Construction and Characterization of Computationally Designed�ComR�Mutants
Lieberman, Ellie
Lieberman, Ellie
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Abstract
This project aims to engineer bacteria as whole-cell biosensors that detect specific peptide biomarkers using the ComR protein. ComR is a transcription factor from Streptococcus spp., which binds and is activated by a cognate peptide, XIP. ComR undergoes a conformational change upon binding XIP. The altered ComR then binds to a specific DNA sequence called the ComR box and activates transcription from downstream genes. A previously developed evolvability program was used to generate point mutations in the ComR sequence to better match patterns in naturally occurring sequences. These mutants were then constructed and characterized through a genetic system in E. coli, in which ComR activation with exogenous peptide leads to GFP expression. Compared to the WT ComR, one of these mutants (H172) has exhibited a higher fold increase in GFP expression in response to the XIP peptide. Additionally, both WT and mutant ComR appear to have increased XIP induced activity within a narrow range of expression.
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Date
1/1/2026
Student Status
Senior (Graduating in 2026)
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Oral Presentation
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Program/Major
Biomedical Engineering
College/School
College of Engineering and Mathematical Sciences
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Engineering