Acetylation of the Yeast Histone H4 N Terminus Regulates Its Binding to Heterochromatin Protein SIR3
Open Access
- 1 February 2002
- journal article
- Published by Elsevier
- Vol. 277 (7) , 4778-4781
- https://doi.org/10.1074/jbc.m110532200
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Highly Specific Antibodies Determine Histone Acetylation Site Usage in Yeast Heterochromatin and EuchromatinMolecular Cell, 2001
- Effects of Histone Acetylation on the Solubility and Folding of the Chromatin FiberJournal of Biological Chemistry, 2001
- Acetylation Increases the α-Helical Content of the Histone Tails of the NucleosomeJournal of Biological Chemistry, 2000
- The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeastNature, 1996
- Spreading of transcriptional represser SIR3 from telomeric heterochromatinNature, 1996
- Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4.Genes & Development, 1996
- Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeastCell, 1995
- Histone H3 amino terminus is required for telomeric and silent mating locus repression in yeastNature, 1994
- Silent domains are assembled continuously from the telomere and are defined by promoter distance and strength, and by SIR3 dosage.Genes & Development, 1993
- Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeastCell, 1988