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TitleOligomerisation of Ku from Mycobacterium tuberculosis promotes DNA synapsis.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 10568, Year 2025
Publish dateNov 26, 2025
AuthorsSayma Zahid / Sonia Baconnais / Henrietta Smith / Saseela Atwal / Lucy Bates / Harriet Read / Ankita Chadda / Florian Morati / Tom Bedwell / Emil G P Stender / Joanne Walter / Steven W Hardwick / Fredrik Westerlund / Eric Galburt / Eric Le Cam / Alice Pyne / Galina V Mukamolova / Amanda K Chaplin /
PubMed AbstractMycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB), is estimated to infect nearly one-quarter of the global population. A key factor in its resilience and persistence is its ...Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB), is estimated to infect nearly one-quarter of the global population. A key factor in its resilience and persistence is its robust DNA repair capacity. Non-homologous end joining (NHEJ) is the primary pathway for repairing DNA double-strand breaks (DSBs) in many organisms, including Mtb, where it is mediated by the Ku protein and the multifunctional LigD enzyme. In this study, we demonstrate that Ku is essential for mycobacterial survival under DNA-damaging conditions. Using cryogenic electron microscopy (cryo-EM), we solved high-resolution structures of both the apo and DNA-bound forms of the Ku-Mtb homodimer. Our structural and biophysical analyses reveal that Ku forms an extended proteo-filament upon binding DNA. We identify critical residues involved in filament formation and DNA synapsis and show that their mutation severely impairs bacterial viability. Furthermore, we propose a model in which the C-terminus of Ku regulates DNA binding and loading and facilitates subsequent recruitment of LigD. These findings provide unique insights into bacterial DNA repair and guide future therapeutics.
External linksNat Commun / PubMed:41298423 / PubMed Central
MethodsEM (single particle)
Resolution2.96 Å
Structure data

52748

9i91

EMDB-52748, PDB-9i91:
Ku from Mycobacterium tuberculosis bound to DNA
Method: EM (single particle) / Resolution: 2.96 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • mycobacterium tuberculosis (bacteria)
  • dna molecule (others)
KeywordsDNA BINDING PROTEIN / DNA repair / tuberculosis / NHEJ

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