Global histone acetylation and deacetylation in yeast
Histone acetyltransferases and deacetylases can be targeted to promoters to activate or repress genes. For example, the histone acetyltransferase GCN5 is part of a yeast multiprotein complex that is recruited by the DNA-binding activator protein GCN4 (refs 1, 2,3). The histone deacetylase RPD3 compl...
Gespeichert in:
Veröffentlicht in: | Nature (London) 2000-11, Vol.408 (6811), p.495-498 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
Zusammenfassung: | Histone acetyltransferases and deacetylases can be targeted to promoters
to activate or repress genes. For example, the histone acetyltransferase GCN5
is part of a yeast multiprotein complex that is recruited by the DNA-binding
activator protein GCN4 (refs 1,
2,3). The histone deacetylase RPD3 complex
is recruited to DNA by the repressor UME6 (refs 4, 5); similar mechanisms exist in other eukaryotes.
However, deletion of RPD3 also increases expression of the PHO5
gene that is repressed by nucleosomes,
and regulated by GCN5 (ref. 10) but not by UME6.
We have determined whether acetylation and deacetylation are promoter specific
at PHO5, by using antibodies against acetylated lysine residues and
chromatin immunoprecipitation to examine the acetylation state of a 4.25-kilobase
region surrounding the PHO5 gene. Here we show that this region is
acetylated extensively by ESA1 and GCN5 and deacetylated by HDA1 and RPD3,
and that widespread histone modification affects three separate chromosomal
regions examined, which total 22 kb. Our data indicate that targeted
modification occurs in a background of global acetylation and deacetylation
that not only reduces basal transcription, but also allows a rapid return
to the initial state of acetylation when targeting is removed. |
---|---|
ISSN: | 0028-0836 1476-4687 |
DOI: | 10.1038/35044127 |