scholarly journals Copper stress response in yeastRhodotorula mucilaginosaAN5 isolated from sea ice, Antarctic

2018 ◽  
Vol 8 (3) ◽  
pp. e00657 ◽  
Author(s):  
Guangfeng Kan ◽  
Xiaofei Wang ◽  
Jie Jiang ◽  
Chengsheng Zhang ◽  
Minglei Chi ◽  
...  
Keyword(s):  
Stress Response ◽  
Sea Ice ◽  
Copper Stress ◽  
Copper Stress Response

Proteomic characterization of copper stress response in Elsholtzia splendens roots and leaves

2009 ◽  
Vol 71 (3) ◽  
pp. 251-263 ◽  
Author(s):  
Feng Li ◽  
Jiyan Shi ◽  
Chaofeng Shen ◽  
Guangcun Chen ◽  
Shaoping Hu ◽  
...  
Keyword(s):  
Stress Response ◽  
Copper Stress ◽  
Elsholtzia Splendens ◽  
Copper Stress Response

Proteomic characterization of copper stress response inCannabis sativa roots

PROTEOMICS ◽  
2007 ◽  
Vol 7 (7) ◽  
pp. 1121-1130 ◽  
Author(s):  
Elisa Bona ◽  
Francesco Marsano ◽  
Maria Cavaletto ◽  
Graziella Berta
Keyword(s):  
Stress Response ◽  
Copper Stress ◽  
Copper Stress Response

Analysis of Gene Expression in Response to Copper Stress in Acidithiobacillus ferrooxidans Strain D2, Isolated from a Copper Bioleaching Operation

2013 ◽  
Vol 825 ◽  
pp. 157-161 ◽  
Author(s):  
Camila N. Salazar ◽  
Mauricio Acosta ◽  
Pedro A. Galleguillos ◽  
Amir Shmaryahu ◽  
Raquel Quatrini ◽  
...  
Keyword(s):  
Stress Response ◽  
Acidithiobacillus Ferrooxidans ◽  
Dna Microarrays ◽  
Copper Stress ◽  
Molecular Response ◽  
Expression Of Genes ◽  
Genes Encoding ◽  
High Concentrations ◽  
P Type ◽  
Upregulated Genes

Acidithiobacillus ferrooxidans strain D2 was isolated from a copper bioleaching operation in Atacama Desert, Chile. Copper is widely used as cofactor in proteins but high concentrations of copper are toxic. Cells require certain mechanisms to maintain the copper homeostasis and avoid toxic effects of high intracellular concentration. The molecular response of A. ferrooxidans strain D2 grown in the presence/absence of copper was examined using a A. ferrooxidans whole-genome DNA microarrays. Roughly 23% of 3,147 genes represented on the microarray were differentially expressed; about 9% of them were upregulated in the presence of copper. Among the upregulated genes, those encoding for the copper efflux protein (CusA) and for the copper-translocating P-type ATPase (CopA) were upregulated. The expression of genes encoding proteins related to iron transport was repressed. Similarly, genes related with assimilative metabolism of sulfur (L-cysteine biosynthesis) cysB, cysJ, cysI, CysD-2 and cysN were upregulated. Our results show that when A. ferrooxidans strain D2 was challenged with high copper concentrations, genes related to copper stress response were upregulated as well as others that have not been reported to be related to that mechanism. In addition, some genes related to other metabolic pathways were repressed, probably because of the energy cost of the stress response.

scholarly journals Copper Induction of Lactate Oxidase of Lactococcus lactis: a Novel Metal Stress Response

2007 ◽  
Vol 189 (16) ◽  
pp. 5947-5954 ◽  
Author(s):  
Olivier Barré ◽  
Frédéric Mourlane ◽  
Marc Solioz
Keyword(s):  
Stress Response ◽  
Lactococcus Lactis ◽  
Regulatory Element ◽  
Copper Stress ◽  
Lactate Oxidase ◽  
Two Dimensional Gel Electrophoresis ◽  
Real Time Quantitative Pcr ◽  
Novel Proteins

ABSTRACT Lactococcus lactis IL1403, a lactic acid bacterium widely used for food fermentation, is often exposed to stress conditions. One such condition is exposure to copper, such as in cheese making in copper vats. Copper is an essential micronutrient in prokaryotes and eukaryotes but can be toxic if in excess. Thus, copper homeostatic mechanisms, consisting chiefly of copper transporters and their regulators, have evolved in all organisms to control cytoplasmic copper levels. Using proteomics to identify novel proteins involved in the response of L. lactis IL1403 to copper, cells were exposed to 200 μM copper sulfate for 45 min, followed by resolution of the cytoplasmic fraction by two-dimensional gel electrophoresis. One protein strongly induced by copper was LctO, which was shown to be a NAD-independent lactate oxidase. It catalyzed the conversion of lactate to pyruvate in vivo and in vitro. Copper, cadmium, and silver induced LctO, as shown by real-time quantitative PCR. A copper-regulatory element was identified in the 5′ region of the lctO gene and shown to interact with the CopR regulator, encoded by the unlinked copRZA operon. Induction of LctO by copper represents a novel copper stress response, and we suggest that it serves in the scavenging of molecular oxygen.

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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