Identification of Protein Redox 'Switches' for Optimized Bioenergy Production in a Purple Nonsulfur Photosynthetic Bacterium
EMSL Project ID
48893
Abstract
Cysteine residues act as thiol-mediated molecular switches that play an important role in redox regulation. Here we propose to use thiol-reactive redox probes for in vivo labeling and identification of redox-sensitive proteins in a purple nonsulfur photosynthetic bacterium (PNSB). In PNSB, redox regulation is involved in regulation of photosynthesis, carbon fixation and nitrogen fixation - processes that can be manipulated to produce energy relevant products like hydrogen gas and hydrocarbons. However, little is known about how PNSB respond to an environmental change such as low light, to affect a change in redox signaling. By using proteomic approaches to identify thiol-containing proteins that are labeled with thiol-reactive probes we expect to uncover novel signal transducers and regulators of enzyme activity. These could constitute targets for optimization of pathways important for bioenergy production. We will use quantitative chemoproteomic and global proteomic approaches, and potentially top-down proteomic, microscopy, and flow cytometry measurements to identify proteins in PNSB that can respond to redox events generated by environmental signals.
Project Details
Project type
Large-Scale EMSL Research
Start Date
2015-10-01
End Date
2017-09-30
Status
Closed
Released Data Link
Team
Principal Investigator