Escherichia coli SymE is a DNA‐binding protein that can condense the nucleoid
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/sym...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2023
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| Online Access: | https://hdl.handle.net/1721.1/150341 |
| _version_ | 1826209412266590208 |
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| author | Thompson, Mary K Nocedal, Isabel Culviner, Peter H Zhang, Tong Gozzi, Kevin R Laub, Michael T |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Thompson, Mary K Nocedal, Isabel Culviner, Peter H Zhang, Tong Gozzi, Kevin R Laub, Michael T |
| author_sort | Thompson, Mary K |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T14:22:06Z |
| format | Article |
| id | mit-1721.1/150341 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T14:22:06Z |
| publishDate | 2023 |
| publisher | Wiley |
| record_format | dspace |
| spelling | mit-1721.1/1503412023-04-04T03:15:33Z Escherichia coli SymE is a DNA‐binding protein that can condense the nucleoid Thompson, Mary K Nocedal, Isabel Culviner, Peter H Zhang, Tong Gozzi, Kevin R Laub, Michael T Massachusetts Institute of Technology. Department of Biology 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. 2023-04-03T15:21:50Z 2023-04-03T15:21:50Z 2022 2023-04-03T15:13:56Z Article http://purl.org/eprint/type/JournalArticle https://hdl.handle.net/1721.1/150341 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). en 10.1111/MMI.14877 Molecular Microbiology Creative Commons Attribution-Noncommercial-Share Alike http://creativecommons.org/licenses/by-nc-sa/4.0/ application/pdf Wiley PMC |
| spellingShingle | Thompson, Mary K Nocedal, Isabel Culviner, Peter H Zhang, Tong Gozzi, Kevin R Laub, Michael T Escherichia coli SymE is a DNA‐binding protein that can condense the nucleoid |
| title | Escherichia coli SymE is a DNA‐binding protein that can condense the nucleoid |
| title_full | Escherichia coli SymE is a DNA‐binding protein that can condense the nucleoid |
| title_fullStr | Escherichia coli SymE is a DNA‐binding protein that can condense the nucleoid |
| title_full_unstemmed | Escherichia coli SymE is a DNA‐binding protein that can condense the nucleoid |
| title_short | Escherichia coli SymE is a DNA‐binding protein that can condense the nucleoid |
| title_sort | escherichia coli syme is a dna binding protein that can condense the nucleoid |
| url | https://hdl.handle.net/1721.1/150341 |
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