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Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation.
Front Plant Sci 2018; 9:1369FP

Abstract

Hydrogen sulfide (H2S) has been largely referred as a toxic gas and environmental hazard, but recent years, it has emerged as an important gas-signaling molecule with effects on multiple physiological processes in both animal and plant systems. The regulatory functions of H2S in plants are involved in important processes such as the modulation of defense responses, plant growth and development, and the regulation of senescence and maturation. The main signaling pathway involving sulfide has been proven to be through protein persulfidation (alternatively called S-sulfhydration), in which the thiol group of cysteine (-SH) in proteins is modified into a persulfide group (-SSH). This modification may cause functional changes in protein activities, structures, and subcellular localizations of the target proteins. New shotgun proteomic approaches and bioinformatic analyses have revealed that persulfidated cysteines regulate important biological processes, highlighting their importance in cell signaling, since about one in 20 proteins in Arabidopsis is persulfidated. During oxidative stress, an increased persulfidation has been reported and speculated that persulfidation is the protective mechanism for protein oxidative damage. Nevertheless, cysteine residues are also oxidized to different post-translational modifications such S-nitrosylation or S-sulfenylation, which seems to be interconvertible. Thus, it must imply a tight cysteine redox regulation essential for cell survival. This review is aimed to focus on the current knowledge of protein persulfidation and addresses the regulation mechanisms that are disclosed based on the knowledge from other cysteine modifications.

Authors+Show Affiliations

Institute of Plant Biochemistry and Photosynthesis, Consejo Superior de Investigaciones Científicas, Universidad de Sevilla, Seville, Spain.Institute of Plant Biochemistry and Photosynthesis, Consejo Superior de Investigaciones Científicas, Universidad de Sevilla, Seville, Spain.Institute of Plant Biochemistry and Photosynthesis, Consejo Superior de Investigaciones Científicas, Universidad de Sevilla, Seville, Spain.

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

30283480

Citation

Aroca, Angeles, et al. "Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation." Frontiers in Plant Science, vol. 9, 2018, p. 1369.
Aroca A, Gotor C, Romero LC. Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation. Front Plant Sci. 2018;9:1369.
Aroca, A., Gotor, C., & Romero, L. C. (2018). Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation. Frontiers in Plant Science, 9, p. 1369. doi:10.3389/fpls.2018.01369.
Aroca A, Gotor C, Romero LC. Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation. Front Plant Sci. 2018;9:1369. PubMed PMID: 30283480.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation. AU - Aroca,Angeles, AU - Gotor,Cecilia, AU - Romero,Luis C, Y1 - 2018/09/19/ PY - 2018/06/03/received PY - 2018/08/29/accepted PY - 2018/10/5/entrez PY - 2018/10/5/pubmed PY - 2018/10/5/medline KW - Arabidopsis KW - cell signaling KW - cysteine KW - hydrogen sulfide KW - persulfidation KW - post-translational modification KW - proteomic SP - 1369 EP - 1369 JF - Frontiers in plant science JO - Front Plant Sci VL - 9 N2 - Hydrogen sulfide (H2S) has been largely referred as a toxic gas and environmental hazard, but recent years, it has emerged as an important gas-signaling molecule with effects on multiple physiological processes in both animal and plant systems. The regulatory functions of H2S in plants are involved in important processes such as the modulation of defense responses, plant growth and development, and the regulation of senescence and maturation. The main signaling pathway involving sulfide has been proven to be through protein persulfidation (alternatively called S-sulfhydration), in which the thiol group of cysteine (-SH) in proteins is modified into a persulfide group (-SSH). This modification may cause functional changes in protein activities, structures, and subcellular localizations of the target proteins. New shotgun proteomic approaches and bioinformatic analyses have revealed that persulfidated cysteines regulate important biological processes, highlighting their importance in cell signaling, since about one in 20 proteins in Arabidopsis is persulfidated. During oxidative stress, an increased persulfidation has been reported and speculated that persulfidation is the protective mechanism for protein oxidative damage. Nevertheless, cysteine residues are also oxidized to different post-translational modifications such S-nitrosylation or S-sulfenylation, which seems to be interconvertible. Thus, it must imply a tight cysteine redox regulation essential for cell survival. This review is aimed to focus on the current knowledge of protein persulfidation and addresses the regulation mechanisms that are disclosed based on the knowledge from other cysteine modifications. SN - 1664-462X UR - https://www.unboundmedicine.com/medline/citation/30283480/Hydrogen_Sulfide_Signaling_in_Plants:_Emerging_Roles_of_Protein_Persulfidation_ L2 - https://doi.org/10.3389/fpls.2018.01369 DB - PRIME DP - Unbound Medicine ER -