Escherichia coli SymE is a DNA‐binding protein that can condense the nucleoid
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nihms-1767296.pdf
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Accepted version
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2.61 MB
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Author(s)
Thompson, Mary K
Nocedal, Isabel
Culviner, Peter H
Zhang, Tong
Gozzi, Kevin R
Laub, Michael T
Date Issued
2022
Journal
Molecular Microbiology
Publisher
Wiley
Citation
Thompson, Mary K, Nocedal, Isabel, Culviner, Peter H, Zhang, Tong, Gozzi, Kevin R et al. 2022. "Escherichia coli SymE is a DNA‐binding protein that can condense the nucleoid." Molecular Microbiology, 117 (4).
Version
Author's final manuscript
Abstract
Type I toxin-antitoxin (TA) systems typically consist of a protein toxin that imbeds in the inner membrane where it can oligomerize and form pores that change membrane permeability, and an RNA antitoxin that interacts directly with toxin mRNA to inhibit its translation. In Escherichia coli, symE/symR is annotated as a type I TA system with a non-canonical toxin. SymE was initially suggested to be an endoribonuclease, but has predicted structural similarity to DNA binding proteins. To better understand SymE function, we used RNA-seq to examine cells ectopically producing it. Although SymE drives major changes in gene expression, we do not find strong evidence of endoribonucleolytic activity. Instead, our biochemical and cell biological studies indicate that SymE binds DNA. We demonstrate that the toxicity of symE overexpression likely stems from its ability to drive severe nucleoid condensation, which disrupts DNA and RNA synthesis and leads to DNA damage, similar to the effects of overproducing the nucleoid-associated protein H-NS. Collectively, our results suggest that SymE represents a new class of nucleoid-associated proteins that is widely distributed in bacteria.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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Creative Commons Attribution-Noncommercial-Share Alike
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DOI of Published Version
https://doi.org/10.1111/MMI.14877
