Spreading of Sir3 protein in cells with severe histone H3 hypoacetylation
- 9 June 2003
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 100 (13) , 7551-7556
- https://doi.org/10.1073/pnas.1332299100
Abstract
Heterochromatin formation in yeast involves deacetylation of histones, but the precise relationship between acetylation and the association of proteins such as Sir3, Sir4, and the histone deacetylase Sir2 with chromatin is still unclear. Here we show that Sir3 protein spreads to subtelomeric DNA in cells lacking the transcription-related histone acetyltransferases GCN5 and ELP3 . Spreading correlates with hypoacetylation of lysines in the histone H3 tail and results in deacetylation of lysine 16 in histone H4. De-repression of genes situated very close to the ends of the chromosomes in gcn5 elp3 suggests that Sir3 spreads into subtelomeric DNA from the tip of the telomere. Interestingly, growth defects caused by gcn5 elp3 mutation can be suppressed by SIR deletion, suggesting that Sir proteins become detrimental for growth when chromatin is severely hypoacetylated.Keywords
This publication has 34 references indexed in Scilit:
- Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencingNature Genetics, 2002
- Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatinNature Genetics, 2002
- Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein associationGenes & Development, 2002
- Highly Specific Antibodies Determine Histone Acetylation Site Usage in Yeast Heterochromatin and EuchromatinMolecular Cell, 2001
- Overlapping roles for the histone acetyltransferase activities of SAGA and Elongator in vivoThe EMBO Journal, 2000
- Beyond the Nucleosome: Epigenetic Aspects of Position–Effect Variegation in DrosophilaCell, 1998
- 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
- Transcriptional silencing in yeast is associated with reduced nucleosome acetylation.Genes & Development, 1993