Dataset Information

Proteomic analysis of S-nitrosation sites in Araucaria angustifolia (Bertol.) Kuntze

ABSTRACT: In the present study, endogenous cysteine S-nitrosation site and S-nitrosated proteins were identified by iodo-TMT labeling during somatic embryogenesis in Brazilian pine, an endangered native conifer of South America.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Araucaria Angustifolia

TISSUE(S): Embryogenic Cell Line

SUBMITTER: Andre Luis Wendt dos Santos

LAB HEAD: Andre Luis Wendt dos Santos

PROVIDER: PXD033177 | Pride | 2022-08-12

REPOSITORIES: Pride

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Publications

Proteomic Analysis of S-Nitrosation Sites During Somatic Embryogenesis in Brazilian Pine, Araucaria angustifolia (Bertol.) Kuntze.

Borges Araujo Alexandre Junio AJ Cerruti Giovanni Victorio GV Zuccarelli Rafael R Rodriguez Ruiz Marta M Freschi Luciano L Singh Ratna R Moerschbacher Bruno Maria BM Floh Eny Iochevet Segal EIS Wendt Dos Santos André Luis AL

Frontiers in plant science 20220630

Cysteine S-nitrosation is a redox-based post-translational modification that mediates nitric oxide (NO) regulation of various aspects of plant growth, development and stress responses. Despite its importance, studies exploring protein signaling pathways that are regulated by S-nitrosation during somatic embryogenesis have not been performed. In the present study, endogenous cysteine S-nitrosation site and S-nitrosated proteins were identified by iodo-TMT labeling duri ...[more]

PMID: 35845673

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Project description:E3 ubiquitin ligases mediate the last step of the ubiquitination pathwayin the ubiquitin-proteasome system (UPS). By targeting transcriptional regulators for their turnover, E3s play a crucial role in every aspect of plant biology. In plants, SKP1/CULLIN1/F-BOX PROTEIN (SCF)-type E3 ubiquitin ligases are essential for the perception and signaling of several key hormones including auxins and jasmonates (JAs). F-box proteins, TRANSPORT INHIBITOR RESPONSE 1 (TIR1) and CORONATINE INSENSITIVE 1 (COI1) bind directly transcriptional repressors AUX/IAAs and JAZs in an auxin- and JAs-depending manner, respectively, which permits the perception of the hormones and transcriptional activation of signaling pathways. Redox modification of proteins mainly by S-nitrosation of cysteines via nitric oxide (NO) has emerged as a valued regulatory mechanism in physiological processes requiring its rapid and versatile integration. Previously, we demonstrated that TIR1 and ASK1 (Arabidopsis thaliana SKP1) are targets of S-nitrosation, and these (NO)-dependent post-translational modifications enhance protein-protein interactions, and positively regulate SCFTIR1 complex assembly and expression of auxin response genes. In this work, we provide evidence on the modulation of SCFCOI1 complex by different S-nitrosation events. We demonstrated that S-nitrosation of ASK1 Cys118 enhanced ASK1-COI1 protein-protein interaction. Overexpression of non-nitrosable ask1 mutant protein impaired the activation of JA-responsive genes mediated by SCFCOI1 illustrating the functional relevance of this redox-mediated regulation in planta. Additionally, in silico analysis positioned COI1 as a promising S-nitrosation target. The regulation of SCF components involved in hormonal perception by S- nitrosation may represent a key strategy to determine the precise time and site-dependent activation of each hormonal signaling pathway, and highlights NO as a pivotal molecular player in these scenarios.

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Dataset Information

Proteomic analysis of S-nitrosation sites in Araucaria angustifolia (Bertol.) Kuntze

Dataset's files

Publications

Proteomic Analysis of <i>S</i>-Nitrosation Sites During Somatic Embryogenesis in Brazilian Pine, <i>Araucaria angustifolia</i> (Bertol.) Kuntze.

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