Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique

Ruzanna Mnatsakanyan, Stavroula Markoutsa, Kim Walbrunn, Andreas Roos, Steven H. L. Verhelst and René P. Zahedi ()
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Ruzanna Mnatsakanyan: Leibniz-Institut für Analytische Wissenschaften-ISAS-e.V.
Stavroula Markoutsa: Leibniz-Institut für Analytische Wissenschaften-ISAS-e.V.
Kim Walbrunn: Leibniz-Institut für Analytische Wissenschaften-ISAS-e.V.
Andreas Roos: Leibniz-Institut für Analytische Wissenschaften-ISAS-e.V.
Steven H. L. Verhelst: Leibniz-Institut für Analytische Wissenschaften-ISAS-e.V.
René P. Zahedi: Leibniz-Institut für Analytische Wissenschaften-ISAS-e.V.

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: Abstract Cysteine modifications emerge as important players in cellular signaling and homeostasis. Here, we present a chemical proteomics strategy for quantitative analysis of reversibly modified Cysteines using bioorthogonal cleavable-linker and switch technique (Cys-BOOST). Compared to iodoTMT for total Cysteine analysis, Cys-BOOST shows a threefold higher sensitivity and considerably higher specificity and precision. Analyzing S-nitrosylation (SNO) in S-nitrosoglutathione (GSNO)-treated and non-treated HeLa extracts Cys-BOOST identifies 8,304 SNO sites on 3,632 proteins covering a wide dynamic range of the proteome. Consensus motifs of SNO sites with differential GSNO reactivity confirm the relevance of both acid-base catalysis and local hydrophobicity for NO targeting to particular Cysteines. Applying Cys-BOOST to SH-SY5Y cells, we identify 2,151 SNO sites under basal conditions and reveal significantly changed SNO levels as response to early nitrosative stress, involving neuro(axono)genesis, glutamatergic synaptic transmission, protein folding/translation, and DNA replication. Our work suggests SNO as a global regulator of protein function akin to phosphorylation and ubiquitination.

Date: 2019
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DOI: 10.1038/s41467-019-10182-4

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