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.

Základní údaje

Originální název

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

Autoři

TICHA, Tereza (203 Česká republika), Jan LOCHMAN (203 Česká republika, garant, domácí), Lucie ČINČALOVÁ (203 Česká republika), Lenka LUHOVÁ (203 Česká republika) a Marek PETŘIVALSKÝ (203 Česká republika)

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 2.559

Kód RIV

RIV/00216224:14310/17:00100142

Organizační jednotka

Přírodovědecká fakulta

DOI

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

UT WoS

000416615300006

Klíčová slova anglicky

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

Štítky

NZ, rivok

Změněno: 11. 4. 2018 12:11, Ing. Nicole Zrilić

Anotace

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 a 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, roč. 494, 1-2, s. 27-33. ISSN 0006-291X. Dostupné z: 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 a 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, roč.~494, 1-2, s.~27-33. ISSN~0006-291X. Dostupné z: https://dx.doi.org/10.1016/j.bbrc.2017.10.090.

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