Global profiling of lysine 2-hydroxyisobutyrylome inToxoplasma gondiiusing affinity purification mass spectrometry
文献类型: 外文期刊
第一作者: Nie, Lan-Bi
作者: Nie, Lan-Bi;Du, Rui;Nie, Lan-Bi;Liang, Qin-Li;Zhu, Xing-Quan;Li, Fa-Cai;Elsheikha, Hany M.;Zhu, Xing-Quan;Li, Fa-Cai
作者机构:
关键词: Toxoplasma gondii; Post-translational modification (PTM); Lysine 2-hydroxyisobutyrylation; Tachyzoite
期刊名称:PARASITOLOGY RESEARCH ( 影响因子:2.289; 五年影响因子:2.403 )
ISSN: 0932-0113
年卷期:
页码:
收录情况: SCI
摘要: Lysine 2-hydroxyisobutyrylation (K-hib) is a recently discovered and evolutionarily conserved form of protein post-translational modification (PTM) found in mammalian and yeast cells. Previous studies have shown that K(hib)plays roles in the activity of gene transcription and K-hib-containing proteins are closely related to the cellular metabolism. In this study, a global K-hib-containing analysis using the latest databases (ToxoDB 46, 8322 sequences, downloaded on April 16, 2020) and sensitive immune-affinity enrichment coupled with liquid chromatography-tandem mass spectrometry was performed. A total of 1078 K(hib)modification sites across 400 K-hib-containing proteins were identified in tachyzoites ofToxoplasma gondiiRH strain. Bioinformatics and functional enrichment analysis showed that K-hib-modified proteins were associated with various biological processes, such as ribosome, glycolysis/gluconeogenesis, and central carbon metabolism. Interestingly, many proteins of the secretory organelles (e.g., microneme, rhoptry, and dense granule) that play roles in the infection cycle ofT. gondiiwere found to be K-hib-modified, suggesting the involvement of K(hib)in key biological process duringT. gondiiinfection. We also found that histone proteins, key enzymes related to cellular metabolism, and several glideosome components had K(hib)sites. These results expanded our understanding of the roles of K(hib)inT. gondiiand should promote further investigations of how K(hib)regulates gene expression and key biological functions inT. gondii.
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