Cargando…
Nhp2 is a reader of H2AQ105me and part of a network integrating metabolism with rRNA synthesis
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 modific...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8490984/ https://www.ncbi.nlm.nih.gov/pubmed/34409714 http://dx.doi.org/10.15252/embr.202152435 |
_version_ | 1784578655613091840 |
---|---|
author | Mawer, Julia S P Massen, Jennifer Reichert, Christina Grabenhorst, Niklas Mylonas, Constantine Tessarz, Peter |
author_facet | Mawer, Julia S P Massen, Jennifer Reichert, Christina Grabenhorst, Niklas Mylonas, Constantine Tessarz, Peter |
author_sort | Mawer, Julia S P |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-8490984 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-84909842021-10-14 Nhp2 is a reader of H2AQ105me and part of a network integrating metabolism with rRNA synthesis Mawer, Julia S P Massen, Jennifer Reichert, Christina Grabenhorst, Niklas Mylonas, Constantine Tessarz, Peter EMBO Rep Reports 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. John Wiley and Sons Inc. 2021-08-19 2021-10-05 /pmc/articles/PMC8490984/ /pubmed/34409714 http://dx.doi.org/10.15252/embr.202152435 Text en © 2021 The Authors. Published under the terms of the CC BY 4.0 license https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Reports Mawer, Julia S P Massen, Jennifer Reichert, Christina Grabenhorst, Niklas Mylonas, Constantine Tessarz, Peter Nhp2 is a reader of H2AQ105me and part of a network integrating metabolism with rRNA synthesis |
title | Nhp2 is a reader of H2AQ105me and part of a network integrating metabolism with rRNA synthesis |
title_full | Nhp2 is a reader of H2AQ105me and part of a network integrating metabolism with rRNA synthesis |
title_fullStr | Nhp2 is a reader of H2AQ105me and part of a network integrating metabolism with rRNA synthesis |
title_full_unstemmed | Nhp2 is a reader of H2AQ105me and part of a network integrating metabolism with rRNA synthesis |
title_short | Nhp2 is a reader of H2AQ105me and part of a network integrating metabolism with rRNA synthesis |
title_sort | nhp2 is a reader of h2aq105me and part of a network integrating metabolism with rrna synthesis |
topic | Reports |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8490984/ https://www.ncbi.nlm.nih.gov/pubmed/34409714 http://dx.doi.org/10.15252/embr.202152435 |
work_keys_str_mv | AT mawerjuliasp nhp2isareaderofh2aq105meandpartofanetworkintegratingmetabolismwithrrnasynthesis AT massenjennifer nhp2isareaderofh2aq105meandpartofanetworkintegratingmetabolismwithrrnasynthesis AT reichertchristina nhp2isareaderofh2aq105meandpartofanetworkintegratingmetabolismwithrrnasynthesis AT grabenhorstniklas nhp2isareaderofh2aq105meandpartofanetworkintegratingmetabolismwithrrnasynthesis AT mylonasconstantine nhp2isareaderofh2aq105meandpartofanetworkintegratingmetabolismwithrrnasynthesis AT tessarzpeter nhp2isareaderofh2aq105meandpartofanetworkintegratingmetabolismwithrrnasynthesis |