title: An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A.
abstract: A yeast gene has been identified that encodes a novel, evolutionarily conserved Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A. The gene has been named NAT4. Recombinant Nat4 protein acetylated a peptide corresponding to the N-terminal tail of H4, but not an H3 peptide nor the peptide adrenocorticotropin. H4 and H2A are N-terminally acetylated in all species from yeast to mammals and hence blocked from sequencing by Edman degradation. In contrast, H4 and H2A purified from a nat4 mutant were unacetylated and could be sequenced. Analysis of yeast histones by acid-urea gel electrophoresis showed that all the H4 and H2A from the mutant migrated more rapidly than the same histones from a wild type strain, consistent with the histones from the mutant having one extra positive charge due to one less acetylated amino group. A comparison of yeast proteins from wild type and a nat4 mutant by two-dimensional gel electrophoresis showed no evidence that other yeast proteins are substrates of this acetyltransferase. Thus, Nat4 may be dedicated specifically to the N-terminal acetylation of histones H4 and H2A. Surprisingly, nat4 mutants grow at a normal rate and have no readily observable phenotypes.
authors.affiliation: Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794-5215, USA.
authors.forename: Ok-kyu
authors.initials: OK
authors.lastname: Song
authors.forename: Xiaorong
authors.initials: X
authors.lastname: Wang
authors.forename: Jakob H
authors.initials: JH
authors.lastname: Waterborg
authors.forename: Rolf
authors.initials: R
authors.lastname: Sternglanz
mesh_terms: D000123:Acetyltransferases / Q000737:chemistry* / Q000378:metabolism* / Q000502:physiology*; D000324:Adrenocorticotropic Hormone / Q000737:chemistry; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D017124:Conserved Sequence; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D051548:Histone Acetyltransferases; D006657:Histones / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D063212:N-Terminal Acetyltransferase D; D010455:Peptides / Q000737:chemistry; D010641:Phenotype; D010957:Plasmids / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000502:physiology*; D014508:Urea / Q000494:pharmacology
chemical_list: D006657:Histones; D010455:Peptides; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D014508:Urea; D000324:Adrenocorticotropic Hormone; D000123:Acetyltransferases; D063212:N-Terminal Acetyltransferase D; C478385:NAT4 protein, S cerevisiae; D051548:Histone Acetyltransferases