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Persulfidation proteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes in Arabidopsis.
J Exp Bot 2017; 68(17):4915-4927JE

Abstract

Hydrogen sulfide-mediated signaling pathways regulate many physiological and pathophysiological processes in mammalian and plant systems. The molecular mechanism by which hydrogen sulfide exerts its action involves the post-translational modification of cysteine residues to form a persulfidated thiol motif, a process called protein persulfidation. We have developed a comparative and quantitative proteomic analysis approach for the detection of endogenous persulfidated proteins in wild-type Arabidopsis and L-CYSTEINE DESULFHYDRASE 1 mutant leaves using the tag-switch method. The 2015 identified persulfidated proteins were isolated from plants grown under controlled conditions, and therefore, at least 5% of the entire Arabidopsis proteome may undergo persulfidation under baseline conditions. Bioinformatic analysis revealed that persulfidated cysteines participate in a wide range of biological functions, regulating important processes such as carbon metabolism, plant responses to abiotic and biotic stresses, plant growth and development, and RNA translation. Quantitative analysis in both genetic backgrounds reveals that protein persulfidation is mainly involved in primary metabolic pathways such as the tricarboxylic acid cycle, glycolysis, and the Calvin cycle, suggesting that this protein modification is a new regulatory component in these pathways.

Authors+Show Affiliations

Instituto de Bioquímica Vegetal y Fotosíntesis.Instituto de Investigaciones Química, Consejo Superior de Investigaciones Científicas y Universidad de Sevilla, Avenida Américo Vespucio, 49, 41092 Sevilla, Spain.Instituto de Bioquímica Vegetal y Fotosíntesis.Instituto de Bioquímica Vegetal y Fotosíntesis.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

28992305

Citation

Aroca, Angeles, et al. "Persulfidation Proteome Reveals the Regulation of Protein Function By Hydrogen Sulfide in Diverse Biological Processes in Arabidopsis." Journal of Experimental Botany, vol. 68, no. 17, 2017, pp. 4915-4927.
Aroca A, Benito JM, Gotor C, et al. Persulfidation proteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes in Arabidopsis. J Exp Bot. 2017;68(17):4915-4927.
Aroca, A., Benito, J. M., Gotor, C., & Romero, L. C. (2017). Persulfidation proteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes in Arabidopsis. Journal of Experimental Botany, 68(17), pp. 4915-4927. doi:10.1093/jxb/erx294.
Aroca A, et al. Persulfidation Proteome Reveals the Regulation of Protein Function By Hydrogen Sulfide in Diverse Biological Processes in Arabidopsis. J Exp Bot. 2017 10 13;68(17):4915-4927. PubMed PMID: 28992305.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Persulfidation proteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes in Arabidopsis. AU - Aroca,Angeles, AU - Benito,Juan M, AU - Gotor,Cecilia, AU - Romero,Luis C, PY - 2017/10/11/pubmed PY - 2018/5/15/medline PY - 2017/10/10/entrez KW - Cysteine KW - hydrogen sulfide KW - mass spectrometry KW - persulfidation KW - post-translational modification KW - proteomics SP - 4915 EP - 4927 JF - Journal of experimental botany JO - J. Exp. Bot. VL - 68 IS - 17 N2 - Hydrogen sulfide-mediated signaling pathways regulate many physiological and pathophysiological processes in mammalian and plant systems. The molecular mechanism by which hydrogen sulfide exerts its action involves the post-translational modification of cysteine residues to form a persulfidated thiol motif, a process called protein persulfidation. We have developed a comparative and quantitative proteomic analysis approach for the detection of endogenous persulfidated proteins in wild-type Arabidopsis and L-CYSTEINE DESULFHYDRASE 1 mutant leaves using the tag-switch method. The 2015 identified persulfidated proteins were isolated from plants grown under controlled conditions, and therefore, at least 5% of the entire Arabidopsis proteome may undergo persulfidation under baseline conditions. Bioinformatic analysis revealed that persulfidated cysteines participate in a wide range of biological functions, regulating important processes such as carbon metabolism, plant responses to abiotic and biotic stresses, plant growth and development, and RNA translation. Quantitative analysis in both genetic backgrounds reveals that protein persulfidation is mainly involved in primary metabolic pathways such as the tricarboxylic acid cycle, glycolysis, and the Calvin cycle, suggesting that this protein modification is a new regulatory component in these pathways. SN - 1460-2431 UR - https://www.unboundmedicine.com/medline/citation/28992305/Persulfidation_proteome_reveals_the_regulation_of_protein_function_by_hydrogen_sulfide_in_diverse_biological_processes_in_Arabidopsis_ L2 - https://academic.oup.com/jxb/article-lookup/doi/10.1093/jxb/erx294 DB - PRIME DP - Unbound Medicine ER -