Proteomics

Dataset Information

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HDX-MS analysis of the DNA-mKu interaction and dynamics

ABSTRACT: This project aims to decipher the DNA-protein interactions of the DNA end-binding protein mKu. In Mycobacterium tuberculosis and prokaryotes in general, Ku serves as the initiator of the non-homologous end-joining (NHEJ) DNA repair pathway. Using HDX-MS complemented with structural data, we investigate critical contacts at the DNA-protein interface and explore the dynamic behavior of the complex in solution.

INSTRUMENT(S):

ORGANISM(S): Mycobacterium Tuberculosis H37rv

DISEASE(S): Tuberculosis

SUBMITTER: Joydeep Baral  

LAB HEAD: Isabelle Rouiller

PROVIDER: PXD060776 | Pride | 2026-01-19

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
231031_cluster.csv Csv
231031_cluster_HIS_tag_removed.csv Csv
231031_mKu.DnX Other
Raw_files.zip Other
checksum.txt Txt
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Publications

Bringing the ends together: cryo-EM structures of mycobacterial Ku in complex with DNA define its role in NHEJ synapsis.

Baral Joydeep J   Ang Ching-Seng CS   McMillan Paul James PJ   Shobhana Kalyan K   Saini Ayushi A   Hinde Elizabeth E   Das Amit Kumar AK   Rouiller Isabelle I  

Nucleic acids research 20260101 1

Non-homologous end joining (NHEJ) is the sole pathway for repairing double-strand breaks in Mycobacterium tuberculosis during dormancy, relying on mycobacterial Ku (mKu) and ligase D, with mKu as the rate-limiting factor. Despite its essential role, the lack of structural information on prokaryotic Ku has hindered understanding of the molecular mechanisms underlying bacterial two-component NHEJ machinery. Here, we present the first cryo-electron microscopy (cryo-EM) structures of mKu in DNA-boun  ...[more]

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