6533b7cffe1ef96bd1258734

RESEARCH PRODUCT

Comprehensive analysis of interacting proteins and genome-wide location studies of the Sas3-dependent NuA3 histone acetyltransferase complex

Mercè PamblancoLorena Magraner-pardoSara Vicente-muñozPaco RomeroVicente TorderaCelia P. Martinez-jimenez

subject

nt nucleotidePTM post-translational modificationNuA3 histone acetyltransferase complexChIP-on-chip chromatin immunoprecipitation with genome-wide location arraysBiologyArticleGeneral Biochemistry Genetics and Molecular BiologyChromatin remodelingHistonesHistone H3NuA3 nucleosomal acetyltransferase of histone H3Histone H1Histone H2APdp3TAP–MS strategyHistone codelcsh:QH301-705.5TAP tandem affinity purificationGeneticsRNAPII RNA polymerase IIHistone acetyltransferaseWCE whole cell extractSAGA Spt-Ada-Gcn acetyltransferaseWT wild-typeChromatinYeastCell biologyChIP-on-chiplcsh:Biology (General)Histone methyltransferasebiology.proteinHAT histone acetyltransferaseTSS transcription start site

description

Highlights • We characterise Sas3p and Gcn5p active HAT complexes in WT and deleted TAP-strains. • We confirm that Pdp3p interacts with NuA3, histones and chromatin regulators. • Pdp3p MS-analysis reveals its phosphorylation, ubiquitination and methylation. • Sas3p can substitute Gcn5p in acetylation of histone H3K14 but not of H3K9. • Genome-wide profiling of Sas3p supports its involvement in transcriptional elongation.

yearjournalcountryeditionlanguage
2014-07-24FEBS Open Bio
https://doi.org/10.1016/j.fob.2014.11.001