title: Identification and analysis of yeast nucleosomal histone acetyltransferase complexes.
abstract: Many studies have linked acetylation of lysine residues on the amino-terminal tails of the core histones to transcriptional activity of cellular chromatin. New insights into this field were gained on the identification of the first nuclear, type A histone acetyltransferase (HAT). The yeast transcriptional adaptor protein Gcn5 was identified as a nuclear HAT and thus provided a direct link between pathways of transcriptional activation and histone acetylation. However, while recombinant Gcn5 can efficiently acetylate free histone H3 and, to a lesser extent, H4 it is unable to acetylate nucleosomal histones. It is therefore very likely that additional proteins are required for Gcn5-mediated acetylation of chromosomal histones. We have recently shown that Gcn5 is the catalytic subunit of two high-molecular-weight histone acetyltransferase complexes in yeast. In addition to the Gcn5-containing ADA and SAGA HAT complexes we have identified two other HAT complexes in yeast. These are called NuA3 and NuA4 for their predominant specificity to acetylate histones H3 and H4, respectively. Here we describe the identification and characterization of four native nuclear high-molecular-weight HAT complexes in Saccharomyces cerevisiae. These purified HATs can be used in a variety of functional assays to further address questions of how acetylation has an impact on transcriptional regulation.
authors.affiliation: Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park 16802-4500, USA.
authors.forename: A
authors.initials: A
authors.lastname: Eberharter
authors.forename: S
authors.initials: S
authors.lastname: John
authors.forename: P A
authors.initials: PA
authors.lastname: Grant
authors.forename: R T
authors.initials: RT
authors.lastname: Utley
authors.forename: J L
authors.initials: JL
authors.lastname: Workman
mesh_terms: D000123:Acetyltransferases / Q000302:isolation & purification* / Q000378:metabolism*; D001671:Biochemistry / Q000379:methods*; D002457:Cell Extracts / Q000302:isolation & purification; D004268:DNA-Binding Proteins; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D005982:Glutathione Transferase / Q000737:chemistry / Q000378:metabolism; D051548:Histone Acetyltransferases; D006657:Histones / Q000737:chemistry / Q000378:metabolism; D009707:Nucleosomes / Q000201:enzymology*; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D013379:Substrate Specificity; D015003:Yeasts / Q000235:genetics / Q000378:metabolism*; D000099224:p300-CBP-Associated Factor
chemical_list: D000123:Acetyltransferases; D002457:Cell Extracts; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D005982:Glutathione Transferase; D051548:Histone Acetyltransferases; D006657:Histones; D009707:Nucleosomes; D010455:Peptides; D011494:Protein Kinases; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; C501392:GCN5 protein, S cerevisiae; D000099224:p300-CBP-Associated Factor