Dataset Information

First Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii

ABSTRACT: Lysine malonylation (Kmal) is a new posttranslational modification (PTM), which has been reported in several prokaryotic and eukaryotic species. Although Kmal can regulate many and diverse biological processes in various organisms, knowledge about this important PTM in the apicomplexan parasite Toxoplasma gondii is limited. In this study, we performed the first global profiling of malonylated proteins in T. gondii tachyzoites using affinity enrichment and LC-MS/MS analysis. Three experiments performed in tandem revealed 331, 367, 373 Kmal sites on 227, 252, 241 malonylated proteins, respectively. Computational analysis showed the identified malonylated proteins to be localized in various subcellular compartments and involved in many cellular functions, particularly mitochondrial function and oxidation of fatty acids. Additionally, two conserved Kmal motifs with a strong bias for cysteine were detected. Taken together, these findings provide the first report of Kmal profile in T. gondii and should be an important resource for studying the physiological roles of Kmal in this parasite.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Toxoplasma Gondii

SUBMITTER: Lan-Be Nie

LAB HEAD: Xing-Quan Zhu

PROVIDER: PXD015809 | Pride | 2020-05-27

REPOSITORIES: Pride

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Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii.

Nie Lan-Bi LB Liang Qin-Li QL Du Rui R Elsheikha Hany M HM Han Nai-Jian NJ Li Fa-Cai FC Zhu Xing-Quan XQ

Frontiers in microbiology 20200428

Lysine malonylation (Kmal) is a new post-translational modification (PTM), which has been reported in several prokaryotic and eukaryotic species. Although Kmal can regulate many and diverse biological processes in various organisms, knowledge about this important PTM in the apicomplexan parasite Toxoplasma gondii is limited. In this study, we performed the first global profiling of malonylated proteins in T. gondii tachyzoites using affinity enrichment and Liquid chromatography-tan ...[more]

PMID: 32411114

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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.

			Action	DRS
	7464PIMa.zip	Other
	7464PIMa_1_exp1.raw	Raw
	7464PIMa_1_exp2.raw	Raw
	7464PIMa_1_exp3.raw	Raw
	7464PIMa_2_exp1.raw	Raw

Dataset Information

First Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii

Dataset's files

Publications

Global Proteomic Analysis of Lysine Malonylation in <i>Toxoplasma gondii</i>.

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