E Coli ◽  
Gram Positive Bacteria ◽  
Acid Stress Response

ABSTRACT The phenolic acid decarboxylase gene padA is involved in the phenolic acid stress response (PASR) in gram-positive bacteria. In Lactobacillus plantarum, the padR gene encodes the negative transcriptional regulator of padA and is cotranscribed with a downstream gene, usp1, which encodes a putative universal stress protein (USP), Usp1, of unknown function. The usp1 gene is overexpressed during the PASR. However, the role and the mechanism of action of the USPs are unknown in gram-positive bacteria. Therefore, to gain insights into the role of USPs in the PASR; (i) a usp1 deletion mutant was constructed; (ii) the two genes padR and usp1 were coexpressed with padA under its own promoter as a reporter gene in Escherichia coli; and (iii) molecular in vitro interactions between the PadR, Usp1, and the padA promoter were studied. Although the usp1 mutant strain retained phenolic acid-dependent PAD activity, it displayed a greater sensitivity to strong acidic conditions compared to that of the wild-type strain. PadR cannot be inactivated directly by phenolic acid in E. coli recombinant cultures but is inactivated by Usp1 when the two proteins are coexpressed in E. coli. The PadR inactivation observed in recombinant E. coli cells was supported by electrophoretic mobility shift assays. Although Usp1 seems not to be absolutely required for the PASR, its capacity to inactivate PadR indicates that it could serve as an important mediator in acid stress response mechanisms through its capacity to interact with transcriptional regulators.

scholarly journals Supramolecular assembly of the Escherichia coli LdcI upon acid stress

2020 ◽  
Vol 118 (2) ◽  
pp. e2014383118
Author(s):  
Matthew Jessop ◽  
Clarissa Liesche ◽  
Jan Felix ◽  
Ambroise Desfosses ◽  
Megghane Baulard ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Stress Response ◽  
Fluorescent Protein ◽  
Mutational Analysis ◽  
Acid Stress ◽  
Low Ph ◽  
Supramolecular Organization ◽  
Cell Periphery ◽  
Wide Field ◽  
Acid Stress Response

Pathogenic and commensal bacteria often have to resist the harsh acidity of the host stomach. The inducible lysine decarboxylase LdcI buffers the cytosol and the local extracellular environment to ensure enterobacterial survival at low pH. Here, we investigate the acid stress-response regulation of Escherichia coli LdcI by combining biochemical and biophysical characterization with negative stain and cryoelectron microscopy (cryo-EM) and wide-field and superresolution fluorescence imaging. Due to deleterious effects of fluorescent protein fusions on native LdcI decamers, we opt for three-dimensional localization of nanobody-labeled endogenous wild-type LdcI in acid-stressed E. coli cells and show that it organizes into distinct patches at the cell periphery. Consistent with recent hypotheses that in vivo clustering of metabolic enzymes often reflects their polymerization as a means of stimulus-induced regulation, we show that LdcI assembles into filaments in vitro at physiologically relevant low pH. We solve the structures of these filaments and of the LdcI decamer formed at neutral pH by cryo-EM and reveal the molecular determinants of LdcI polymerization, confirmed by mutational analysis. Finally, we propose a model for LdcI function inside the enterobacterial cell, providing a structural and mechanistic basis for further investigation of the role of its supramolecular organization in the acid stress response.

scholarly journals Acid stress response in Escherichia coli: mechanism of regulation of gadA transcription by RcsB and GadE

2010 ◽  
Vol 38 (11) ◽  
pp. 3546-3554 ◽  
Author(s):  
Marie-Pierre Castanié-Cornet ◽  
Kaymeuang Cam ◽  
Bénédicte Bastiat ◽  
Adeline Cros ◽  
Patricia Bordes ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Stress Response ◽  
Acid Stress ◽  
Acid Stress Response

MgrB affects the acid stress response of Escherichia coli by modulating the expression of iraM

2019 ◽  
Vol 366 (11) ◽  
Author(s):  
Jintian Xu ◽  
Ting Li ◽  
Yunrong Gao ◽  
Jiaoyu Deng ◽  
Jing Gu
Keyword(s):  
Escherichia Coli ◽  
Stress Response ◽  
Acid Stress ◽  
Acid Stress Response

Acid stress response in environmental and clinical strains of enteric bacteria

2012 ◽  
Vol 7 (6) ◽  
pp. 495-505 ◽  
Author(s):  
Gabriel J. Swenson ◽  
J. Stochastic ◽  
Franklyn F. Bolander ◽  
Richard A. Long
Keyword(s):  
Stress Response ◽  
Acid Stress ◽  
Enteric Bacteria ◽  
Clinical Strains ◽  
Acid Stress Response

Integrative multiomics analysis of the acid stress response of Oenococcus oeni mutants at different growth stages

2021 ◽  
pp. 103905
Author(s):  
Qiling Chen ◽  
Xiangke Yang ◽  
Qiang Meng ◽  
Lili Zhao ◽  
Yuxin Yuan ◽  
...  
Keyword(s):  
Stress Response ◽  
Acid Stress ◽  
Oenococcus Oeni ◽  
Growth Stages ◽  
Acid Stress Response ◽  
Different Growth Stages
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