Phosphoproteomic investigation of Clostridium acetobutylicum.
- Author:
Xue BAI
1
;
Jingjing ZHAO
;
Qian WANG
;
Wei TONG
;
Jiyuan ZHANG
;
Jin ZI
;
Zhen CHEN
;
Siqi LIU
;
Quanhui WANG
Author Information
1. Department of Proteomics, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing 101300, China.
- Publication Type:Journal Article
- MeSH:
Bacterial Proteins;
metabolism;
Clostridium acetobutylicum;
genetics;
metabolism;
Electrophoresis, Gel, Two-Dimensional;
Mass Spectrometry;
Phosphorylation;
Proteome;
analysis;
Proteomics;
methods
- From:
Chinese Journal of Biotechnology
2010;26(10):1357-1362
- CountryChina
- Language:Chinese
-
Abstract:
Protein phosphorylation in bacteria is important for signaling and metabolic activity. Clostridium acetobutyicum can synthesize high yield of organic solvent under acidic condition. How solventogenesis is regulated at molecular level in this bacterium, is not clearly elucidated yet. We used two dimensional electrophoresis (2-DE) and mass spectrometry to have a differential analysis of the bacterial proteins from Clostridium acetobutylicum at acedogenic and solventogenic stage. We focused on these iso-spots with similar molecular mass and different pI values. Totally, eight string spots were identified, which displayed significant changes of pI values as well as spot volumes in response to solventogenic development. The data acquired from mass spectrometry demonstrated that all of the iso-spots contained the phosphrylated peptides. Bioinformatic analysis revealed that these proteins partake in the pathways of solvent synthesis.
