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Persulfidation proteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes in Arabidopsis

Opened Access Persulfidation proteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes in Arabidopsis

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Autor: Aroca Aguilar, Ángeles
Benito, Juan M.
Gotor Martínez, Cecilia
Romero González, Luis Carlos
Departamento: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Fecha: 2017
Publicado en: Journal of Experimental Botany, 68 (17), 4915-4927.
Tipo de documento: Artículo
Resumen: 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...
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Cita: Aroca, Á., Benito, J.M., Gotor Martínez, C. y Romero González, 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), 4915-4927.
Tamaño: 2.391Mb
Formato: PDF

URI: http://hdl.handle.net/11441/67880

DOI: doi:10.1093/jxb/erx294

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