Article
Sir2 deacetylates histone H3 lysine 56 to regulate telomeric heterochromatin structure in yeast.
Molecular cell - 21 Sept 2007
Xu Feng, Zhang Qiongyi, Zhang Kangling, Xie Wei, Grunstein Michael
Abstract excerpt
At telomeric heterochromatin in yeast, the Sir protein complex spreads from Rap1 sites to silence adjacent genes. This cascade is believed to occur when Sir2, an NAD(+)-dependent enzyme, deacetylates histone H3 and H4 N termini, in particular histone H4 K16, enabling more Sir protein binding. Lysine 56 of histone H3 is located at the entry-exit points of the DNA superhelix surrounding the nucleosome, where it may...
Topics
- Acetylation
- Amino Acid Substitution
- Genes, Fungal
- Heterochromatin
- Histone Deacetylases
- Histones
- Lysine
- Mutation
- Protein Binding
- Saccharomyces cerevisiae
- Silent Information Regulator Proteins, Saccharomyces cerevisiae
- Sirtuin 2
- Sirtuins
- Site-Specific DNA-Methyltransferase (Adenine-Specific)