Global profiling of lysine acetylation in human histoplasmosis pathogen Histoplasma capsulatum.
Global profiling of lysine acetylation in human histoplasmosis pathogen Histoplasma capsulatum.
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DOI：
10.1016/j.biocel.2016.01.008
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发表时间：
2016-04
期刊：
影响因子：
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通讯作者：
Longxiang Xie;W. Fang;Wanyan Deng;Zhaoxiao Yu;Juan Li;Min Chen;W. Liao;Jianping Xie;W. Pan
中科院分区：
文献类型：
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作者：
Longxiang Xie;W. Fang;Wanyan Deng;Zhaoxiao Yu;Juan Li;Min Chen;W. Liao;Jianping Xie;W. Pan
Histoplasma capsulatumis the causative agent of human histoplasmosis, which can cause respiratory and systemic mycosis in immune-compromised individuals. Lysine acetylation, a protein posttranslational protein modification, is widespread in both eukaryotes and prokaryotes. Although increasing evidence suggests that lysine acetylation may play critical roles in fungus physiology, very little is known about its extent and function inH. capsulatum. To comprehensively profile protein lysine acetylation inH. capsulatum, we performed a global acetylome analysis through peptide prefractionation, antibody enrichment, and LC−MS/MS analysis, identifying 775 acetylation sites on 456 acetylated proteins; and functionally analysis showing their involvement in different biological processes. We defined six types of acetylation site motifs, and the results imply that lysine residue of polypeptide with tyrosine at the −1 and +1 positions, histidine at the +1 position, and phenylalanine (F) at the +1 and +2 position is a preferred substrate of lysine acetyltransferase. Moreover, some virulence factors candidates including calmodulin and DnaK are acetylated. In conclusion, our data set may serve as an important resource for the elucidation of associations between functional protein lysine acetylation and virulence inH. capsulatum.
