PreprintCited by 21Genomics and Chromatin DynamicsTrypanosoma species research and implicationsNuclear Structure and Function

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Histone divergence in Trypanosoma brucei results in unique alterations to nucleosome structure

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Preprint — published as 10.1093/nar/gkad577 · Paper page

Abstract

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-H2B interface 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 understanding evolutionary divergence in chromatin structure.

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Metadata

Authors
Deák, G., Wapenaar, H., Sandoval, G., Chen, R., Taylor, M. R. D., Burdett, H., Watson, J. A., Tuijtel, M. W., Webb, S., & Wilson, M. D.
Affiliations
  • Wellcome Centre for Cell Biology (GB)
  • Max Planck Institute of Biophysics (DE)
Corresponding author
Wilson, Marcus D.
Venue
Nucleic Acids Research
Publisher
openRxiv
Published
2023-04-17
Volume
51
Issue
15
Pages
7882-7899
ISSN
0305-1048 (ISSN-L)
OpenAlex
W4383709538
Cited by
21
References
1
Citations by year
2026: 5 · 2025: 9 · 2024: 6 · 2023: 1
FWCI
1.87
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Nucleic Acids Research (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, other-oa)
Funders
  • Wellcome Trust (210493, 087658/Z/08/Z, 203149)
  • Diamond Light Source
  • University of Edinburgh
  • Directorate for Biological Sciences
  • Medical Research Council (203149, T029471/1)
  • Biotechnology and Biological Sciences Research Council (BB/M010996/1, M010996, M010996/1, 203149)
  • Institute of Genetics
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Health Sciences › Medicine › Epidemiology › Trypanosoma species research and implications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords
nucleosome core particle, Trypanosoma brucei, kinetoplastids, nucleosome structure, acidic patch, DNA binding
MeSH terms
Chromatin, DNA, Histones, Nucleosomes, Trypanosoma brucei brucei

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