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TitleStructural basis for the inhibition of RecBCD by Gam and its synergistic antibacterial effect with quinolones.
Journal, issue, pagesElife, Vol. 5, Year 2016
Publish dateDec 23, 2016
AuthorsMartin Wilkinson / Luca Troman / Wan Ak Wan Nur Ismah / Yuriy Chaban / Matthew B Avison / Mark S Dillingham / Dale B Wigley /
PubMed AbstractOur previous paper (Wilkinson , 2016) used high-resolution cryo-electron microscopy to solve the structure of the RecBCD complex, which acts in both the repair of double-stranded DNA breaks and the ...Our previous paper (Wilkinson , 2016) used high-resolution cryo-electron microscopy to solve the structure of the RecBCD complex, which acts in both the repair of double-stranded DNA breaks and the degradation of bacteriophage DNA. To counteract the latter activity, bacteriophage λ encodes a small protein inhibitor called Gam that binds to RecBCD and inactivates the complex. Here, we show that Gam inhibits RecBCD by competing at the DNA-binding site. The interaction surface is extensive and involves molecular mimicry of the DNA substrate. We also show that expression of Gam in or increases sensitivity to fluoroquinolones; antibacterials that kill cells by inhibiting topoisomerases and inducing double-stranded DNA breaks. Furthermore, fluoroquinolone-resistance in clinical isolates is reversed by expression of Gam. Together, our data explain the synthetic lethality observed between topoisomerase-induced DNA breaks and the RecBCD gene products, suggesting a new co-antibacterial strategy.
External linksElife / PubMed:28009252 / PubMed Central
MethodsEM (single particle)
Resolution3.8 Å
Structure data

3460

5mbv

EMDB-3460, PDB-5mbv:
Cryo-EM structure of Lambda Phage protein GamS bound to RecBCD.
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • escherichia coli (E. coli)
  • enterobacteria phage lambda (virus)
KeywordsDNA BINDING PROTEIN / Inhibitor / Complex / DNA repair / Helicase/Nuclease

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