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Class I Histone Deacetylase Thd1p Promotes Global Chromatin Condensation in Tetrahymena thermophila
- Source :
- Eukaryotic Cell. 6:1913-1924
- Publication Year :
- 2007
- Publisher :
- American Society for Microbiology, 2007.
-
Abstract
- Class I histone deacetylases (HDACs) regulate DNA-templated processes such as transcription. They act both at specific loci and more generally across global chromatin, contributing to acetylation patterns that may underlie large-scale chromatin dynamics. Although hypoacetylation is correlated with highly condensed chromatin, little is known about the contribution of individual HDACs to chromatin condensation mechanisms. Using the ciliated protozoan Tetrahymena thermophila , we investigated the role of a specific class I HDAC, Τhd1p, in the reversible condensation of global chromatin. In this system, the normal physiological response to cell starvation includes the widespread condensation of the macronuclear chromatin and general repression of gene transcription. We show that the chromatin in Thd1p-deficient cells failed to condense during starvation. The condensation failure correlated with aberrant hyperphosphorylation of histone H1 and the overexpression of CDC2 , encoding the major histone H1 kinase. Changes in the rate of acetate turnover on core histones and in the distribution of acetylated lysines 9 and 23/27 on histone H3 isoforms that were found to correlate with normal chromatin condensation were absent from Thd1p mutant cells. These results point to a role for a class I HDAC in the formation of reversible higher-order chromatin structures and global genome compaction through mechanisms involving the regulation of H1 phosphorylation and core histone acetylation/deacetylation kinetics.
- Subjects :
- Acetates
Biology
Methylation
Microbiology
Histone Deacetylases
Chromatin remodeling
Tetrahymena thermophila
Histones
Histone H3
Histone H1
Macronucleus
Histone H2A
Animals
Histone code
Phosphorylation
Molecular Biology
Lysine
Acetylation
Articles
General Medicine
Chromatin Assembly and Disassembly
Mi-2/NuRD complex
Chromatin
Biochemistry
Histone methyltransferase
Mutation
Food Deprivation
Subjects
Details
- ISSN :
- 15359786 and 15359778
- Volume :
- 6
- Database :
- OpenAIRE
- Journal :
- Eukaryotic Cell
- Accession number :
- edsair.doi.dedup.....b1d2474bda6e9b4248040392ee968bd1