| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1178220 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2016 | 9 Pages |
•Established a dimethyl-SRM method for Salmonella protein analysis•Analyzed activation dynamics of Salmonella PhoP/PhoQ network•Discovered distinct patterns in PhoP/PhoQ activation•Found new protein groups and pathways regulated by PhoP/PhoQ
SRM (selected reaction monitoring), a tandem mass spectrometry-based method characterized by high repeatability and accuracy, is an effective tool for the quantification of predetermined proteins. In this study, we built a time-scheduled dimethyl-SRM method that can provide the precise relative quantification of 92 proteins in one run. By applying this method to the Salmonella PhoP/PhoQ two-component system, we found that the expression of selected PhoP/PhoQ-activated proteins in response to Mg2 + concentrations could be divided into two distinct patterns. For the time-course SRM experiment, we found that the dynamics of the selected PhoP/PhoQ-activated proteins could be divided into three distinct patterns, providing a new clue regarding PhoP/PhoQ activation and regulation. Moreover, the results for iron homeostasis proteins in response to Mg2 + concentrations revealed that the PhoP/PhoQ two-component system may serve as a repressor for iron uptake proteins. And ribosomal protein levels clearly showed a response to different Mg2 + concentrations and to time.
