Histone divergence in trypanosomes results in unique alterations to nucleosome structure
Open accessPublished version of a preprint
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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Cites
Highly accurate protein structure prediction with AlphaFold
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- 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
- ORCID
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2023-07-10
- Volume
- 51
- Issue
- 15
- Pages
- 7882-7899
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC10450195
- OpenAlex
- W4383709538
- Cited by
- 21
- References
- 4
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 6 · 2023: 1
- FWCI
- 1.86
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- 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)
- Medical Research Council (T029471/1)
- University of Edinburgh
- BBSRC (BB/M010996/1, 203149)
- SULSA
- Wellcome Centre for Cell Biology
- 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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