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TitleOcr-mediated suppression of BrxX unveils a phage counter-defense mechanism.
Journal, issue, pagesNucleic Acids Res, Vol. 52, Issue 14, Page 8580-8594, Year 2024
Publish dateAug 12, 2024
AuthorsShen Li / Tianhao Xu / Xinru Meng / Yujuan Yan / Ying Zhou / Lei Duan / Yulong Tang / Li Zhu / Litao Sun /
PubMed AbstractThe burgeoning crisis of antibiotic resistance has directed attention to bacteriophages as natural antibacterial agents capable of circumventing bacterial defenses. Central to this are the bacterial ...The burgeoning crisis of antibiotic resistance has directed attention to bacteriophages as natural antibacterial agents capable of circumventing bacterial defenses. Central to this are the bacterial defense mechanisms, such as the BREX system, which utilizes the methyltransferase BrxX to protect against phage infection. This study presents the first in vitro characterization of BrxX from Escherichia coli, revealing its substrate-specific recognition and catalytic activity. We demonstrate that BrxX exhibits nonspecific DNA binding but selectively methylates adenine within specific motifs. Kinetic analysis indicates a potential regulation of BrxX by the concentration of its co-substrate, S-adenosylmethionine, and suggests a role for other BREX components in modulating BrxX activity. Furthermore, we elucidate the molecular mechanism by which the T7 phage protein Ocr (Overcoming classical restriction) inhibits BrxX. Despite low sequence homology between BrxX from different bacterial species, Ocr effectively suppresses BrxX's enzymatic activity through high-affinity binding. Cryo-electron microscopy and biophysical analyses reveal that Ocr, a DNA mimic, forms a stable complex with BrxX, highlighting a conserved interaction interface across diverse BrxX variants. Our findings provide insights into the strategic counteraction by phages against bacterial defense systems and offer a foundational understanding of the complex interplay between phages and their bacterial hosts, with implications for the development of phage therapy to combat antibiotic resistance.
External linksNucleic Acids Res / PubMed:38989624 / PubMed Central
MethodsEM (single particle)
Resolution3.09 - 3.18 Å
Structure data

60037

8zek

EMDB-60037, PDB-8zek:
Cryo-EM structure of the E. coli BrxX methyltransferase complexed with Ocr
Method: EM (single particle) / Resolution: 3.15 Å

EMDB-60038: The composite map of E. coli BrxX methyltransferase in complex with Ocr resolved by cryo-EM
Method: EM (single particle) / Resolution: 3.15 Å

EMDB-62670: Local refinement map of the NTD and MTD regions of BrxX in the BrxX-Ocr complex
Method: EM (single particle) / Resolution: 3.18 Å

EMDB-62678: Local refinement map of the TRD and CTD regions of BrxX and two Ocr molecules in the BrxX-Ocr complex
Method: EM (single particle) / Resolution: 3.09 Å

Source
  • escherichia coli (E. coli)
  • escherichia phage t7 (virus)
KeywordsTRANSFERASE / methyltransferase / complex

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