Redox regulation of plant S-nitrosoglutathione reductase
activity through post-translational modifications of cysteine
residues

J 2017

Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues

TICHA, Tereza, Jan LOCHMAN, Lucie ČINČALOVÁ, Lenka LUHOVÁ, Marek PETŘIVALSKÝ et. al.

Basic information

Original name

Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues

Authors

TICHA, Tereza (203 Czech Republic), Jan LOCHMAN (203 Czech Republic, guarantor, belonging to the institution), Lucie ČINČALOVÁ (203 Czech Republic), Lenka LUHOVÁ (203 Czech Republic) and Marek PETŘIVALSKÝ (203 Czech Republic)

Edition

Biochemical and biophysical research communications, SAN DIEGO, ACADEMIC PRESS INC ELSEVIER SCIENCE, 2017, 0006-291X

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 2.559

RIV identification code

RIV/00216224:14310/17:00100142

Organization unit

Faculty of Science

DOI

http://dx.doi.org/10.1016/j.bbrc.2017.10.090

UT WoS

000416615300006

Keywords in English

Nitric oxide; Post-translational modifications; Redox regulation; S-nitrosoglutathione reductase; S-nitrosation

Abstract

V originále

Nitric oxide (NO) is considered as a signalling molecule involved in a variety of important physiological and pathological processes in plant and animal systems. The major pathway of NO reactions in vivo represents S-nitrosation of thiols to form S-nitrosothiols. S-nitrosoglutathione reductase (GSNOR) is the key enzyme in the degradation pathway of S-nitrosoglutathione (GSNO), a low-molecular weight adduct of NO and glutathione. GSNOR indirectly regulates the level of protein S-nitrosothiol in the cells. This study was focused on the dynamic regulation of the activity of plant GSNORs through reversible S-nitrosation and/or oxidative modifications of target cysteine residues. Pre-incubation with NO/NO- donors or hydrogen peroxide resulted in a decreased reductase and dehydrogenase activity of all studied plant GSNORs. Incubation with thiol reducing agent completely reversed inhibitory effects of nitrosative modifications and partially also oxidative inhibition. In biotin-labelled samples, S-nitrosation of plant GSNORs was confirmed after immunodetection and using mass spectrometry S-nitrosation of conserved Cys271 was identified in tomato GSNOR. Negative regulation of constitutive GSNOR activity in vivo by nitrosative or oxidative modifications might present an important mechanism to control GSNO levels, a critical mediator of the downstream signalling effects of NO, as well as for formaldehyde detoxification in dehydrogenase reaction mode. (C) 2017 Elsevier Inc. All rights reserved.

Citovat

TICHA, Tereza, Jan LOCHMAN, Lucie ČINČALOVÁ, Lenka LUHOVÁ and Marek PETŘIVALSKÝ. Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues. Biochemical and biophysical research communications. SAN DIEGO: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2017, vol. 494, 1-2, p. 27-33. ISSN 0006-291X. Available from: https://dx.doi.org/10.1016/j.bbrc.2017.10.090.

@article{1409625,
   author = {Ticha, Tereza and Lochman, Jan and Činčalová, Lucie and Luhová, Lenka and Petřivalský, Marek},
   article_location = {SAN DIEGO},
   article_number = {1-2},
   doi = {http://dx.doi.org/10.1016/j.bbrc.2017.10.090},
   keywords = {Nitric oxide; Post-translational modifications; Redox regulation; S-nitrosoglutathione reductase; S-nitrosation},
   language = {eng},
   issn = {0006-291X},
   journal = {Biochemical and biophysical research communications},
   title = {Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues},
   volume = {494},
   year = {2017}
}

TY  - JOUR
ID  - 1409625
AU  - Ticha, Tereza - Lochman, Jan - Činčalová, Lucie - Luhová, Lenka - Petřivalský, Marek
PY  - 2017
TI  - Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues
JF  - Biochemical and biophysical research communications
VL  - 494
IS  - 1-2
SP  - 27-33
EP  - 27-33
PB  - ACADEMIC PRESS INC ELSEVIER SCIENCE
SN  - 0006291X
KW  - Nitric oxide
KW  - Post-translational modifications
KW  - Redox regulation
KW  - S-nitrosoglutathione reductase
KW  - S-nitrosation
N2  - Nitric oxide (NO) is considered as a signalling molecule involved in a variety of important physiological and pathological processes in plant and animal systems. The major pathway of NO reactions in vivo represents S-nitrosation of thiols to form S-nitrosothiols. S-nitrosoglutathione reductase (GSNOR) is the key enzyme in the degradation pathway of S-nitrosoglutathione (GSNO), a low-molecular weight adduct of NO and glutathione. GSNOR indirectly regulates the level of protein S-nitrosothiol in the cells. This study was focused on the dynamic regulation of the activity of plant GSNORs through reversible S-nitrosation and/or oxidative modifications of target cysteine residues. Pre-incubation with NO/NO- donors or hydrogen peroxide resulted in a decreased reductase and dehydrogenase activity of all studied plant GSNORs. Incubation with thiol reducing agent completely reversed inhibitory effects of nitrosative modifications and partially also oxidative inhibition. In biotin-labelled samples, S-nitrosation of plant GSNORs was confirmed after immunodetection and using mass spectrometry S-nitrosation of conserved Cys271 was identified in tomato GSNOR. Negative regulation of constitutive GSNOR activity in vivo by nitrosative or oxidative modifications might present an important mechanism to control GSNO levels, a critical mediator of the downstream signalling effects of NO, as well as for formaldehyde detoxification in dehydrogenase reaction mode. (C) 2017 Elsevier Inc. All rights reserved.
ER  -

TICHA, Tereza, Jan LOCHMAN, Lucie ČINČALOVÁ, Lenka LUHOVÁ and Marek PETŘIVALSKÝ. Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues. \textit{Biochemical and biophysical research communications}. SAN DIEGO: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2017, vol.~494, 1-2, p.~27-33. ISSN~0006-291X. Available from: https://dx.doi.org/10.1016/j.bbrc.2017.10.090.

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