The FNR transcription factor is the protein that controls the switch between aerobic and anaerobic respiration in facultative anaerobes. It is only active as a dimer and contains a [4Fe-4S] cluster, which is destabilized in the presence of oxygen. Escherichia coli FNR has yet to be isolated and crystallized, but mutagenesis experiments can be done to better understand the fine interactions and mechanics that allow FNR to control gene expression. Due to similarities in function and amino acid sequence, Aliivibrio fischeri FNR is used as a reference structure. This work focuses on using site directed mutagenesis to test the role of position 142 in dimerization, because glutamine 142 is in the dimerization helix and the A. fischeri structure suggests it may interact with the amino acids that ligate the cluster. A variety of amino acid substitutions have been made at this position and the effect on the activity of the protein will be evaluated.

Investigating the effect of position 142 on the dimerization of the fumarate nitrate reductase transcription factor in E. coli bacteria

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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