Uni TU_NP_Library_treated with cys
Ontology highlight
ABSTRACT:
INSTRUMENT(S): impact II
ORGANISM(S): Not Applicable
SUBMITTER: 
Daniel Petras Chambers Hughes
PROVIDER: MSV000093503 | MassIVE | Mon Nov 27 01:25:00 GMT 2023
REPOSITORIES: MassIVE
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Project description:Yeast protein microarrays were utilized to investigate determinants of S-nitrosylation by biologically relevant low-mass S-nitrosothiols (SNOs). Large numbers of S-nitrosylated yeast proteins were identified after treatment with SNOs, among which those with active-site Cys thiols residing at N termini of alpha-helices or within catalytic loops were particularly prominent. However, S-nitrosylation varied substantially even within these families of proteins (e.g., papain-related Cys-dependent hydrolases and rhodanese/Cdc25 phosphatases), suggesting that neither secondary structure nor intrinsic nucleophilicity of Cys thiols was sufficient to explain specificity. Further analyses revealed a substantial influence of NO-donor stereochemistry and structure on efficiency of S-nitrosylation as well as an unanticipated and important role for allosteric effectors. Thus, high-throughput screening and unbiased proteome coverage reveal multifactorial determinants of S-nitrosylation (which may be overlooked in alternative proteomic analyses), and support the idea that target specificity can be achieved through rational design of S-nitrosothiols Invitrogen yeast Protoarrays for kinase substrate identification (KSI) were treated with S-nitrosothiols and assayed for protein S-nitrosylation by using a modified biotin switch protocol. Slides were scanned and with a Genepix 4000b scanner (Molecular Devices) using Genepix Pro and analyzed by using Prospector Analyzer (Invitrogen). Results were validated using yeast cell lysates and recombinant, purified yeast proteins.
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Project description:Yeast protein microarrays were utilized to investigate determinants of S-nitrosylation by biologically relevant low-mass S-nitrosothiols (SNOs). Large numbers of S-nitrosylated yeast proteins were identified after treatment with SNOs, among which those with active-site Cys thiols residing at N termini of alpha-helices or within catalytic loops were particularly prominent. However, S-nitrosylation varied substantially even within these families of proteins (e.g., papain-related Cys-dependent hydrolases and rhodanese/Cdc25 phosphatases), suggesting that neither secondary structure nor intrinsic nucleophilicity of Cys thiols was sufficient to explain specificity. Further analyses revealed a substantial influence of NO-donor stereochemistry and structure on efficiency of S-nitrosylation as well as an unanticipated and important role for allosteric effectors. Thus, high-throughput screening and unbiased proteome coverage reveal multifactorial determinants of S-nitrosylation (which may be overlooked in alternative proteomic analyses), and support the idea that target specificity can be achieved through rational design of S-nitrosothiols
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Project description:Cysteine (Cys) reversible post-translational modifications (PTMs) are emerging as important players in cellular signaling and redox homeostasis. Here we present Cys-BOOST a novel strategy for LC-MS/MS based quantitative analysis of reversibly modified Cys using switch technique, enrichment via bio-orthogonal cleavable linker and quantification using tandem mas tag (TMT) reagents. We performed direct comparison of Cys-BOOST (n=3) with iodo-TMT (n=3) by analyzing the total CysCys from HeLa cell extracts. As a result higher sensitivity (25,019 vs 9,966 Cys peptides), specificity (98 vs 74 %) and technical reproducibility were obtained by Cys-BOOST. In addition, the application of Cys-BOOST for the analysis of Cys nitrosylation (SNO) in S-nitrosoglutathione (GSNO) treated and non-treated HeLa cell extracts lead to the identification of unprecedented number of SNO proteins (3,537), SNO peptides (9,314) and unique SNO sites (8,304). Based on the quantitative data we describe SNO consensus motifs for endogenous SNO and SNO sites with differential reactivity to GSNO. Collectively, our findings suggest Cys-BOOST as a concurrent method of choice for Cys PTM analysis.
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