Regulatory thiol oxidation in chloroplast metabolism, oxidative stress response and environmental signaling in plants

2020 ◽  
Vol 477 (10) ◽  
pp. 1865-1878 ◽  
Author(s):  
Lara Vogelsang ◽  
Karl-Josef Dietz
Keyword(s):  
Protein Function ◽  
Fundamental Property ◽  
Redox Potentials ◽  
Thiol Oxidation ◽  
Cellular Regulation ◽  
Mixed Disulfide ◽  
Thiol Redox State ◽  
Chloroplast Metabolism ◽  
Thiol Redox ◽  
Cellular Compartments

The antagonism between thiol oxidation and reduction enables efficient control of protein function and is used as central mechanism in cellular regulation. The best-studied mechanism is the dithiol-disulfide transition in the Calvin Benson Cycle in photosynthesis, including mixed disulfide formation by glutathionylation. The adjustment of the proper thiol redox state is a fundamental property of all cellular compartments. The glutathione redox potential of the cytosol, stroma, matrix and nucleoplasm usually ranges between −300 and −320 mV. Thiol reduction proceeds by short electron transfer cascades consisting of redox input elements and redox transmitters such as thioredoxins. Thiol oxidation ultimately is linked to reactive oxygen species (ROS) and reactive nitrogen species (RNS). Enhanced ROS production under stress shifts the redox network to more positive redox potentials. ROS do not react randomly but primarily with few specific redox sensors in the cell. The most commonly encountered reaction within the redox regulatory network however is the disulfide swapping. The thiol oxidation dynamics also involves transnitrosylation. This review compiles present knowledge on this network and its central role in sensing environmental cues with focus on chloroplast metabolism.

scholarly journals Nucleoredoxin-Dependent Targets and Processes in Neuronal Cells

2018 ◽  
Vol 2018 ◽  
pp. 1-11 ◽  
Author(s):  
Claudia Urbainsky ◽  
Rolf Nölker ◽  
Marcel Imber ◽  
Adrian Lübken ◽  
Jörg Mostertz ◽  
...  
Keyword(s):  
Redox State ◽  
Redox Regulation ◽  
Neuroblastoma Cells ◽  
Neuronal Cell ◽  
Biological Processes ◽  
Quantitative Mass Spectrometry ◽  
Mixed Disulfide ◽  
Protein Thiols ◽  
Thiol Redox State ◽  
Thiol Redox

Nucleoredoxin (Nrx) is an oxidoreductase of the thioredoxin family of proteins. It was shown to act as a signal transducer in some pathways; however, so far, no comprehensive analysis of its regulated substrates and functions was available. Here, we used a combination of two different strategies to fill this gap. First, we analyzed the thiol-redox state of the proteome of SH-SY5Y neuroblastoma cells depleted of Nrx compared to control cells using a differential thiol-labeling technique and quantitative mass spectrometry. 171 proteins were identified with an altered redox state; 161 of these were more reduced in the absence of Nrx. This suggests functions of Nrx in the oxidation of protein thiols. Second, we utilized the active site mutant Cys208Ser of Nrx, which stabilizes a mixed disulfide intermediate with its substrates and therefore trapped interacting proteins from the mouse brain (identifying 1710 proteins) and neuronal cell culture extracts (identifying 609 proteins). Profiling of the affected biological processes and molecular functions in cells of neuronal origin suggests numerous functions of Nrx in the redox regulation of metabolic pathways, cellular morphology, and signal transduction. These results characterize Nrx as a cellular oxidase that itself may be oxidized by the formation of disulfide relays with peroxiredoxins.

scholarly journals The thiol redox state of lymphoid organs is modified by immunization: Role of different immune cell populations

2008 ◽  
Vol 38 (9) ◽  
pp. 2419-2425 ◽  
Author(s):  
Patrizia Castellani ◽  
Giovanna Angelini ◽  
Laura Delfino ◽  
Andrea Matucci ◽  
Anna Rubartelli
Keyword(s):  
Redox State ◽  
Immune Cell ◽  
Lymphoid Organs ◽  
Cell Populations ◽  
Thiol Redox State ◽  
Thiol Redox

scholarly journals The Effectiveness of Glutathione Redox Status as a Possible Tumor Marker in Colorectal Cancer

2021 ◽  
Vol 22 (12) ◽  
pp. 6183
Author(s):  
Delia Acevedo-León ◽  
Lidia Monzó-Beltrán ◽  
Segundo Ángel Gómez-Abril ◽  
Nuria Estañ-Capell ◽  
Natalia Camarasa-Lillo ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Redox State ◽  
Reduced Glutathione ◽  
Redox Status ◽  
Oxidation Products ◽  
Interventional Study ◽  
Thiol Redox State ◽  
Thiol Redox ◽  
Glutathione Redox

The role of oxidative stress (OS) in cancer is a matter of great interest due to the implication of reactive oxygen species (ROS) and their oxidation products in the initiation of tumorigenesis, its progression, and metastatic dissemination. Great efforts have been made to identify the mechanisms of ROS-induced carcinogenesis; however, the validation of OS byproducts as potential tumor markers (TMs) remains to be established. This interventional study included a total of 80 colorectal cancer (CRC) patients and 60 controls. By measuring reduced glutathione (GSH), its oxidized form (GSSG), and the glutathione redox state in terms of the GSSG/GSH ratio in the serum of CRC patients, we identified significant changes as compared to healthy subjects. These findings are compatible with the effectiveness of glutathione as a TM. The thiol redox state showed a significant increase towards oxidation in the CRC group and correlated significantly with both the tumor state and the clinical evolution. The sensitivity and specificity of serum glutathione levels are far above those of the classical TMs CEA and CA19.9. We conclude that the GSSG/GSH ratio is a simple assay which could be validated as a novel clinical TM for the diagnosis and monitoring of CRC.

scholarly journals Detecting intracellular thiol redox state in leukaemia and heterogeneous immune cell populations: An optimised protocol for digital flow cytometers

MethodsX ◽  
2018 ◽  
Vol 5 ◽  
pp. 1473-1483 ◽  
Author(s):  
Alex J. Wadley ◽  
Rhys G. Morgan ◽  
Kate J. Heesom ◽  
Paul S. Hole ◽  
Steven J. Coles
Keyword(s):  
Redox State ◽  
Immune Cell ◽  
Cell Populations ◽  
Thiol Redox State ◽  
Thiol Redox

scholarly journals Increased hepatic telomerase activity in a rat model of iron overload: A role for altered thiol redox state?

2007 ◽  
Vol 42 (2) ◽  
pp. 228-235 ◽  
Author(s):  
Kyle E. Brown ◽  
M. Meleah Mathahs ◽  
Kimberly A. Broadhurst ◽  
Mitchell C. Coleman ◽  
Lisa A. Ridnour ◽  
...  
Keyword(s):  
Iron Overload ◽  
Rat Model ◽  
Redox State ◽  
Telomerase Activity ◽  
Thiol Redox State ◽  
Thiol Redox

scholarly journals Hypoxia elicits broad and systematic changes in protein subcellular localization

2011 ◽  
Vol 301 (4) ◽  
pp. C913-C928 ◽  
Author(s):  
Robert Michael Henke ◽  
Ranita Ghosh Dastidar ◽  
Ajit Shah ◽  
Daniela Cadinu ◽  
Xiao Yao ◽  
...  
Keyword(s):  
Protein Function ◽  
Protein Localization ◽  
Cell Periphery ◽  
Protein Distribution ◽  
Yeast Saccharomyces Cerevisiae ◽  
Transcriptional Regulatory ◽  
Chromatin Remodeling Complexes ◽  
Oxygen Signaling ◽  
Cellular Compartments ◽  
Control Protein

Oxygen provides a crucial energy source in eukaryotic cells. Hence, eukaryotes ranging from yeast to humans have developed sophisticated mechanisms to respond to changes in oxygen levels. Regulation of protein localization, like protein modifications, can be an effective mechanism to control protein function and activity. However, the contribution of protein localization in oxygen signaling has not been examined on a genomewide scale. Here, we examine how hypoxia affects protein distribution on a genomewide scale in the model eukaryote, the yeast Saccharomyces cerevisiae . We demonstrate, by live cell imaging, that hypoxia alters the cellular distribution of 203 proteins in yeast. These hypoxia-redistributed proteins include an array of proteins with important functions in various organelles. Many of them are nuclear and are components of key regulatory complexes, such as transcriptional regulatory and chromatin remodeling complexes. Under hypoxia, these proteins are synthesized and retained in the cytosol. Upon reoxygenation, they relocalize effectively to their normal cellular compartments, such as the nucleus, mitochondria, endoplasmic reticulum, and cell periphery. The resumption of the normal cellular locations of many proteins can occur even when protein synthesis is inhibited. Furthermore, we show that the changes in protein distribution induced by hypoxia follow a slower trajectory than those induced by reoxygenation. These results show that the regulation of protein localization is a common and potentially dominant mechanism underlying oxygen signaling and regulation. These results may have broad implications in understanding oxygen signaling and hypoxia responses in higher eukaryotes such as humans.

scholarly journals Characterization of cellular oxidative stress response by stoichiometric redox proteomics

2020 ◽  
Author(s):  
Tong Zhang ◽  
Matthew J. Gaffrey ◽  
Xiaolu Li ◽  
Wei-Jun Qian
Keyword(s):  
Oxidative Stress ◽  
Posttranslational Modifications ◽  
Protein Function ◽  
Regulatory Networks ◽  
Total Oxidation ◽  
Redox Proteomics ◽  
Thiol Redox ◽  
Cysteine Thiols ◽  
In Cells

The thiol redox proteome refers to all proteins whose cysteine thiols are subjected to various redox-dependent posttranslational modifications (PTMs) including S-glutathionylation (SSG), S-nitrosylation (SNO), S-sulfenylation (SOH), and S-sulfhydration (SSH). These modifications can impact various aspects of protein function such as activity, binding, conformation, localization, and interactions with other molecules. To identify novel redox proteins in signaling and regulation, it is highly desirable to have robust redox proteomics methods that can provide global, site-specific, and stoichiometric quantification of redox PTMs. Mass spectrometry (MS)-based redox proteomics has emerged as the primary platform for broad characterization of thiol PTMs in cells and tissues. Herein we review recent advances in MS-based redox proteomics approaches for quantitative profiling of redox PTMs at physiological or oxidative stress conditions and highlight some recent applications. Considering the relative maturity of available methods, emphasis will be on two types of modifications: 1) total oxidation (i.e., all reversible thiol modifications), the level of which represents the overall redox state, and 2) S-glutathionylation, a major form of reversible thiol oxidation. We also discuss the significance of stoichiometric measurements of thiol PTMs as well as future perspectives towards a better understanding of cellular redox regulatory networks in cells and tissues

scholarly journals LmTDRM Database: A Comprehensive Database on Thiol Metabolic Gene/Gene Products in Listeria monocytogenes EGDe

2014 ◽  
Vol 11 (1) ◽  
pp. 17-29
Author(s):  
Vanishree Srinivas ◽  
Shubha Gopal
Keyword(s):  
Oxidative Stress ◽  
Listeria Monocytogenes ◽  
Protein Function ◽  
Model Organism ◽  
Reducing Power ◽  
Major Step ◽  
Redox Metabolism ◽  
Interaction Database ◽  
Insertion Elements ◽  
Thiol Redox

Summary There are a number of databases on the Listeria species and about their genome. However, these databases do not specifically address a set of network that is important in defence mechanism of the bacteria. Listeria monocytogenes EGDe is a well-established intracellular model organism to study host pathogenicity because of its versatility in the host environment. Here, we have focused on thiol disulphide redox metabolic network proteins, specifically in L. monocytogenes EGDe. The thiol redox metabolism is involved in oxidative stress mechanism and is found in all living cells. It functions to maintain the thiol disulphide balance required for protein folding by providing reducing power. Nevertheless, they are involved in the reversible oxidation of thiol groups in biomolecules by creating disulphide bonds; therefore, the term thiol disulphide redox metabolism (TDRM). TDRM network genes play an important role in oxidative stress mechanism and during host-pathogen interaction. Therefore, it is essential to have detailed information on these proteins with regard to other bacteria and its genome analysis to understand the presence of tRNA, transposons, and insertion elements for horizontal gene transfer. LmTDRM database is a new comprehensive web-based database on thiol proteins and their functions. It includes: Description, Search, TDRM analysis, and genome viewer. The quality of these data has been evaluated before they were aggregated to produce a final representation. The web interface allows for various queries to understand the protein function and their annotation with respect to their relationship with other bacteria. LmTDRM is a major step towards the development of databases on thiol disulphide redox proteins; it would definitely help researchers to understand the mechanism of these proteins and their interaction. Database URL: www.lmtdrm.com

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