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TitleStructural basis for TRF2-RAP1 recruitment by EBNA1 at the EBV origin of replication.
Journal, issue, pagesSci Rep, Vol. 16, Issue 1, Year 2026
Publish dateApr 9, 2026
AuthorsSamantha Sustek / Troy E Messick / Jayaraju Dheekollu / Coltin Albitz / Christopher Chen / Anneliese Faustino / Hsin-Yao Tang / Hee Jong Kim / Kenji Murakami / Paul M Lieberman /
PubMed AbstractEpstein-Barr Nuclear Antigen 1 (EBNA1) is essential for the episomal maintenance and DNA replication of Epstein-Barr virus (EBV) in latently infected cells and acts through binding to The minimal ...Epstein-Barr Nuclear Antigen 1 (EBNA1) is essential for the episomal maintenance and DNA replication of Epstein-Barr virus (EBV) in latently infected cells and acts through binding to The minimal replicative unit of (½DS) contains four EBNA1 binding sites flanked by single telomeric nonamers that recruit shelterin proteins TRF2 and Rap1, but the structural basis for host-factor engagement is not known. Here, we integrate cryo-electron microscopy, zero-length cross-linking mass spectrometry, Alphafold3 modeling, and biochemical binding assays to define the complex formed by EBNA1-TRF2-Rap1 assembly on the ½DS. We find that a highly dynamic complex is formed, with the TRF2 homodimerization domain (TRFH) flexibly interacting with EBNA1 on the surface opposite the DNA-binding region, where there is a large acidic patch in EBNA1 that is unique amongst the herpesvirus episome maintenance proteins. Mutagenesis of this acidic patch abolishes TRFH binding and dependent plasmid replication. These findings identify a previously uncharacterized acidic patch docking surface on EBNA1 essential for coordinating TRF2-Rap1 at and provide new insights into both EBV and telomere DNA replication.
SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1038/s41598-026-43067-w.
External linksSci Rep / PubMed:41957069 / PubMed Central
MethodsEM (single particle)
Resolution7.1 Å
Structure data

EMDB-73305: Cryo-EM structure of the EBV 1/2 DS bound to the EBNA1 DBD, TRF2, and Rap1
Method: EM (single particle) / Resolution: 7.1 Å

Source
  • Escherichia coli (E. coli)

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