Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification
Open accessAbstract
Nucleosomes are decorated with numerous post-translational modifications capable of influencing many DNA processes. Here we describe a new class of histone modification, methylation of glutamine, occurring on yeast histone H2A at position 105 (Q105) and human H2A at Q104. We identify Nop1 as the methyltransferase in yeast and demonstrate that fibrillarin is the orthologue enzyme in human cells. Glutamine methylation of H2A is restricted to the nucleolus. Global analysis in yeast, using an H2AQ105me-specific antibody, shows that this modification is exclusively enriched over the 35S ribosomal DNA transcriptional unit. We show that the Q105 residue is part of the binding site for the histone chaperone FACT (facilitator of chromatin transcription) complex. Methylation of Q105 or its substitution to alanine disrupts binding to FACT in vitro. A yeast strain mutated at Q105 shows reduced histone incorporation and increased transcription at the ribosomal DNA locus. These features are phenocopied by mutations in FACT complex components. Together these data identify glutamine methylation of H2A as the first histone epigenetic mark dedicated to a specific RNA polymerase and define its function as a regulator of FACT interaction with nucleosomes.
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Many tumour suppressor genes are silenced by DNA methylation in cancer.
“Notably, many tumour suppressor genes are silenced by DNA methylation in cancer 23 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [23]
CpG DNA methylation represents a fundamental mechanism of stable repression underlying X chromosome inactivation and gene imprinting.
“CpG DNA methylation represents a fundamental mechanism of stable repression underlying processes such as X chromosome inactivation [G] and gene imprinting [G] 23 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [23]
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References 43 · Cited by 243
- Authors
- Tessarz, P., Santos-Rosa, H., Robson, S. C., Sylvestersen, K. B., Nelson, C. J., Nielsen, M. L., & Kouzarides, T.
- Affiliations
- University of Cambridge (GB)
- University of Copenhagen (DK)
- University of Victoria (CA)
- Corresponding author
- Kouzarides, Tony
- ORCID
- Venue
- Nature
- Published
- 2013-12-18
- Volume
- 505
- Issue
- 7484
- Pages
- 564-568
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3901671
- OpenAlex
- W2044490236
- Cited by
- 243
- References
- 43
- Citations by year
- 2026: 6 · 2025: 16 · 2024: 19 · 2023: 14 · 2022: 16 · 2021: 23 · 2020: 18 · 2019: 28 · 2018: 22 · 2017: 13 · 2016: 26 · 2015: 27 · 2014: 15
- FWCI
- 10.16
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Wellcome Trust (092096)
- Cancer Research UK (10827, 17001, A10827)
- Novo Nordisk Fonden (NNF13OC0006477)
- Biotechnology and Biological Sciences Research Council (BB/K017438/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- histone modifications, RNA polymerase I, rRNA methyltransferase, fibrillarin, nucleolus, rDNA transcription, FACT complex, histone chaperone, nucleosome binding, yeast, human cells
- MeSH terms
- Alanine, Amino Acid Sequence, Binding Sites, Cell Nucleolus, Chromatin, Chromosomal Proteins, Non-Histone, DNA, Ribosomal, Epistasis, Genetic, Glutamine, Histones, Humans, Methylation, Methyltransferases, Molecular Sequence Data, Nuclear Proteins, Nucleosomes, Protein Binding, Protein Processing, Post-Translational, RNA, RNA Polymerase I, Saccharomyces cerevisiae, Substrate Specificity, Transcription, Genetic, Molecular Chaperones, Ribonucleoproteins, Small Nucleolar, Amino Acid Motifs, Saccharomyces cerevisiae Proteins, Multiprotein Complexes
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