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Crosstalk between diverse synthetic protein degradation tags in Escherichia coli

Nicholas C. Butzin, William H. Mather
doi: https://doi.org/10.1101/136812
Nicholas C. Butzin
1Department of Physics, Virginia Polytechnic Inst. and State University
2Center for Soft Matter and Biological Physics, Virginia Polytechnic Inst. and State University
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William H. Mather
1Department of Physics, Virginia Polytechnic Inst. and State University
2Center for Soft Matter and Biological Physics, Virginia Polytechnic Inst. and State University
3Deptartment of Biology, Virginia Polytechnic Inst. and State University
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  • For correspondence: wmather@vt.edu
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Abstract

Recently, a synthetic circuit in E. coli demonstrated that two proteins engineered with LAA tags targeted to the native protease ClpXP are susceptible to crosstalk due to competition for degradation between proteins. To understand proteolytic crosstalk beyond the single protease regime, we investigated in E. coli a set of synthetic circuits designed to probe the dynamics of existing and novel degradation tags fused to fluorescent proteins. These circuits were tested using both microplate reader and single-cell assays. We first quantified the degradation rates of each tag in isolation. We then tested if there was crosstalk between two distinguishable fluorescent proteins engineered with identical or different degradation tags. We demonstrated that proteolytic crosstalk was indeed not limited to the LAA degradation tag, but was also apparent between other diverse tags, supporting the complexity of the E. coli protein degradation system.

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Posted May 11, 2017.
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Crosstalk between diverse synthetic protein degradation tags in Escherichia coli
Nicholas C. Butzin, William H. Mather
bioRxiv 136812; doi: https://doi.org/10.1101/136812
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Crosstalk between diverse synthetic protein degradation tags in Escherichia coli
Nicholas C. Butzin, William H. Mather
bioRxiv 136812; doi: https://doi.org/10.1101/136812

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