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Abo1, a conserved bromodomain AAA‐ATPase, maintains global nucleosome occupancy and organisation
Maintenance of the correct level and organisation of nucleosomes is crucial for genome function. Here, we uncover a role for a conserved bromodomain AAA‐ATPase, Abo1, in the maintenance of nucleosome architecture in fission yeast. Cells lacking abo1 (+) experience both a reduction and mis‐positionin...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4718406/ https://www.ncbi.nlm.nih.gov/pubmed/26582768 http://dx.doi.org/10.15252/embr.201540476 |
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author | Gal, Csenge Murton, Heather E Subramanian, Lakxmi Whale, Alex J Moore, Karen M Paszkiewicz, Konrad Codlin, Sandra Bähler, Jürg Creamer, Kevin M Partridge, Janet F Allshire, Robin C Kent, Nicholas A Whitehall, Simon K |
author_facet | Gal, Csenge Murton, Heather E Subramanian, Lakxmi Whale, Alex J Moore, Karen M Paszkiewicz, Konrad Codlin, Sandra Bähler, Jürg Creamer, Kevin M Partridge, Janet F Allshire, Robin C Kent, Nicholas A Whitehall, Simon K |
author_sort | Gal, Csenge |
collection | PubMed |
description | Maintenance of the correct level and organisation of nucleosomes is crucial for genome function. Here, we uncover a role for a conserved bromodomain AAA‐ATPase, Abo1, in the maintenance of nucleosome architecture in fission yeast. Cells lacking abo1 (+) experience both a reduction and mis‐positioning of nucleosomes at transcribed sequences in addition to increased intragenic transcription, phenotypes that are hallmarks of defective chromatin re‐establishment behind RNA polymerase II. Abo1 is recruited to gene sequences and associates with histone H3 and the histone chaperone FACT. Furthermore, the distribution of Abo1 on chromatin is disturbed by impaired FACT function. The role of Abo1 extends to some promoters and also to silent heterochromatin. Abo1 is recruited to pericentromeric heterochromatin independently of the HP1 ortholog, Swi6, where it enforces proper nucleosome occupancy. Consequently, loss of Abo1 alleviates silencing and causes elevated chromosome mis‐segregation. We suggest that Abo1 provides a histone chaperone function that maintains nucleosome architecture genome‐wide. |
format | Online Article Text |
id | pubmed-4718406 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-47184062016-03-23 Abo1, a conserved bromodomain AAA‐ATPase, maintains global nucleosome occupancy and organisation Gal, Csenge Murton, Heather E Subramanian, Lakxmi Whale, Alex J Moore, Karen M Paszkiewicz, Konrad Codlin, Sandra Bähler, Jürg Creamer, Kevin M Partridge, Janet F Allshire, Robin C Kent, Nicholas A Whitehall, Simon K EMBO Rep Articles Maintenance of the correct level and organisation of nucleosomes is crucial for genome function. Here, we uncover a role for a conserved bromodomain AAA‐ATPase, Abo1, in the maintenance of nucleosome architecture in fission yeast. Cells lacking abo1 (+) experience both a reduction and mis‐positioning of nucleosomes at transcribed sequences in addition to increased intragenic transcription, phenotypes that are hallmarks of defective chromatin re‐establishment behind RNA polymerase II. Abo1 is recruited to gene sequences and associates with histone H3 and the histone chaperone FACT. Furthermore, the distribution of Abo1 on chromatin is disturbed by impaired FACT function. The role of Abo1 extends to some promoters and also to silent heterochromatin. Abo1 is recruited to pericentromeric heterochromatin independently of the HP1 ortholog, Swi6, where it enforces proper nucleosome occupancy. Consequently, loss of Abo1 alleviates silencing and causes elevated chromosome mis‐segregation. We suggest that Abo1 provides a histone chaperone function that maintains nucleosome architecture genome‐wide. John Wiley and Sons Inc. 2015-11-18 2016-01 /pmc/articles/PMC4718406/ /pubmed/26582768 http://dx.doi.org/10.15252/embr.201540476 Text en © 2015 The Authors. Published under the terms of the CC BY 4.0 license This is an open access article under the terms of the Creative Commons Attribution 4.0 (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Articles Gal, Csenge Murton, Heather E Subramanian, Lakxmi Whale, Alex J Moore, Karen M Paszkiewicz, Konrad Codlin, Sandra Bähler, Jürg Creamer, Kevin M Partridge, Janet F Allshire, Robin C Kent, Nicholas A Whitehall, Simon K Abo1, a conserved bromodomain AAA‐ATPase, maintains global nucleosome occupancy and organisation |
title | Abo1, a conserved bromodomain AAA‐ATPase, maintains global nucleosome occupancy and organisation |
title_full | Abo1, a conserved bromodomain AAA‐ATPase, maintains global nucleosome occupancy and organisation |
title_fullStr | Abo1, a conserved bromodomain AAA‐ATPase, maintains global nucleosome occupancy and organisation |
title_full_unstemmed | Abo1, a conserved bromodomain AAA‐ATPase, maintains global nucleosome occupancy and organisation |
title_short | Abo1, a conserved bromodomain AAA‐ATPase, maintains global nucleosome occupancy and organisation |
title_sort | abo1, a conserved bromodomain aaa‐atpase, maintains global nucleosome occupancy and organisation |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4718406/ https://www.ncbi.nlm.nih.gov/pubmed/26582768 http://dx.doi.org/10.15252/embr.201540476 |
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