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Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii

Nie, Lan-Bi; Liang, Qin-Li; Du, Rui; Elsheikha, Hany M.; Han, Nai-Jian; Li, Fa-Cai; Zhu, Xing-Quan

Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii Thumbnail


Authors

Lan-Bi Nie

Qin-Li Liang

Rui Du

Nai-Jian Han

Fa-Cai Li

Xing-Quan Zhu



Abstract

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-tandem mass spectrometry (LC-MS/MS) analysis. Three experiments performed in tandem revealed 294, 345, 352 Kmal sites on 203, 236, 230 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. Additionally, one conserved Kmal motif with a strong bias for cysteine was 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.

Journal Article Type Article
Acceptance Date Mar 31, 2020
Online Publication Date Apr 28, 2020
Publication Date Apr 28, 2020
Deposit Date Apr 29, 2020
Publicly Available Date Apr 29, 2020
Journal Frontiers in Microbiology
Electronic ISSN 1664-302X
Publisher Frontiers Media
Peer Reviewed Peer Reviewed
Volume 11
Article Number 776
DOI https://doi.org/10.3389/fmicb.2020.00776
Keywords Microbiology (medical); Microbiology
Public URL https://nottingham-repository.worktribe.com/output/4359377
Publisher URL https://www.frontiersin.org/articles/10.3389/fmicb.2020.00776/full

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