Histone divergence in trypanosomes results in unique alterations to nucleosome structure

Gauri Deák, Hannah Wapenaar, Gorka Sandoval, Ruofan Chen, Mark R D Taylor, Hayden Burdett, James Watson, Maarten W Tuijtel, Shaun Webb, Marcus D Wilson

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Eukaryotes have a multitude of diverse mechanisms for organising and using their genomes, but the histones that make up chromatin are highly conserved. Unusually, histones from kinetoplastids are highly divergent. The structural and functional consequences of this variation are unknown. Here, we have biochemically and structurally characterised nucleosome core particles (NCPs) from the kinetoplastid parasite Trypanosoma brucei. A structure of the T. brucei NCP reveals that global histone architecture is conserved, but specific sequence alterations lead to distinct DNA and protein interaction interfaces. The T. brucei NCP is unstable and has weakened overall DNA binding. However, dramatic changes at the H2A-H2Binterface introduce local reinforcement of DNA contacts. The T. brucei acidic patch has altered topology and is refractory to known binders, indicating that the nature of chromatin interactions in T. brucei may be unique. Overall, our results provide a detailed molecular basis for under standing evolutionary divergence in chromatin structure.
Original languageEnglish
Article numbergkad577
Pages (from-to)7882-7899
Number of pages66
JournalNucleic Acids Research
Issue number15
Early online date10 Jul 2023
Publication statusPublished - 25 Aug 2023

Keywords / Materials (for Non-textual outputs)

  • protein nucleic acid interaction
  • chromatin and epigenetics


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