ArticleEMBO reports2021
Nhp2 is a reader of H2AQ105me and part of a network integrating metabolism with rRNA synthesis.
Article in EMBO reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- Nucleoli-localized KANSL2 as an epigenetic regulator of ribosome biogenesis in glioblastoma cells.Communications biology · 2026Article
- Direct and Indirect Protein Interactions Link FUS Aggregation to Histone Post-Translational Modification Dysregulation and Growth Suppression in an ALS/FTD Yeast Model.Journal of fungi (Basel, Switzerland) · 2025Article
- Review
- Semisynthesis of Glutamine-Methylated Proteins Enabled by Genetic Code Expansion.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Histone post-translational modifications - cause and consequence of genome function.Nature reviews. Genetics · 2022Review
- Effects of Hst3p inhibition inFrontiers in cellular and infection microbiology · 2022Article
- Nhp2 is a reader of H2AQ105me and part of a network integrating metabolism with rRNA synthesis.EMBO reports · 2021Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
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Abstract
Ribosome biogenesis is an essential cellular process that requires integration of extracellular cues, such as metabolic state, with intracellular signalling, transcriptional regulation and chromatin accessibility at the ribosomal DNA. Here, we demonstrate that the recently identified histone modification, methylation of H2AQ105 (H2AQ105me), is an integral part of a dynamic chromatin network at the rDNA locus. Its deposition depends on a functional mTor signalling pathway and acetylation of histone H3 at position K56, thus integrating metabolic and proliferative signals. Furthermore, we identify a first epigenetic reader of this modification, the ribonucleoprotein Nhp2, which specifically recognizes H2AQ105me. Based on functional and proteomic data, we suggest that Nhp2 functions as an adapter to bridge rDNA chromatin with components of the small subunit processome to efficiently coordinate transcription of rRNA with its post-transcriptional processing. We support this by showing that an H2AQ105A mutant has a mild defect in early processing of rRNA.
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