Original Research ARTICLE
Genome Wide Phosphoproteome Analysis of Zymomonas Mobilis under Anaerobic, Aerobic, and N2-Fixing Conditions
- 1University of Wisconsin-Madison, United States
- 2Great Lakes Bioenergy Research Center (DOE ), United States
Protein phosphorylation is a post-translational modification with widespread regulatory roles in both eukaryotes and prokaryotes. Using mass spectrometry, we performed a genome wide investigation of protein phosphorylation in the non-model organism and biofuel producer Zymomonas mobilis under anaerobic, aerobic, and N2-fixing conditions. Our phosphoproteome analysis revealed 125 unique phosphorylated proteins, belonging to major pathways such as glycolysis, TCA cycle, electron transport, nitrogen metabolism, and protein synthesis. Quantitative analysis revealed significant and widespread changes in protein phosphorylation across growth conditions. For example, we observed increased phosphorylation of nearly all glycolytic enzymes and a large fraction of ribosomal proteins during aerobic and N2-fixing conditions. We also observed substantial changes in the phosphorylation status of enzymes and regulatory proteins involved in nitrogen fixation and ammonia assimilation during N2-fixing conditions, including nitrogenase, the Rnf electron transport complex, the transcription factor NifA, GS-GOGAT cycle enzymes, and the PII regulatory protein. This suggested that protein phosphorylation may play an important role at regulating all aspects of nitrogen metabolism in Z. mobilis. This study provides new knowledge regarding the specific pathways and cellular processes that may potentially be regulated by protein phosphorylation in this important industrial organism and provides a useful road map for future experiments that investigate the physiological role of specific phosphorylation events in Z. mobilis.
Keywords: Zymomonas mobilis, Protein phosphorylation, Nitrogen Fixation, phosphoproteome analysis, Mass spectrometry - LC-MS/MS, Entner Doudoroff pathway
Received: 04 Jun 2019;
Accepted: 13 Aug 2019.
Copyright: © 2019 Tatli, Hebert, Coon and Amador-Noguez. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: Dr. Daniel Amador-Noguez, University of Wisconsin-Madison, Madison, 53715-1149, Alabama, United States, email@example.com