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A substrate trapping approach identifies proteins regulated by reversible S-nitrosylation

ABSTRACT: In this study we adapted the Trx trapping strategy for global profiling of cellular nitrosylation/denitrosylation processes. Using this approach, we report the identification of hundreds of potential new nitrosylated targets in monoctyes and macrophages followed by validation using biochemical and functional assays.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): B Cell

SUBMITTER: Tamar Ziv

LAB HEAD: Moran Benhar

PROVIDER: PXD001001 | Pride | 2014-07-02

REPOSITORIES: Pride

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A substrate trapping approach identifies proteins regulated by reversible S-nitrosylation.

Ben-Lulu Shani S Ziv Tamar T Admon Arie A Weisman-Shomer Pnina P Benhar Moran M

Molecular & cellular proteomics : MCP 20140627 10

Protein S-nitrosylation, the nitric oxide-mediated posttranslational modification of cysteine residues, has emerged as an important regulatory mechanism in diverse cellular processes. Yet, knowledge about the S-nitrosoproteome in different cell types and cellular contexts is still limited and many questions remain regarding the precise roles of protein S-nitrosylation and denitrosylation. Here we present a novel strategy to identify reversibly nitrosylated proteins. Our approach is based on nitr ...[more]

PMID: 24973421

Similar Datasets

Project description:Toxoplasma gondii transmitted via various route and rapidly duplicated during the acute infection, which caused the important zoonosis regarding to medicine and veterinary, toxoplasmosis. T. gondii possessed innate capability of producing nitric oxide (NO) and nitric oxide derivatives and S-nitrosylation not only participated in their signaling transduction, but also was a regulatory mechanism of protein post-translation. To date, S-nitrosylation proteome of T .gondii remains a mystery. In present study, we reported the first S-nitrosylated proteomic profile in T. gondii using mass spectrometry in combination with resin-assisted enrichment. 637 proteins were found to be S-nitrosylated and more than half of these S-nitrosylated proteins were localized in nucleus or cy-toplasm. Motif analysis identified seven motifs including five motifs containing lysine and two motif harboring isoleucine. GO enrichment revealed that S-nitrosylated proteins were mainly lo-cated in the mitochondrial inner membrane and organelle inner membrane in the cell. Those S-nitrosylated proteins were related with diverse biological and metabolic processes including or-ganic acid binding, carboxylic acid binding ribose and phosphate biosynthetic process. Glycoly-sis/gluconeogenesis and aminoacyl-tRNA biosynthesis were two remarkable pathways in which T. gondii S-nitrosylated proteins engaged. Twenty seven ribosomal proteins and eleven microneme proteins out of 22 secretory proteins were identified as S-nitrosylated proteins, which suggested that proteins in ribosome and microneme were S-nitrosylated with high proportion. PPI analysis identified three subnetworks with high relevancy ribosome, RNA transport and chaperonin com-plex component. These results implied that S-nitrosylated proteins in T. gondii were associated with protein translation in ribosome, gene transcription, invasion and proliferation of T. gondii. Our research firstly identified the S-nitrosylated proteomic profile of T. gondii and will provide a valuable resource for deep-going investigation of the functions of S-nitrosylation in T. gondii.

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