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Proteome Wide Profiling of N-ε-Lysine Acetylation Reveals a Novel Mechanism of Regulation of the Chitinase Activity in Francisella novicida.
Journal of Proteome Research ( IF 4.4 ) Pub Date : 2020-02-14 , DOI: 10.1021/acs.jproteome.9b00512
Ekaterina Marakasova 1 , Alexandra Ii 1 , Kristina T Nelson 2 , Monique L van Hoek 1
Affiliation  

Francisella tularensis is a Gram-negative bacterium that causes the zoonotic disease tularemia. The historical development of tularemia as a biological weapon has led to it being characterized by the CDC as a category A biothreat agent. Neither posttranslational modification (PTM) of proteins, in particular lysine acetylation, in Francisella nor its subsequent regulation of the protein activity has been well studied. In this work, we analyze N-ε-lysine acetylation of the F. tularensis ssp. novicida proteome by mass spectrometry for the first time. To create a comprehensive acetylation profile, we enriched protein acetylation using two approaches: (1) the addition of glucose or acetate into the culture medium and (2) direct chemical acetylation of N-ε-lysines with acetyl phosphate. We discovered 280 acetylated proteins with 1178 acetylation sites in the F. tularensis ssp. novicida strain U112. Lysine acetylation is an important PTM that regulates multiple cellular processes in bacteria, including metabolism, transcription, translation, stress response, and protein folding. We discovered that Francisella chitinases A and B are acetylated naturally and when chemically induced by acetyl phosphate. Moreover, chemical overacetylation of chitinases results in silencing of the enzymatic activity. Our findings suggest a novel mechanism of posttranslational regulation of the chitinase activity and that acetylation may play a role in Francisella's regulation of the protein activity.

中文翻译:

N-ε-赖氨酸乙酰化的蛋白质组学广泛分析揭示了新弗朗西斯菌中几丁质酶活性调节的新机制。

图拉弗朗西斯菌(Francisella tularensis)是一种革兰氏阴性细菌,可引起人畜共患疾病图拉血病。Tularemia作为生物武器的历史发展,使其以CDC为A类生物威胁因子为特征。在弗朗西斯菌中,蛋白质的翻译后修饰(PTM),特别是赖氨酸乙酰化,以及其对蛋白质活性的后续调控都没有得到很好的研究。在这项工作中,我们分析了F. tularensis ssp的N-ε-赖氨酸乙酰化。首次通过质谱测定蛋白质组。为了创建全面的乙酰化特性,我们使用两种方法丰富了蛋白质的乙酰化作用:(1)在培养基中添加葡萄糖或乙酸盐;(2)用乙酰基磷酸直接对N-ε-赖氨酸进行化学乙酰化。我们在F. tularensis ssp中发现了280个具有1178个乙酰化位点的乙酰化蛋白。Novicida菌株U112。赖氨酸乙酰化是一种重要的PTM,它调节细菌中的多个细胞过程,包括代谢,转录,翻译,应激反应和蛋白质折叠。我们发现,弗朗西斯菌几丁质酶A和B自然地被乙酰化,并在被乙酰磷酸化学诱导时被乙酰化。此外,几丁质酶的化学过度乙酰化导致酶活性的沉默。我们的发现提示了几丁质酶活性的翻译后调控的新机制,乙酰化可能在弗朗西斯菌对蛋白质活性的调控中起作用。包括新陈代谢,转录,翻译,应激反应和蛋白质折叠。我们发现,弗朗西斯菌几丁质酶A和B自然地被乙酰化,并在被乙酰磷酸化学诱导时被乙酰化。此外,几丁质酶的化学过度乙酰化导致酶活性的沉默。我们的发现提示了几丁质酶活性的翻译后调控的新机制,乙酰化可能在弗朗西斯菌对蛋白质活性的调控中起作用。包括新陈代谢,转录,翻译,应激反应和蛋白质折叠。我们发现,弗朗西斯菌几丁质酶A和B自然地被乙酰化,并在被乙酰磷酸化学诱导时被乙酰化。此外,几丁质酶的化学过度乙酰化导致酶活性的沉默。我们的发现提示了几丁质酶活性的翻译后调控的新机制,乙酰化可能在弗朗西斯菌对蛋白质活性的调控中起作用。
更新日期:2020-02-14
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