title: High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans.
abstract: 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.
authors.affiliation: Key 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.
authors.forename: Xing-Jun
authors.initials: XJ
authors.lastname: Cao
authors.forename: Jie
authors.initials: J
authors.lastname: Dai
authors.forename: Hao
authors.initials: H
authors.lastname: Xu
authors.forename: Song
authors.initials: S
authors.lastname: Nie
authors.forename: Xiao
authors.initials: X
authors.lastname: Chang
authors.forename: Bao-Yu
authors.initials: BY
authors.lastname: Hu
authors.forename: Quan-Hu
authors.initials: QH
authors.lastname: Sheng
authors.forename: Lian-Shui
authors.initials: LS
authors.lastname: Wang
authors.forename: Zhi-Bin
authors.initials: ZB
authors.lastname: Ning
authors.forename: Yi-Xue
authors.initials: YX
authors.lastname: Li
authors.forename: Xiao-Kui
authors.initials: XK
authors.lastname: Guo
authors.forename: Guo-Ping
authors.initials: GP
authors.lastname: Zhao
authors.forename: Rong
authors.initials: R
authors.lastname: Zeng
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism; D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D001483:Base Sequence; D016680:Genome, Bacterial; D007921:Leptospira interrogans / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D011499:Protein Processing, Post-Translational / Q000502:physiology; D020543:Proteome / Q000032:analysis*; D040901:Proteomics / Q000379:methods; D017386:Sequence Homology, Amino Acid; D013144:Spirochaetales / Q000235:genetics / Q000378:metabolism; D053719:Tandem Mass Spectrometry
chemical_list: D001426:Bacterial Proteins; D020543:Proteome; D000123:Acetyltransferases; D011494:Protein Kinases