• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>MicrobiologyOpen >The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites
【24h】

The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites

机译：大肠杆菌sirtuin CobB对酶促和非酶促赖氨酸乙酰化底物位点没有偏爱

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

AbstractNε-lysine acetylation is an abundant posttranslational modification of thousands of proteins involved in diverse cellular processes. In the model bacterium Escherichia coli, the ε-amino group of a lysine residue can be acetylated either catalytically by acetyl-coenzyme A (acCoA) and lysine acetyltransferases, or nonenzymatically by acetyl phosphate (acP). It is well known that catalytic acCoA-dependent Nε-lysine acetylation can be reversed by deacetylases. Here, we provide genetic, mass spectrometric, structural and immunological evidence that CobB, a deacetylase of the sirtuin family of NAD+-dependent deacetylases, can reverse acetylation regardless of acetyl donor or acetylation mechanism. We analyzed 69 lysines on 51 proteins that we had previously detected as robustly, reproducibly, and significantly more acetylated in a cobB mutant than in its wild-type parent. Functional and pathway enrichment analyses supported the hypothesis that CobB regulates protein function in diverse and often essential cellular processes, most notably translation. Combined mass spectrometry, bioinformatics, and protein structural data provided evidence that the accessibility and three-dimensional microenvironment of the target acetyllysine help determine CobB specificity. Finally, we provide evidence that CobB is the predominate deacetylase in E. coli.
机译：摘要N ε-赖氨酸乙酰化作用是对涉及多种细胞过程的数千种蛋白质的大量翻译后修饰。在大肠杆菌模型中，赖氨酸残基的ε-氨基可以通过乙酰辅酶A（acCoA）和赖氨酸乙酰转移酶催化乙酰化，也可以通过乙酰磷酸（acP）非酶催化乙酰化。众所周知，脱乙酰基酶可以逆转催化的acCoA依赖性N ε-赖氨酸乙酰化作用。在这里，我们提供了遗传，质谱，结构和免疫学方面的证据，表明CobB是NAD + 依赖性脱乙酰酶的瑟土因家族的一种脱乙酰酶，可以逆转乙酰化，而与乙酰基供体或乙酰化机制无关。我们对51种蛋白质的69个赖氨酸进行了分析，这些蛋白质先前在cobB突变体中比在其野生型亲本中被检测为具有较强的可重复性，并且乙酰化程度明显更高。功能和途径富集分析支持以下假设，即CobB在各种通常是必不可少的细胞过程（尤其是翻译）中调节蛋白质功能。结合质谱，生物信息学和蛋白质结构数据提供的证据表明，目标乙酰赖氨酸的可及性和三维微环境有助于确定CobB特异性。最后，我们提供了CobB是大肠杆菌中主要的脱乙酰基酶的证据。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号