ArticlePLoS genetics2011
Substitutions in the amino-terminal tail of neurospora histone H3 have varied effects on DNA methylation.
Article in PLoS genetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- H3T11 phosphorylation by CKII is required for heterochromatin formation in Neurospora.Nucleic acids research · 2024Article
- Histone 3.3-related chromatinopathy: missense variants throughout H3-3A and H3-3B cause a range of functional consequences across species.Human genetics · 2024Review
- The effect of SiNPs on DNA methylation of genome in mouse spermatocytes.Environmental science and pollution research international · 2021Article
- Review
- Article
- Nucleosome Positioning by an Evolutionarily Conserved Chromatin Remodeler Prevents Aberrant DNA Methylation inGenetics · 2019Article
- Induction of H3K9me3 and DNA methylation by tethered heterochromatin factors inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Dual chromatin recognition by the histone deacetylase complex HCHC is required for proper DNA methylation in Neurospora crassa.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Loss of HP1 causes depletion of H3K27me3 from facultative heterochromatin and gain of H3K27me2 at constitutive heterochromatin.Genome research · 2016Article
- Neurospora importin α is required for normal heterochromatic formation and DNA methylation.PLoS genetics · 2015Article
- Heterochromatin controls γH2A localization in Neurospora crassa.Eukaryotic cell · 2014Article
- Effect of dynamic DNA methylation and histone acetylation on cPouV expression in differentiation of chick embryonic germ cells.Stem cells and development · 2013Article
- Neurospora crassa, a model system for epigenetics research.Cold Spring Harbor perspectives in biology · 2013Review
- Distinct amino acids of histone H3 control secondary metabolism in Aspergillus nidulans.Applied and environmental microbiology · 2013Article
- Regional control of histone H3 lysine 27 methylation in Neurospora.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Modification of enhancer chromatin: what, how, and why?Molecular cell · 2013Review
- A permissive chromatin structure is adopted prior to site-specific DNA demethylation of developmentally expressed genes involved in macronuclear differentiation.Epigenetics & chromatin · 2013Article
- Article
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5 authors at 1 institution in 1 country.
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Abstract
Eukaryotic genomes are partitioned into active and inactive domains called euchromatin and heterochromatin, respectively. In Neurospora crassa, heterochromatin formation requires methylation of histone H3 at lysine 9 (H3K9) by the SET domain protein DIM-5. Heterochromatin protein 1 (HP1) reads this mark and directly recruits the DNA methyltransferase, DIM-2. An ectopic H3 gene carrying a substitution at K9 (hH3(K9L) or hH3(K9R)) causes global loss of DNA methylation in the presence of wild-type hH3 (hH3(WT)). We investigated whether other residues in the N-terminal tail of H3 are important for methylation of DNA and of H3K9. Mutations in the N-terminal tail of H3 were generated and tested for effects in vitro and in vivo, in the presence or absence of the wild-type allele. Substitutions at K4, K9, T11, G12, G13, K14, K27, S28, and K36 were lethal in the absence of a wild-type allele. In contrast, mutants bearing substitutions of R2, A7, R8, S10, A15, P16, R17, K18, and K23 were viable. The effect of substitutions on DNA methylation were variable; some were recessive and others caused a semi-dominant loss of DNA methylation. Substitutions of R2, A7, R8, S10, T11, G12, G13, K14, and P16 caused partial or complete loss of DNA methylation in vivo. Only residues R8-G12 were required for DIM-5 activity in vitro. DIM-5 activity was inhibited by dimethylation of H3K4 and by phosphorylation of H3S10, but not by acetylation of H3K14. We conclude that the H3 tail acts as an integrating platform for signals that influence DNA methylation, in part through methylation of H3K9.
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