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Systematic identification of the lysine succinylation in the protozoan parasite Toxoplasma gondii.

Authors
  • Li, Xiaolong
  • Hu, Xin
  • Wan, Yujing
  • Xie, Guizhen
  • Li, Xiangzhi
  • Chen, Di
  • Cheng, Zhongyi
  • Yi, Xingling
  • Liang, Shaohui
  • Tan, Feng
Type
Published Article
Journal
Journal of Proteome Research
Publisher
American Chemical Society
Publication Date
Dec 05, 2014
Volume
13
Issue
12
Pages
6087–6095
Identifiers
DOI: 10.1021/pr500992r
PMID: 25377623
Source
Medline
Keywords
License
Unknown

Abstract

Lysine succinylation is a new posttranslational modification identified in histone proteins of Toxoplasma gondii, an obligate intracellular parasite of the phylum Apicomplexa. However, very little is known about their scope and cellular distribution. Here, using LC-MS/MS to identify parasite peptides enriched by immunopurification with succinyl lysine antibody, we produced the first lysine succinylome in this parasite. Overall, a total of 425 lysine succinylation sites that occurred on 147 succinylated proteins were identified in extracellular Toxoplasma tachyzoites, which is a proliferative stage that results in acute toxoplasmosis. With the bioinformatics analysis, it is shown that these succinylated proteins are evolutionarily conserved and involved in a wide variety of cellular functions such as metabolism and epigenetic gene regulation and exhibit diverse subcellular localizations. Moreover, we defined five types of definitively conserved succinylation site motifs, and the results imply that lysine residue of a polypeptide with lysine on the +3 position and without lysine at the -1 to +2 position is a preferred substrate of lysine succinyltransferase. In conclusion, our findings suggest that lysine succinylation in Toxoplasma involves a diverse array of cellular functions, although the succinylation occurs at a low level.

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