Proteomic analysis of lysine succinylation of the human pathogen Histoplasma capsulatum.
Proteomic analysis of lysine succinylation of the human pathogen Histoplasma capsulatum.
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DOI：
10.1016/j.jprot.2016.12.020
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发表时间：
2017-02
影响因子：
3.3
通讯作者：
Longxiang Xie;Juan Li;Wanyan Deng;Zhaoxiao Yu;W. Fang;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;Juan Li;Wanyan Deng;Zhaoxiao Yu;W. Fang;Min Chen;W. Liao;Jianping Xie;W. Pan
荚膜组织浆体是组织浆体病（也称为达令氏病）的病原体，可影响免疫正常和免疫功能低下的宿主。赖氨酸琥珀酰化（Ksuc）是真核生物和原核生物中常见的翻译后蛋白修饰。近年来，琥珀酰化及其调控酶在细菌、哺乳动物和真菌代谢途径中的作用得到了广泛的关注。在这里，我们报告了赖氨酸琥珀酰化的第一个全球分析，在202个蛋白质中有463个修饰位点。利用抗琥珀酰赖氨酸抗体与质谱法偶联免疫亲和富集，鉴定出荚膜nam1。生物信息学结果包括氧化石墨烯功能和富集分析表明，这些琥珀化蛋白主要参与中枢代谢和蛋白质合成，与之前的报道一致。组蛋白上的13个赖氨酸琥珀酰化位点，包括H2A， H2B， H3和H4。荚膜首次报道。这些数据为进一步表征h中赖氨酸琥珀酰化的功能提供了良好的资源。capsulatum。生物significanceH。荚膜菌是肺部组织胞浆菌病的病原体。h的能力。荚膜酵母菌作为细胞内病原菌感染巨噬细胞并在巨噬细胞内增殖，可能与多种毒力因素和代谢调节有关。赖氨酸琥珀酰化最近被证明在白色念珠菌的代谢调节中起关键作用。本研究首次对荚膜琥珀酰化蛋白进行了表征，生物信息学结果表明该修饰也可能与h的中枢代谢有关。capsulatum。组蛋白上新的琥珀酰化位点被报道。这是解决h函数的重要资源。capsulatumlysine succinylation。
Histoplasma capsulatum, the causative agent of histoplasmosis (also called “Darling's disease”), can affect both immunocompetent and immunocompromised hosts. Post-translational protein modification by lysine succinylation (Ksuc) is a frequent occurrence in eukaryote and prokaryote. Recently, the roles of succinylation and its regulatory enzymes in regulating metabolic pathway in bacteria, mammalian and fungus were highlighted. Here, we report the first global profiling of lysine succinylation, with 463 modification sites in 202 proteins fromH. capsulatumNAM1 identified, coupling immune-affinity enrichment using an anti-succinyllysine antibody with mass spectrometry. The bioinformatics results including GO functional and enrichment analysis showed that these succinylated proteins are mainly involved in central metabolism and protein synthesis, consistent with previous reports. 13 lysine succinylation sites on histones including H2A, H2B, H3 and H4 inH. capsulatumwere firstly reported. The data is a good resource for further functional characterization of lysine succinylation inH. capsulatum.Biological significanceH. capsulatumis the causative agent of lung disease histoplasmosis. The ability ofH. capsulatumyeasts to infect and proliferate within macrophages as an intracellular pathogen can be contributed to several virulence factors and metabolic regulation. Lysine succinylation was recently shown to play a critical role in the metabolism regulation ofCandida albicans.H. capsulatumsuccinylated proteins were firstly characterized in this work, and bioinformatics results showed that this modification may also be relevant with central metabolism inH. capsulatum. New succinylation sites on histones were reported. This represents an important resource to address the function ofH. capsulatumlysine succinylation.