Abstract |
Post-translational modifications of histone proteins have a crucial role in regulating gene expression. If efficiently re-established after chromosome duplication, histone modifications could help propagate gene expression patterns in dividing cells by epigenetic mechanisms. We used an integrated approach to investigate the dynamics of the conserved methylation of histone H3 Lys 79 (H3K79) by Dot1. Our results show that methylation of H3K79 progressively changes after histone deposition, which is incompatible with a rapid copy mechanism. Instead, methylation accumulates on ageing histones, providing the cell with a timer mechanism to directly couple cell-cycle length to changes in chromatin modification on the nucleosome core.
|
Authors | Dirk De Vos, Floor Frederiks, Marit Terweij, Tibor van Welsem, Kitty F Verzijlbergen, Ekaterina Iachina, Erik L de Graaf, A F Maarten Altelaar, Gideon Oudgenoeg, Albert J R Heck, Jeroen Krijgsveld, Barbara M Bakker, Fred van Leeuwen |
Journal | EMBO reports
(EMBO Rep)
Vol. 12
Issue 9
Pg. 956-62
(Sep 01 2011)
ISSN: 1469-3178 [Electronic] England |
PMID | 21760613
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
|
Chemical References |
- Chromatin
- Histones
- Nuclear Proteins
- Nucleosomes
- Saccharomyces cerevisiae Proteins
- Dot1 protein, S cerevisiae
- Histone-Lysine N-Methyltransferase
|
Topics |
- Aging
(metabolism)
- Cell Cycle
- Chromatin
(metabolism)
- Gene Expression Regulation, Fungal
- Histone-Lysine N-Methyltransferase
(genetics, metabolism)
- Histones
(metabolism)
- Methylation
- Nuclear Proteins
(genetics, metabolism)
- Nucleosomes
- Protein Processing, Post-Translational
- Saccharomyces cerevisiae
(genetics, growth & development, metabolism)
- Saccharomyces cerevisiae Proteins
(genetics, metabolism)
|