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Combinatorial design of chemical-dependent protein switches for controlling intracellular electron transfer

View ORCID ProfileBingyan Wu, View ORCID ProfileJoshua T. Atkinson, Dimithree Kahanda, George. N. Bennett, View ORCID ProfileJonathan J. Silberg
doi: https://doi.org/10.1101/645978
Bingyan Wu
1Biochemistry & Cell Biology Graduate Program, Rice University, MS-140, 6100 Main Street, Houston, TX, 77005
2Department of Biosciences, Rice University, MS-140, 6100 Main Street, Houston, TX, 77005
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Joshua T. Atkinson
2Department of Biosciences, Rice University, MS-140, 6100 Main Street, Houston, TX, 77005
3Systems, Synthetic, & Physical Biology Graduate Program, Rice University, MS-180, 6100 Main Street, Houston, TX, 77005
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Dimithree Kahanda
2Department of Biosciences, Rice University, MS-140, 6100 Main Street, Houston, TX, 77005
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George. N. Bennett
2Department of Biosciences, Rice University, MS-140, 6100 Main Street, Houston, TX, 77005
4Department of Chemical & Biomolecular Engineering, Rice University, 6100 Main Street, MS-362, Houston, Texas 77005
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Jonathan J. Silberg
2Department of Biosciences, Rice University, MS-140, 6100 Main Street, Houston, TX, 77005
4Department of Chemical & Biomolecular Engineering, Rice University, 6100 Main Street, MS-362, Houston, Texas 77005
5Department of Bioengineering, Rice University, 6100 Main Street, MS-142, Houston, Texas 77005
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  • For correspondence: joff@rice.edu
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ABSTRACT

One challenge with controlling electron flow in cells is the lack of biomolecules that directly couple the sensing of environmental conditions to electron transfer efficiency. To overcome this protein component limitation, we randomly inserted the ligand binding domain (LBD) from the human estrogen receptor (ER) into a thermostable 2Fe-2S ferredoxin (Fd) from Mastigocladus laminosus and used a bacterial selection to identify Fd-LBD fusion proteins that support electron transfer from a Fd-NADP reductase (FNR) to a Fd-dependent sulfite reductase (SIR). Mapping LBD insertion sites onto structure revealed that Fd tolerates domain insertion adjacent to or within the tetracysteine motif that coordinates the 2Fe-2S metallocluster. With both classes of the fusion proteins, cellular ET was enhanced by the ER antagonist 4-hydroxytamoxifen. In addition, one of Fds arising from ER-LBD insertion within the tetracysteine motif acquires an oxygen-tolerant 2Fe-2S cluster, suggesting that ET is regulated through post-translational ligand binding.

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Posted May 23, 2019.
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Combinatorial design of chemical-dependent protein switches for controlling intracellular electron transfer
Bingyan Wu, Joshua T. Atkinson, Dimithree Kahanda, George. N. Bennett, Jonathan J. Silberg
bioRxiv 645978; doi: https://doi.org/10.1101/645978
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Combinatorial design of chemical-dependent protein switches for controlling intracellular electron transfer
Bingyan Wu, Joshua T. Atkinson, Dimithree Kahanda, George. N. Bennett, Jonathan J. Silberg
bioRxiv 645978; doi: https://doi.org/10.1101/645978

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