High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans
High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans
复制标题
高覆盖率蛋白质组分析首次揭示了致病性螺旋体问号钩端螺旋体中蛋白质修饰系统
DOI：
10.1038/cr.2009.127
复制
发表时间：
2010-02-01
期刊：
影响因子：
44.1
通讯作者：
Zeng, Rong
中科院分区：
文献类型：
--
作者：
Cao, Xing-Jun;Dai, Jie;Zeng, Rong
钩端螺旋体病是一种广泛流行的人畜共患病，由钩端螺旋体属致病螺旋体引起，可感染人类和多种动物。通过结合计算预测和高精度串联质谱学，我们修订了问号钩端螺旋体血清型Lai的基因组注释，为新基因和新的基因边界提供了大量的肽证据。随后，我们提出了对蛋白质表达和多重翻译后修饰(PTM)的高覆盖率蛋白质组分析。通过检测2540个蛋白，大约64.3%的预测问号钩端螺旋体蛋白被编目。与此同时，同时建立了多个PTMS的图谱，总共包含32个磷酸化蛋白质、46个乙酰化蛋白质和155个甲基化蛋白质。LAI血型中的PTM系统表现出独特的特征。问号钩端螺旋体的蛋白质修饰在磷酸化和精氨酸甲基化两个方面都显示出独特的真核样特征。这一系统的分析不仅提供了原核生物高覆盖率蛋白表达和多重修饰的全面信息，而且表明进化上原始的问号钩端螺旋体在蛋白质修饰系统上与真核生物有显著的相似性。
Leptospirosis is a widespread zoonotic disease caused by pathogenic spirochetes of the genus Leptospira that infects humans and a wide range of animals. By combining computational prediction and high-accuracy tandem mass spectra, we revised the genome annotation of Leptospira interrogans serovar Lai, a free-living pathogenic spirochete responsible for leptospirosis, providing substantial peptide evidence for novel genes and new gene boundaries. Subsequently, we presented a high-coverage proteome analysis of protein expression and multiple posttranslational modifications (PTMs). Approximately 64.3% of the predicted L. interrogans proteins were cataloged by detecting 2 540 proteins. Meanwhile, a profile of multiple PTMs was concurrently established, containing in total 32 phosphorylated, 46 acetylated and 155 methylated proteins. The PTM systems in the serovar Lai show unique features. Unique eukaryotic-like features of L. interrogans protein modifications were demonstrated in both phosphorylation and arginine methylation. This systematic analysis provides not only comprehensive information of high-coverage protein expression and multiple modifications in prokaryotes but also a view suggesting that the evolutionarily primitive L. interrogans shares significant similarities in protein modification systems with eukaryotes.