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 |
|---|---|
| Pages (from-to) | 2435-2442 |
| Number of pages | 8 |
| Journal | Cell Cycle |
| Volume | 12 |
| Issue number | 15 |
| DOIs | |
| State | Published - Aug 1 2013 |
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Keywords
- Heterochromatin
- HML
- Nucleotide excision repair
- Rad4p
- SIR complex
ASJC Scopus subject areas
- Cell Biology
- Molecular Biology
- Developmental Biology
Cite this
Detection of an altered heterochromatin structure in the absence of the nucleotide excision repair protein Rad4 in Saccharomtyces cerevisiae. / Zhang, Ling; Chen, Hua; Bi, Xin; Gong, Feng.
In: Cell Cycle, Vol. 12, No. 15, 01.08.2013, p. 2435-2442.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Detection of an altered heterochromatin structure in the absence of the nucleotide excision repair protein Rad4 in Saccharomtyces cerevisiae
AU - Zhang, Ling
AU - Chen, Hua
AU - Bi, Xin
AU - Gong, Feng
PY - 2013/8/1
Y1 - 2013/8/1
N2 - 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.
AB - 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.
KW - Heterochromatin
KW - HML
KW - Nucleotide excision repair
KW - Rad4p
KW - SIR complex
UR - http://www.scopus.com/inward/record.url?scp=84881491156&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84881491156&partnerID=8YFLogxK
U2 - 10.4161/cc.25457
DO - 10.4161/cc.25457
M3 - Article
VL - 12
SP - 2435
EP - 2442
JO - Cell Cycle
JF - Cell Cycle
SN - 1538-4101
IS - 15
ER -