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Signaling by hydrogen sulfide and cyanide through post-translational modification.
J Exp Bot 2019; 70(16):4251-4265JE

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.

Authors+Show Affiliations

Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, Avenida Américo Vespucio, Seville, Spain.Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, Avenida Américo Vespucio, Seville, Spain.Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, Avenida Américo Vespucio, Seville, Spain.Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, Avenida Américo Vespucio, Seville, Spain.Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, Avenida Américo Vespucio, Seville, Spain.Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, Avenida Américo Vespucio, Seville, Spain.Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, Avenida Américo Vespucio, Seville, Spain.Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, Avenida Américo Vespucio, Seville, Spain.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31087094

Citation

Gotor, Cecilia, et al. "Signaling By Hydrogen Sulfide and Cyanide Through Post-translational Modification." Journal of Experimental Botany, vol. 70, no. 16, 2019, pp. 4251-4265.
Gotor C, García I, Aroca Á, et al. Signaling by hydrogen sulfide and cyanide through post-translational modification. J Exp Bot. 2019;70(16):4251-4265.
Gotor, C., García, I., Aroca, Á., Laureano-Marín, A. M., Arenas-Alfonseca, L., Jurado-Flores, A., ... Romero, L. C. (2019). Signaling by hydrogen sulfide and cyanide through post-translational modification. Journal of Experimental Botany, 70(16), pp. 4251-4265. doi:10.1093/jxb/erz225.
Gotor C, et al. Signaling By Hydrogen Sulfide and Cyanide Through Post-translational Modification. J Exp Bot. 2019 Aug 19;70(16):4251-4265. PubMed PMID: 31087094.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Signaling by hydrogen sulfide and cyanide through post-translational modification. AU - Gotor,Cecilia, AU - García,Irene, AU - Aroca,Ángeles, AU - Laureano-Marín,Ana M, AU - Arenas-Alfonseca,Lucía, AU - Jurado-Flores,Ana, AU - Moreno,Inmaculada, AU - Romero,Luis C, PY - 2019/01/09/received PY - 2019/05/03/accepted PY - 2019/5/16/pubmed PY - 2019/5/16/medline PY - 2019/5/16/entrez KW - S-cyanylation KW - L-cysteine desulfhydrase KW - cyanide KW - persulfidation KW - redox regulation KW - sulfide KW - thiol group KW - β-Cyanoalanine synthase SP - 4251 EP - 4265 JF - Journal of experimental botany JO - J. Exp. Bot. VL - 70 IS - 16 N2 - 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. SN - 1460-2431 UR - https://www.unboundmedicine.com/medline/citation/31087094/Signaling_by_hydrogen_sulfide_and_cyanide_through_posttranslational_modification L2 - https://academic.oup.com/jxb/article-lookup/doi/10.1093/jxb/erz225 DB - PRIME DP - Unbound Medicine ER -