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Citation: DONG Hanyang, GUO Zhenchang, TIAN Shanshan, ZHAI Guijin, ZHANG Kai. Analysis of lysine 2-hydroxyisobutyrylation proteins in Proteus mirabilis[J]. Chinese Journal of Chromatography, ;2016, 34(12): 1215-1218. doi: 10.3724/SP.J.1123.2016.08040 shu

Analysis of lysine 2-hydroxyisobutyrylation proteins in Proteus mirabilis

Tianjin Key Laboratory of Medical Epigenetics, Department of Biochemistry and Molecular Biology, Tianjin Medical University, Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin 300070, China

Received Date: 31 August 2016

Fund Project: National Basic Research Program of China (No. 2012CB910601)

Protein lysine modifications play important roles in gene regulation, transcription, metabolism and other biological processes. Lysine 2-hydroxyisobutyrylation on histones has recently been discovered as a novel protein modification, and this modification was associated with germ cell differentiation. The problem whether the novel modification may or may not exist in prokaryotes was investigated. A number of 2-hydroxyisobutyrylated proteins and sites were identified in Proteus mirabilis using affinity enrichment, high performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) and bioinformatics. The modified proteins were further characterized according to protein distribution properties, interaction networks and pathways. The results indicated that lysine 2-hydroxyisobutyrylation is widely distributed in prokaryotes, and may be significant in biological functions in prokaryotes.
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