Abstract
Rad4p is a DNA damage recognition protein essential for global genomic nucleotide excision repair in Saccharomyces cerevisiae. Here, we show that Rad4p binds to the heterochromatic HML locus. In a yeast mutant lacking Rad4p, an increased level of SIR complex binding at the HML locus is accompanied by an altered, more compact heterochromatin structure, as revealed by a topological analysis of chromatin circles released from the locus. In addition, gene silencing at the HML locus is enhanced in the rad4Δ mutant. Importantly, re-expression of Rad4p in the rad4Δ mutant restores the altered heterochromatin structure to a conformation similar to that detected in wild-type cells. These findings reveal a novel role of Rad4p in the regulation of heterochromatin structure and gene silencing.
Original language | English (US) |
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Pages (from-to) | 2435-2442 |
Number of pages | 8 |
Journal | Cell Cycle |
Volume | 12 |
Issue number | 15 |
DOIs | |
State | Published - Aug 1 2013 |
Keywords
- Heterochromatin
- HML
- Nucleotide excision repair
- Rad4p
- SIR complex
ASJC Scopus subject areas
- Cell Biology
- Molecular Biology
- Developmental Biology