title: AtEAF1 is a potential platform protein for Arabidopsis NuA4 acetyltransferase complex.
abstract: 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.
authors: Tomasz
authors: T
authors: Bieluszewski
authors: Lukasz
authors: L
authors: Galganski
authors: Weronika
authors: W
authors: Sura
authors: Anna
authors: A
authors: Bieluszewska
authors: Mateusz
authors: M
authors: Abram
authors: Agnieszka
authors: A
authors: Ludwikow
authors: Piotr Andrzej
authors: PA
authors: Ziolkowski
authors: Jan
authors: J
authors: Sadowski
mesh_terms: D000107:Acetylation / Q000187:drug effects; D000123:Acetyltransferases / Q000378:metabolism*; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000187:drug effects / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002467:Cell Nucleus / Q000187:drug effects / Q000378:metabolism; D035264:Flowers / Q000187:drug effects / Q000502:physiology; D018506:Gene Expression Regulation, Plant / Q000187:drug effects; D017343:Genes, Plant; D006657:Histones / Q000378:metabolism; D006877:Hydroxamic Acids / Q000494:pharmacology; D035683:MicroRNAs / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000378:metabolism*; D009154:Mutation / Q000235:genetics; D011485:Protein Binding / Q000187:drug effects; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D014158:Transcription, Genetic / Q000187:drug effects
chemical_list: D029681:Arabidopsis Proteins; D006657:Histones; D006877:Hydroxamic Acids; D035683:MicroRNAs; D046912:Multiprotein Complexes; D012333:RNA, Messenger; C012589:trichostatin A; D000123:Acetyltransferases