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AtEAF1 is a potential platform protein for Arabidopsis NuA4 acetyltransferase complex
BACKGROUND: Histone acetyltransferase complex NuA4 and histone variant exchanging complex SWR1 are two chromatin modifying complexes which act cooperatively in yeast and share some intriguing structural similarities. Protein subunits of NuA4 and SWR1-C are highly conserved across eukaryotes, but for...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4358907/ https://www.ncbi.nlm.nih.gov/pubmed/25849764 http://dx.doi.org/10.1186/s12870-015-0461-1 |
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author | Bieluszewski, Tomasz Galganski, Lukasz Sura, Weronika Bieluszewska, Anna Abram, Mateusz Ludwikow, Agnieszka Ziolkowski, Piotr Andrzej Sadowski, Jan |
author_facet | Bieluszewski, Tomasz Galganski, Lukasz Sura, Weronika Bieluszewska, Anna Abram, Mateusz Ludwikow, Agnieszka Ziolkowski, Piotr Andrzej Sadowski, Jan |
author_sort | Bieluszewski, Tomasz |
collection | PubMed |
description | BACKGROUND: Histone acetyltransferase complex NuA4 and histone variant exchanging complex SWR1 are two chromatin modifying complexes which act cooperatively in yeast and share some intriguing structural similarities. Protein subunits of NuA4 and SWR1-C are highly conserved across eukaryotes, but form different multiprotein arrangements. For example, the human TIP60-p400 complex consists of homologues of both yeast NuA4 and SWR1-C subunits, combining subunits necessary for histone acetylation and histone variant exchange. It is currently not known what protein complexes are formed by the plant homologues of NuA4 and SWR1-C subunits. RESULTS: We report on the identification and molecular characterization of AtEAF1, a new subunit of Arabidopsis NuA4 complex which shows many similarities to the platform protein of the yeast NuA4 complex. AtEAF1 copurifies with Arabidopsis homologues of NuA4 and SWR1-C subunits ARP4 and SWC4 and interacts physically with AtYAF9A and AtYAF9B, homologues of the YAF9 subunit. Plants carrying a T-DNA insertion in one of the genes encoding AtEAF1 showed decreased FLC expression and early flowering, similarly to Atyaf9 mutants. Chromatin immunoprecipitation analyses of the single mutant Ateaf1b-2 and artificial miRNA knock-down Ateaf1 lines showed decreased levels of H4K5 acetylation in the promoter regions of major flowering regulator genes, further supporting the role of AtEAF1 as a subunit of the plant NuA4 complex. CONCLUSIONS: Growing evidence suggests that the molecular functions of the NuA4 and SWR1 complexes are conserved in plants and contribute significantly to plant development and physiology. Our work provides evidence for the existence of a yeast-like EAF1 platform protein in A. thaliana, filling an important gap in the knowledge about the subunit organization of the plant NuA4 complex. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12870-015-0461-1) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4358907 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-43589072015-03-14 AtEAF1 is a potential platform protein for Arabidopsis NuA4 acetyltransferase complex Bieluszewski, Tomasz Galganski, Lukasz Sura, Weronika Bieluszewska, Anna Abram, Mateusz Ludwikow, Agnieszka Ziolkowski, Piotr Andrzej Sadowski, Jan BMC Plant Biol Research Article BACKGROUND: Histone acetyltransferase complex NuA4 and histone variant exchanging complex SWR1 are two chromatin modifying complexes which act cooperatively in yeast and share some intriguing structural similarities. Protein subunits of NuA4 and SWR1-C are highly conserved across eukaryotes, but form different multiprotein arrangements. For example, the human TIP60-p400 complex consists of homologues of both yeast NuA4 and SWR1-C subunits, combining subunits necessary for histone acetylation and histone variant exchange. It is currently not known what protein complexes are formed by the plant homologues of NuA4 and SWR1-C subunits. RESULTS: We report on the identification and molecular characterization of AtEAF1, a new subunit of Arabidopsis NuA4 complex which shows many similarities to the platform protein of the yeast NuA4 complex. AtEAF1 copurifies with Arabidopsis homologues of NuA4 and SWR1-C subunits ARP4 and SWC4 and interacts physically with AtYAF9A and AtYAF9B, homologues of the YAF9 subunit. Plants carrying a T-DNA insertion in one of the genes encoding AtEAF1 showed decreased FLC expression and early flowering, similarly to Atyaf9 mutants. Chromatin immunoprecipitation analyses of the single mutant Ateaf1b-2 and artificial miRNA knock-down Ateaf1 lines showed decreased levels of H4K5 acetylation in the promoter regions of major flowering regulator genes, further supporting the role of AtEAF1 as a subunit of the plant NuA4 complex. CONCLUSIONS: Growing evidence suggests that the molecular functions of the NuA4 and SWR1 complexes are conserved in plants and contribute significantly to plant development and physiology. Our work provides evidence for the existence of a yeast-like EAF1 platform protein in A. thaliana, filling an important gap in the knowledge about the subunit organization of the plant NuA4 complex. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12870-015-0461-1) contains supplementary material, which is available to authorized users. BioMed Central 2015-03-05 /pmc/articles/PMC4358907/ /pubmed/25849764 http://dx.doi.org/10.1186/s12870-015-0461-1 Text en © Bieluszewski et al.; licensee BioMed Central. 2015 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Bieluszewski, Tomasz Galganski, Lukasz Sura, Weronika Bieluszewska, Anna Abram, Mateusz Ludwikow, Agnieszka Ziolkowski, Piotr Andrzej Sadowski, Jan AtEAF1 is a potential platform protein for Arabidopsis NuA4 acetyltransferase complex |
title | AtEAF1 is a potential platform protein for Arabidopsis NuA4 acetyltransferase complex |
title_full | AtEAF1 is a potential platform protein for Arabidopsis NuA4 acetyltransferase complex |
title_fullStr | AtEAF1 is a potential platform protein for Arabidopsis NuA4 acetyltransferase complex |
title_full_unstemmed | AtEAF1 is a potential platform protein for Arabidopsis NuA4 acetyltransferase complex |
title_short | AtEAF1 is a potential platform protein for Arabidopsis NuA4 acetyltransferase complex |
title_sort | ateaf1 is a potential platform protein for arabidopsis nua4 acetyltransferase complex |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4358907/ https://www.ncbi.nlm.nih.gov/pubmed/25849764 http://dx.doi.org/10.1186/s12870-015-0461-1 |
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