Purification of Plant Protein Phosphatase PP7 and Evidence for Its Redox Regulation

2001 ◽  
Vol 396 (1) ◽  
pp. 65-70 ◽  
Author(s):  
Alexandra V. Andreeva ◽  
Olga V. Solov'eva ◽  
Dmitry L. Kakuev ◽  
Mikhail A. Kutuzov
Keyword(s):  
Protein Phosphatase ◽  
Redox Regulation ◽  
Plant Protein

scholarly journals The Subcellular Localization of Plant Protein Phosphatase 5 Isoforms Is Determined by Alternative Splicing

2003 ◽  
Vol 133 (2) ◽  
pp. 702-712 ◽  
Author(s):  
Sergio de la Fuente van Bentem ◽  
Jack H. Vossen ◽  
Josephus E.M. Vermeer ◽  
Marianne J. de Vroomen ◽  
Theodorus W.J. Gadella ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Subcellular Localization ◽  
Protein Phosphatase ◽  
Plant Protein ◽  
Protein Phosphatase 5

scholarly journals Reconstruction of spatial structure of plant protein phosphatase type 1, 2a and 4 in complexes with microcystin-LR

1970 ◽  
pp. 339-344
Author(s):  
D. A. Samofalova ◽  
P. A. Karpov ◽  
O. V. Raievskyi ◽  
Ya. B. Blume
Keyword(s):  
Molecular Docking ◽  
Spatial Structure ◽  
Protein Phosphatase ◽  
Protein Phosphatases ◽  
Specific Interaction ◽  
Specific Protein ◽  
Plant Protein ◽  
Scoring Functions ◽  
High Level

Aim. The major toxicity of Microcystin-LR (MCLR) has been ascribed to its potent ability to inhibit serine/threonine-specific protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A). Although MCLR is widely used in animal models its selectivity for these enzymes of plant origin is not still investigated in details for phylogenetically diversified sources. Methods. The spatial structure of plant PP1, PP2A, PP4 protein phosphatases was reconstructed with homology modeling method. Flexible docking of MCLR was performed using CCDC GOLD Suite 5.3. For docking evaluations, GOLD scoring functions were used. Results. Information about amino acids, involved in ligand binding, was obtained from 8 experimentally proved human MCLR-PP1 and PP2A complexes. The sites of microcystin-LR binding with plant protein phosphatases (type-1, 2A and 4) were proved by comparative analysis and molecular docking. A high level of sequence and structure identity of plant and animal phosphatases allow us to conclude similarity of MCLR binding in PP1, PP2A and PP4. Keywords: microcystin-LR, protein phosphatase, specific interaction, molecular docking.

Redox Regulation Of Protein Phosphatase 2A (PP2A) Phosphorylation Prevents Smoke-Induced Lung Injury

2011 ◽  
Author(s):  
Alison M.R. Wallace ◽  
Andrew A. Hardigan ◽  
Adam Gaffney ◽  
Oleg Mirochnitchenko ◽  
Jincy Thankachen ◽  
...  
Keyword(s):  
Lung Injury ◽  
Protein Phosphatase ◽  
Redox Regulation ◽  
Protein Phosphatase 2A ◽  
Phosphatase 2A

Sensing electrons: protein phosphatase redox regulation

2000 ◽  
Vol 25 (11) ◽  
pp. 527-529 ◽  
Author(s):  
Frank Rusnak ◽  
Tiffany Reiter
Keyword(s):  
Protein Phosphatase ◽  
Redox Regulation

Redox Regulation of a Soybean Tyrosine-Specific Protein Phosphatase†

Biochemistry ◽  
2005 ◽  
Vol 44 (21) ◽  
pp. 7696-7703 ◽  
Author(s):  
David P. Dixon ◽  
Anthony P. Fordham-Skelton ◽  
Robert Edwards
Keyword(s):  
Protein Phosphatase ◽  
Redox Regulation ◽  
Specific Protein

Activation of cytochrome c to a peroxidase compound I-type intermediate by H2O2: relevance to redox signalling in apoptosis

2004 ◽  
Vol 71 ◽  
pp. 97-106 ◽  
Author(s):  
Mark Burkitt ◽  
Clare Jones ◽  
Andrew Lawrence ◽  
Peter Wardman
Keyword(s):  
Cytochrome C ◽  
Hydroxyl Radical ◽  
Redox Regulation ◽  
Chemotherapeutic Agents ◽  
Tyrosyl Radical ◽  
Compound I ◽  
Definitive Evidence ◽  
Enhanced Production ◽  
Physico Chemical

The release of cytochrome c from mitochondria during apoptosis results in the enhanced production of superoxide radicals, which are converted to H2O2 by Mn-superoxide dismutase. We have been concerned with the role of cytochrome c/H2O2 in the induction of oxidative stress during apoptosis. Our initial studies showed that cytochrome c is a potent catalyst of 2′,7′-dichlorofluorescin oxidation, thereby explaining the increased rate of production of the fluorophore 2′,7′-dichlorofluorescein in apoptotic cells. Although it has been speculated that the oxidizing species may be a ferryl-haem intermediate, no definitive evidence for the formation of such a species has been reported. Alternatively, it is possible that the hydroxyl radical may be generated, as seen in the reaction of certain iron chelates with H2O2. By examining the effects of radical scavengers on 2′,7′-dichlorofluorescin oxidation by cytochrome c/H2O2, together with complementary EPR studies, we have demonstrated that the hydroxyl radical is not generated. Our findings point, instead, to the formation of a peroxidase compound I species, with one oxidizing equivalent present as an oxo-ferryl haem intermediate and the other as the tyrosyl radical identified by Barr and colleagues [Barr, Gunther, Deterding, Tomer and Mason (1996) J. Biol. Chem. 271, 15498-15503]. Studies with spin traps indicated that the oxo-ferryl haem is the active oxidant. These findings provide a physico-chemical basis for the redox changes that occur during apoptosis. Excessive changes (possibly catalysed by cytochrome c) may have implications for the redox regulation of cell death, including the sensitivity of tumour cells to chemotherapeutic agents.

Signal-regulated oxidation of proteins via MICAL

2020 ◽  
Vol 48 (2) ◽  
pp. 613-620
Author(s):  
Clara Ortegón Salas ◽  
Katharina Schneider ◽  
Christopher Horst Lillig ◽  
Manuela Gellert
Keyword(s):  
Signal Transduction ◽  
Hydrogen Peroxide ◽  
Cell Death ◽  
Redox Regulation ◽  
Signal Transduction Pathways ◽  
Cellular Functions ◽  
Intracellular Signals ◽  
Amino Acid Side Chains ◽  
Specific Receptors ◽  
Sulfur Containing

Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificity, redox signalling requires catalysis, just like phosphorylation signalling requires kinases and phosphatases. While reducing enzymes of both cysteinyl- and methionyl-derivates have been characterised in great detail before, the discovery and characterisation of MICAL proteins evinced the first examples of specific oxidases in signal transduction. This article provides an overview of the functions of MICAL proteins in the redox regulation of cellular functions.

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