scholarly journals Redox regulation of the yeast voltage-gated Ca2+channel homolog Cch1p by glutathionylation of specific cysteine residues

2017 ◽  
Vol 130 (14) ◽  
pp. 2317-2328 ◽  
Author(s):  
Avinash Chandel ◽  
Anand K. Bachhawat
Keyword(s):  
Redox Regulation ◽  
Cysteine Residues ◽  
Voltage Gated

scholarly journals Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis–trans isomerase and redox-related functions

2006 ◽  
Vol 401 (1) ◽  
pp. 287-297 ◽  
Author(s):  
Miriam Laxa ◽  
Janine König ◽  
Karl-Josef Dietz ◽  
Andrea Kandlbinder
Keyword(s):  
Conformational Changes ◽  
Protein Function ◽  
Redox Regulation ◽  
Catalytic Efficiency ◽  
Structural Rearrangement ◽  
Disulfide Bridge ◽  
Cysteine Residues ◽  
Active Centre ◽  
Independent Functions

Cyps (cyclophilins) are ubiquitous proteins of the immunophilin superfamily with proposed functions in protein folding, protein degradation, stress response and signal transduction. Conserved cysteine residues further suggest a role in redox regulation. In order to get insight into the conformational change mechanism and functional properties of the chloroplast-located CYP20-3, site-directed mutagenized cysteine→serine variants were generated and analysed for enzymatic and conformational properties under reducing and oxidizing conditions. Compared with the wild-type form, elimination of three out of the four cysteine residues decreased the catalytic efficiency of PPI (peptidyl-prolyl cis–trans isomerase) activity of the reduced CYP20-3, indicating a regulatory role of dithiol–disulfide transitions in protein function. Oxidation was accompanied by conformational changes with a predominant role in the structural rearrangement of the disulfide bridge formed between Cys54 and Cys171. The rather negative Em (midpoint redox potential) of −319 mV places CYP20-3 into the redox hierarchy of the chloroplast, suggesting the activation of CYP20-3 in the light under conditions of limited acceptor availability for photosynthesis as realized under environmental stress. Chloroplast Prx (peroxiredoxins) were identified as interacting partners of CYP20-3 in a DNA-protection assay. A catalytic role in the reduction of 2-Cys PrxA and 2-Cys PrxB was assigned to Cys129 and Cys171. In addition, it was shown that the isomerization and disulfide-reduction activities are two independent functions of CYP20-3 that both are regulated by the redox state of its active centre.

Plastidic P2 glucose-6P dehydrogenase from poplar is modulated by thioredoxin m-type: Distinct roles of cysteine residues in redox regulation and NADPH inhibition

Plant Science ◽  
2016 ◽  
Vol 252 ◽  
pp. 257-266 ◽  
Author(s):  
Manuela Cardi ◽  
Mirko Zaffagnini ◽  
Alessia De Lillo ◽  
Daniela Castiglia ◽  
Kamel Chibani ◽  
...  
Keyword(s):  
Redox Regulation ◽  
Cysteine Residues

PGluS: prediction of protein S-glutathionylation sites with multiple features and analysis

2015 ◽  
Vol 11 (3) ◽  
pp. 923-929 ◽  
Author(s):  
Xiaowei Zhao ◽  
Qiao Ning ◽  
Meiyu Ai ◽  
Haiting Chai ◽  
Minghao Yin
Keyword(s):  
Protein Stability ◽  
Redox Regulation ◽  
Protein S ◽  
Cysteine Residues ◽  
Post Translational Modification ◽  
Multiple Features ◽  
Mixed Disulfides

S-Glutathionylation is a reversible protein post-translational modification, which generates mixed disulfides between glutathione (GSH) and cysteine residues, playing an important role in regulating protein stability, activity, and redox regulation.

Redox-dependent stability of the γ-glutamylcysteine synthetase enzyme of Escherichia coli: a novel means of redox regulation

2013 ◽  
Vol 449 (3) ◽  
pp. 783-794 ◽  
Author(s):  
Shailesh Kumar ◽  
Neha Kasturia ◽  
Amit Sharma ◽  
Manish Datt ◽  
Anand K. Bachhawat
Keyword(s):  
Escherichia Coli ◽  
Disulfide Bond ◽  
Redox Regulation ◽  
Catalytic Efficiency ◽  
Reduced Form ◽  
Cysteine Residues ◽  
Glutathione Biosynthesis ◽  
Glutamylcysteine Synthetase ◽  
The Stability

Glutathione is a thiol-containing tripeptide that plays important roles in redox-related processes. The first step in glutathione biosynthesis is catalysed by γ-GCS (γ-glutamylcysteine synthetase). The crystal structure of Escherichia coli γ-GCS has revealed the presence of a disulfide bond. As the disulfide-bonding cysteine residues Cys372 and Cys395 are not well conserved among γ-GCS enzymes in this lineage, we have initiated a biochemical genetic strategy to investigate the functional importance of these and other cysteine residues. In a cysteine-free γ-GCS that was non-functional, suppressor analysis yielded combinations of cysteine and aromatic residues at the position of the disulfide bond, and one mutant that lacked any cysteine residues. Kinetic analysis of the wild-type and mutant enzymes revealed that the disulfide bond was not involved in determining the affinity of the enzyme towards its substrate, but had an important role in determining the stability of the protein, and its catalytic efficiency. We show that in vivo the γ-GCS enzyme can also exist in a reduced form and that the mutants lacking the disulfide bond show a decreased half-life. These results demonstrate a novel means of regulation of γ-GCS by the redox environment that works by an alteration in its stability.

scholarly journals Redox Regulation of Neuronal Voltage-Gated Calcium Channels

2014 ◽  
Vol 21 (6) ◽  
pp. 880-891 ◽  
Author(s):  
Slobodan M. Todorovic ◽  
Vesna Jevtovic-Todorovic
Keyword(s):  
Calcium Channels ◽  
Redox Regulation ◽  
Voltage Gated ◽  
Voltage Gated Calcium Channels

scholarly journals Role of cysteine residues in regulation of p53 function.

1995 ◽  
Vol 15 (7) ◽  
pp. 3892-3903 ◽  
Author(s):  
R Rainwater ◽  
D Parks ◽  
M E Anderson ◽  
P Tegtmeyer ◽  
K Mann
Keyword(s):  
Dna Binding ◽  
Transcriptional Activation ◽  
Redox Regulation ◽  
Binding Domain ◽  
Zinc Binding ◽  
Cysteine Residues ◽  
Dna Binding Domain ◽  
Site Specific ◽  
Functional Consequences

Previous studies of p53 have implicated cysteine residues in site-specific DNA binding via zinc coordination and redox regulation (P. Hainaut and J. Milner, Cancer Res. 53:4469-4473, 1993; T. R. Hupp, D. W. Meek, C. A. Midgley, and D. P. Lane, Nucleic Acids Res. 21:3167-3174, 1993). We show here that zinc binding and redox regulation are, at least in part, distinct determinants of the binding of p53 to DNA. Moreover, by substituting serine for each cysteine in murine p53, we have investigated the roles of individual cysteines in the regulation of p53 function. Substitution of serine for cysteine at position 40, 179, 274, 293, or 308 had little or no effect on p53 function. In contrast, replacement of cysteine at position 173, 235, or 239 markedly reduced in vitro DNA binding, completely blocked transcriptional activation, and led to a striking enhancement rather than a suppression of transformation by p53. These three cysteines have been implicated in zinc binding by X-ray diffraction studies (Y. Cho, S. Gorina, P.D. Jeffrey, and N.P. Pavletich, Science 265:346-355, 1994); our studies demonstrate the functional consequences of the inability of the central DNA-binding domain of p53 to studies demonstrate the functional consequences of the inability of the central DNA-binding domain of p53 to bind zinc. Lastly, substitutions for cysteines at position 121, 132, 138, or 272 partially blocked both transactivation and the suppression of transformation by p53. These four cysteines are located in the loop-sheet-helix region of the site-specific DNA-binding domain of p53. Like the cysteines in the zinc-binding region, therefore, these cysteines may cooperate to modulate the structure of the DNA-binding domain. Our findings argue that p53 is subject to more than one level of conformational modulation through oxidation-reduction of cysteines at or near the p53-DNA interface.

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