A conserved nuclease facilitates environmental DNA uptake

Bacteria acquire new traits through the uptake of genetic material from the environment, a process requiring DNA processing. However, the molecular inventory mediating this process is far from being completely understood. Here, we identify YhaM in Bacillus subtilis as a conserved 3'-deoxyribonuclease essential for the uptake and processing of genetic information in the form of single-stranded DNA. Our results show that YhaM assembles into hexamers in the presence of divalent cations, enhancing substrate binding, which is achieved through its conserved oligonucleotide-binding domain. Cells lacking YhaM show a severe defect in the uptake of plasmids and genomic DNA, but the transduction of double-stranded DNA by the phage SPP1 remains unaffected. These findings highlight a critical role of YhaM in single-stranded DNA maturation during natural transformation. Importantly, this function is conserved in various Gram-positive human pathogens such as Staphylococcus aureus, suggesting that it could contribute to the spread of antibiotic resistance.

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Publication Details

Journal
Nucleic Acids Research
Published
2025-05-22
DOI
https://doi.org/10.1093/nar/gkaf443
Citations
2
Primary Topic
Bacteriophages and microbial interactions
Type
article
Field-Weighted Citation Impact
3.43

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article

A conserved nuclease facilitates environmental DNA uptake

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A conserved nuclease facilitates environmental DNA uptake

Juri Hanßmann, Christine Ziegler, Clemens Thölken, Franziska Sendker, Marcus Lechner, Lifei Fu, Martin Thanbichler, Gert Bange, Jan Pané‐Farré, Mathias Girbig, M. Gregor Madej, Georg Hochberg, Rebecca Hinrichs, Milena Meiser
article en
2 citations

Abstract

Bacteria acquire new traits through the uptake of genetic material from the environment, a process requiring DNA processing. However, the molecular inventory mediating this process is far from being completely understood. Here, we identify YhaM in Bacillus subtilis as a conserved 3'-deoxyribonuclease essential for the uptake and processing of genetic information in the form of single-stranded DNA. Our results show that YhaM assembles into hexamers in the presence of divalent cations, enhancing substrate binding, which is achieved through its conserved oligonucleotide-binding domain. Cells lacking YhaM show a severe defect in the uptake of plasmids and genomic DNA, but the transduction of double-stranded DNA by the phage SPP1 remains unaffected. These findings highlight a critical role of YhaM in single-stranded DNA maturation during natural transformation. Importantly, this function is conserved in various Gram-positive human pathogens such as Staphylococcus aureus, suggesting that it could contribute to the spread of antibiotic resistance.

Nucleic Acids ResearchVol. 53(10)
Philipps University of Marburg (DE), Loewe Center for Synthetic Microbiology (DE), Max Planck Institute for Terrestrial Microbiology (DE), University of Regensburg (DE)
Philipps-Universität Marburg, Deutsche Forschungsgemeinschaft, Max-Planck-Gesellschaft, Peter und Traudl Engelhorn Stiftung, H2020 European Research Council
Life in Land
Openalex Percentile: Top 9%
Bacteriophages and microbial interactions
3.43
DOIOpen Access PDFOpenAlex
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