Signaling by hydrogen sulfide and cyanide through post-translational modification. (14th May 2019)
- Record Type:
- Journal Article
- Title:
- Signaling by hydrogen sulfide and cyanide through post-translational modification. (14th May 2019)
- Main Title:
- Signaling by hydrogen sulfide and cyanide through post-translational modification
- Authors:
- Gotor, Cecilia
García, Irene
Aroca, Ángeles
Laureano-Marín, Ana M
Arenas-Alfonseca, Lucía
Jurado-Flores, Ana
Moreno, Inmaculada
Romero, Luis C - Editors:
- Kopriva, Stanislav
- Abstract:
- Abstract: Two cysteine metabolism-related molecules, hydrogen sulfide and hydrogen cyanide, which are considered toxic, have now been considered as signaling molecules. Hydrogen sulfide is produced in chloroplasts through the activity of sulfite reductase and in the cytosol and mitochondria by the action of sulfide-generating enzymes, and regulates/affects essential plant processes such as plant adaptation, development, photosynthesis, autophagy, and stomatal movement, where interplay with other signaling molecules occurs. The mechanism of action of sulfide, which modifies protein cysteine thiols to form persulfides, is related to its chemical features. This post-translational modification, called persulfidation, could play a protective role for thiols against oxidative damage. Hydrogen cyanide is produced during the biosynthesis of ethylene and camalexin in non-cyanogenic plants, and is detoxified by the action of sulfur-related enzymes. Cyanide functions include the breaking of seed dormancy, modifying the plant responses to biotic stress, and inhibition of root hair elongation. The mode of action of cyanide is under investigation, although it has recently been demonstrated to perform post-translational modification of protein cysteine thiols to form thiocyanate, a process called S -cyanylation. Therefore, the signaling roles of sulfide and most probably of cyanide are performed through the modification of specific cysteine residues, altering protein functions. Abstract :Abstract: Two cysteine metabolism-related molecules, hydrogen sulfide and hydrogen cyanide, which are considered toxic, have now been considered as signaling molecules. Hydrogen sulfide is produced in chloroplasts through the activity of sulfite reductase and in the cytosol and mitochondria by the action of sulfide-generating enzymes, and regulates/affects essential plant processes such as plant adaptation, development, photosynthesis, autophagy, and stomatal movement, where interplay with other signaling molecules occurs. The mechanism of action of sulfide, which modifies protein cysteine thiols to form persulfides, is related to its chemical features. This post-translational modification, called persulfidation, could play a protective role for thiols against oxidative damage. Hydrogen cyanide is produced during the biosynthesis of ethylene and camalexin in non-cyanogenic plants, and is detoxified by the action of sulfur-related enzymes. Cyanide functions include the breaking of seed dormancy, modifying the plant responses to biotic stress, and inhibition of root hair elongation. The mode of action of cyanide is under investigation, although it has recently been demonstrated to perform post-translational modification of protein cysteine thiols to form thiocyanate, a process called S -cyanylation. Therefore, the signaling roles of sulfide and most probably of cyanide are performed through the modification of specific cysteine residues, altering protein functions. Abstract : Sulfide and cyanide are considered signaling molecules, acting through post-translational modification of cysteine residues of proteins. … (more)
- Is Part Of:
- Journal of experimental botany. Volume 70:Number 16(2019)
- Journal:
- Journal of experimental botany
- Issue:
- Volume 70:Number 16(2019)
- Issue Display:
- Volume 70, Issue 16 (2019)
- Year:
- 2019
- Volume:
- 70
- Issue:
- 16
- Issue Sort Value:
- 2019-0070-0016-0000
- Page Start:
- 4251
- Page End:
- 4265
- Publication Date:
- 2019-05-14
- Subjects:
- β-Cyanoalanine synthase -- cyanide -- L-cysteine desulfhydrase -- persulfidation -- redox regulation -- S-cyanylation -- sulfide -- thiol group
Botany -- Periodicals
Botany, Experimental -- Periodicals
Plant physiology -- Periodicals
580 - Journal URLs:
- http://ukcatalogue.oup.com/ ↗
http://jxb.oxfordjournals.org/ ↗ - DOI:
- 10.1093/jxb/erz225 ↗
- Languages:
- English
- ISSNs:
- 0022-0957
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4981.000000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 11819.xml