Back to Search
Start Over
Variant histone H2A.Z, but not the HMG proteins Nhp6a/b, is essential for the recruitment of Swi/Snf, Mediator, and SAGA to the yeast GAL1 UAS(G).
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2008 May 16; Vol. 369 (4), pp. 1103-7. Date of Electronic Publication: 2008 Mar 10. - Publication Year :
- 2008
-
Abstract
- Chromatin architecture is very important for the regulation of transcriptional activation. Here, we investigated the role of two different chromatin components, the histone variant H2A.Z and HMG proteins Nhp6a/b, in regulating GAL1 gene expression. We have shown that recruitment of the Mediator complex is significantly affected in the absence of H2A.Z. Furthermore, H2A.Z is also required to fully recruit the SAGA and Swi/Snf complexes to the yeast GAL1-10 UAS(G). On the other hand, the HMG protein Nhp6a/b is not required to recruit the aforementioned components to the GAL1 promoter. The Nhp6 protein has been shown to interact with nucleosomes, and we show that its distribution is unaffected in the absence of H2A.Z. Our results suggest that the incorporation of the histone variant H2A.Z, but not the HMG proteins Nhp6a/b, in promoter regions creates a specialized chromatin domain that is required for pre-initiation complex assembly at the GAL1 locus.
- Subjects :
- Chromosomal Proteins, Non-Histone metabolism
DNA-Binding Proteins genetics
HMGN Proteins
Histone Acetyltransferases metabolism
Histones genetics
Mediator Complex
Nuclear Proteins genetics
Promoter Regions, Genetic
Saccharomyces cerevisiae metabolism
Trans-Activators metabolism
Transcription Factors metabolism
DNA-Binding Proteins metabolism
Galactokinase genetics
Gene Expression Regulation, Fungal
High Mobility Group Proteins metabolism
Histones metabolism
Nuclear Proteins metabolism
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae Proteins genetics
Saccharomyces cerevisiae Proteins metabolism
Transcriptional Activation
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 369
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 18331823
- Full Text :
- https://doi.org/10.1016/j.bbrc.2008.02.144