Label-Free Quantitative Proteomic Analysis of Nitrogen Starvation in Arabidopsis Root Reveals New Aspects of H<sub>2</sub>S Signaling by Protein Persulfidation
Hydrogen sulfide (H<sub>2</sub>S)-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 posttranslational modification of cysteine residues...
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doaj-401659fe402440f8ae84548a37b2d7bb2021-03-25T00:07:18ZengMDPI AGAntioxidants2076-39212021-03-011050850810.3390/antiox10040508Label-Free Quantitative Proteomic Analysis of Nitrogen Starvation in Arabidopsis Root Reveals New Aspects of H<sub>2</sub>S Signaling by Protein PersulfidationAna Jurado-Flores0Luis C. Romero1Cecilia Gotor2Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, 41092 Sevilla, SpainInstituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, 41092 Sevilla, SpainInstituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, 41092 Sevilla, SpainHydrogen sulfide (H<sub>2</sub>S)-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 posttranslational modification of cysteine residues to form a persulfidated thiol motif. We developed a comparative and label-free quantitative proteomic analysis approach for the detection of endogenous persulfidated proteins in N-starved <i>Arabidopsis thaliana</i> roots by using the tag-switch method. In this work, we identified 5214 unique proteins from root tissue that were persulfidated, 1674 of which were quantitatively analyzed and found to show altered persulfidation levels in vivo under N deprivation. These proteins represented almost 13% of the entire annotated proteome in Arabidopsis. Bioinformatic analysis revealed that persulfidated proteins were involved in a wide range of biological functions, regulating important processes such as primary metabolism, plant responses to stresses, growth and development, RNA translation and protein degradation. Quantitative mass spectrometry analysis allowed us to obtain a comprehensive view of hydrogen sulfide signaling via changes in the persulfidation levels of key protein targets involved in ubiquitin-dependent protein degradation and autophagy, among others.https://www.mdpi.com/2076-3921/10/4/508Arabidopsisautophagycysteinehydrogen sulfidepersulfidationproteomic |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Ana Jurado-Flores Luis C. Romero Cecilia Gotor |
spellingShingle |
Ana Jurado-Flores Luis C. Romero Cecilia Gotor Label-Free Quantitative Proteomic Analysis of Nitrogen Starvation in Arabidopsis Root Reveals New Aspects of H<sub>2</sub>S Signaling by Protein Persulfidation Antioxidants Arabidopsis autophagy cysteine hydrogen sulfide persulfidation proteomic |
author_facet |
Ana Jurado-Flores Luis C. Romero Cecilia Gotor |
author_sort |
Ana Jurado-Flores |
title |
Label-Free Quantitative Proteomic Analysis of Nitrogen Starvation in Arabidopsis Root Reveals New Aspects of H<sub>2</sub>S Signaling by Protein Persulfidation |
title_short |
Label-Free Quantitative Proteomic Analysis of Nitrogen Starvation in Arabidopsis Root Reveals New Aspects of H<sub>2</sub>S Signaling by Protein Persulfidation |
title_full |
Label-Free Quantitative Proteomic Analysis of Nitrogen Starvation in Arabidopsis Root Reveals New Aspects of H<sub>2</sub>S Signaling by Protein Persulfidation |
title_fullStr |
Label-Free Quantitative Proteomic Analysis of Nitrogen Starvation in Arabidopsis Root Reveals New Aspects of H<sub>2</sub>S Signaling by Protein Persulfidation |
title_full_unstemmed |
Label-Free Quantitative Proteomic Analysis of Nitrogen Starvation in Arabidopsis Root Reveals New Aspects of H<sub>2</sub>S Signaling by Protein Persulfidation |
title_sort |
label-free quantitative proteomic analysis of nitrogen starvation in arabidopsis root reveals new aspects of h<sub>2</sub>s signaling by protein persulfidation |
publisher |
MDPI AG |
series |
Antioxidants |
issn |
2076-3921 |
publishDate |
2021-03-01 |
description |
Hydrogen sulfide (H<sub>2</sub>S)-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 posttranslational modification of cysteine residues to form a persulfidated thiol motif. We developed a comparative and label-free quantitative proteomic analysis approach for the detection of endogenous persulfidated proteins in N-starved <i>Arabidopsis thaliana</i> roots by using the tag-switch method. In this work, we identified 5214 unique proteins from root tissue that were persulfidated, 1674 of which were quantitatively analyzed and found to show altered persulfidation levels in vivo under N deprivation. These proteins represented almost 13% of the entire annotated proteome in Arabidopsis. Bioinformatic analysis revealed that persulfidated proteins were involved in a wide range of biological functions, regulating important processes such as primary metabolism, plant responses to stresses, growth and development, RNA translation and protein degradation. Quantitative mass spectrometry analysis allowed us to obtain a comprehensive view of hydrogen sulfide signaling via changes in the persulfidation levels of key protein targets involved in ubiquitin-dependent protein degradation and autophagy, among others. |
topic |
Arabidopsis autophagy cysteine hydrogen sulfide persulfidation proteomic |
url |
https://www.mdpi.com/2076-3921/10/4/508 |
work_keys_str_mv |
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