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Title

Signaling by hydrogen sulfide and cyanide through post-translational modification

AuthorsGotor, Cecilia CSIC ORCID ; Aroca, Ángeles CSIC ORCID; Laureano-Marín, Ana M. CSIC ORCID; Arenas-Alfonseca, Lucía CSIC ORCID; Jurado-Flores, Ana; Moreno, Inmaculada CSIC ORCID; Romero, Luis C. CSIC ORCID CVN
Keywordsb-cyanoalanine synthase
Cyanide
L-cysteine desulfhydrase
Persulfidation
Redox regulation
S-cyanylation
Sulfide
Thiol group
Issue Date2019
PublisherOxford University Press
CitationJournal of Experimental Botany 70: 4251- 4265 (2019)
AbstractTwo 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.
URIhttp://hdl.handle.net/10261/189691
DOIhttp://dx.doi.org/10.1093/jxb/erz225
Identifiersdoi: 10.1093/jxb/erz225
issn: 0022-0957
Appears in Collections:(IBVF) Artículos
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