Global profiling of lysine 2-hydroxyisobutyrylome in Toxoplasma gondii using affinity purification mass spectrometry.
Global profiling of lysine 2-hydroxyisobutyrylome in Toxoplasma gondii using affinity purification mass spectrometry.
复制标题
使用亲和纯化质谱法对弓形虫中的赖氨酸 2-羟基异丁酰组进行整体分析。
DOI:
10.1007/s00436-020-06923-w
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发表时间:
2020
影响因子:
2
通讯作者:
Li Facai
中科院分区:
文献类型:
--
作者:
Nie Lanbi;Liang Qinli;Elsheikha Hany M.;Du Rui;Zhu Xingquan;Li Facai
Lysine 2-hydroxyisobutyrylation (Khib) 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 Khibplays roles in the activity of gene transcription and Khib-containing proteins are closely related to the cellular metabolism. In this study, a global Khib-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 Khibmodification sites across 400 Khib-containing proteins were identified in tachyzoites ofToxoplasma gondiiRH strain. Bioinformatics and functional enrichment analysis showed that Khib-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 Khib-modified, suggesting the involvement of Khibin key biological process duringT. gondiiinfection. We also found that histone proteins, key enzymes related to cellular metabolism, and several glideosome components had Khibsites. These results expanded our understanding of the roles of KhibinT. gondiiand should promote further investigations of how Khibregulates gene expression and key biological functions inT. gondii.