Volume 20, No 2, Feb 2010
ISSN: 1001-0602
EISSN: 1748-7838 2018
impact factor 17.848*
(Clarivate Analytics, 2019)
Volume 20 Issue 2, February 2010: 197-210
ORIGINAL ARTICLES
High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans
Xing-Jun Cao1,2, Jie Dai1, Hao Xu1, Song Nie1, Xiao Chang1, Bao-Yu Hu3, Quan-Hu Sheng1, Lian-Shui Wang1, Zhi-Bin Ning1, Yi-Xue Li1, Xiao-Kui Guo3, Guo-Ping Zhao4 and Rong Zeng1
1Key Laboratory of Systems Biology, Institute of Biochemistry and Cell Biology, Shanghai Institute for Biological Sciences, Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China
2Graduate University of the Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China
3Department of Medical Microbiology and Parasitology, Institutes of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China
4State Key Laboratory for Disease and Health Genomics, Chinese National Human Genome Center at Shanghai, Zhangjiang High Tech Park, Shanghai 201203, China
Correspondence: Rong Zeng, Guo-Ping Zhao,(zr@sibs.ac.cn; gpzhao@sibs.ac.cn )
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.
Cell Research (2010) 20:197-210. doi: 10.1038/cr.2009.127; published online 17 November 2009
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