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TitleA conserved nuclease facilitates environmental DNA uptake.
Journal, issue, pagesNucleic Acids Res, Vol. 53, Issue 10, Year 2025
Publish dateMay 22, 2025
AuthorsJuri Hanßmann / Jan Pané-Farré / Milena Meiser / Mathias Girbig / Lifei Fu / M Gregor Madej / Franziska L Sendker / Clemens Thölken / Marcus Lechner / Christine Ziegler / Georg K A Hochberg / Gert Bange / Martin Thanbichler / Rebecca Hinrichs /
PubMed AbstractBacteria 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 ...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.
External linksNucleic Acids Res / PubMed:40421801 / PubMed Central
MethodsEM (single particle)
Resolution3.47 Å
Structure data

51819

9h3f

EMDB-51819, PDB-9h3f:
Cryo-EM structure of YhaM
Method: EM (single particle) / Resolution: 3.47 Å

Chemicals

ChemComp-MG:
Unknown entry

Source
  • bacillus subtilis (bacteria)
KeywordsDNA BINDING PROTEIN / 3'-5' exoribonuclease

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