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Signaling by hydrogen sulfide and cyanide through posttranslational modification.

Abstract

A new concept has arisen regarding two cysteine metabolism-related molecules, hydrogen sulfide and hydrogen cyanide, which are considered toxic but have now been established as signaling molecules. Hydrogen sulfide is produced in chloroplasts through the sulfite reductase activity 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 posttranslational modification, called persulfidation, could play a protective function for thiols against oxidative damage. Hydrogen cyanide is produced during the biosynthesis of ethylene and camalexin in noncyanogenic 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 posttranslational 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, thus altering protein functions.

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  • Authors+Show Affiliations

    ,

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

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    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.

    Source

    Pub Type(s)

    Journal Article

    Language

    eng

    PubMed ID

    31087094

    Citation

    Gotor, Cecilia, et al. "Signaling By Hydrogen Sulfide and Cyanide Through Posttranslational Modification." Journal of Experimental Botany, 2019.
    Gotor C, García I, Aroca Á, et al. Signaling by hydrogen sulfide and cyanide through posttranslational modification. J Exp Bot. 2019.
    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 posttranslational modification. Journal of Experimental Botany, doi:10.1093/jxb/erz225.
    Gotor C, et al. Signaling By Hydrogen Sulfide and Cyanide Through Posttranslational Modification. J Exp Bot. 2019 May 14; PubMed PMID: 31087094.
    * Article titles in AMA citation format should be in sentence-case
    TY - JOUR T1 - Signaling by hydrogen sulfide and cyanide through posttranslational 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, Y1 - 2019/05/14/ PY - 2019/01/09/received 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 JF - Journal of experimental botany JO - J. Exp. Bot. N2 - A new concept has arisen regarding two cysteine metabolism-related molecules, hydrogen sulfide and hydrogen cyanide, which are considered toxic but have now been established as signaling molecules. Hydrogen sulfide is produced in chloroplasts through the sulfite reductase activity 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 posttranslational modification, called persulfidation, could play a protective function for thiols against oxidative damage. Hydrogen cyanide is produced during the biosynthesis of ethylene and camalexin in noncyanogenic 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 posttranslational 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, thus 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 -