Histone acetylation in chromatin structure and transcription
- 25 September 1997
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 389 (6649), 349-352
- https://doi.org/10.1038/38664
Abstract
The amino termini of histones extend from the nucleosomal core and are modified by acetyltransferases and deacetylases during the cell cycle. These acetylation patterns may direct histone assembly and help regulate the unfolding and activity of genes.Keywords
This publication has 78 references indexed in Scilit:
- What's Up and Down with Histone Deacetylation and Transcription?Cell, 1997
- Transcriptional activation by recruitmentNature, 1997
- The Transcriptional Coactivators p300 and CBP Are Histone AcetyltransferasesCell, 1996
- HDA1 and HDA3 Are Components of a Yeast Histone Deacetylase (HDA) ComplexPublished by Elsevier ,1996
- Yeast histone H3 and H4 amino termini are important for nucleosome assembly in vivo and in vitro: redundant and position-independent functions in assembly but not in gene regulation.Genes & Development, 1996
- Stable nucleosome positioning and complete repression by the yeast alpha 2 repressor are disrupted by amino-terminal mutations in histone H4.Genes & Development, 1992
- Yeast histone H4 N-terminal sequence is required for promoter activation in vivoCell, 1991
- A yeast protein that influences the chromatin structure of UASG and functions as a powerful auxiliary gene activator.Genes & Development, 1990
- Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeastCell, 1988
- NUCLEASE HYPERSENSITIVE SITES IN CHROMATINAnnual Review of Biochemistry, 1988