Format

Send to:

Choose Destination
See comment in PubMed Commons below
Cell Cycle. 2013 Aug 1;12(15):2435-42. doi: 10.4161/cc.25457. Epub 2013 Jul 3.

Detection of an altered heterochromatin structure in the absence of the nucleotide excision repair protein Rad4 in Saccharomyces cerevisiae.

Author information

  • 1Department of Biochemistry and Molecular Biology; University of Miami Miller School of Medicine; Miami, FL USA.

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.

KEYWORDS:

HML; Rad4p; SIR complex; heterochromatin; nucleotide excision repair

PMID:
23839037
[PubMed - indexed for MEDLINE]
PMCID:
PMC3841322
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Landes Bioscience Icon for PubMed Central
    Loading ...
    Write to the Help Desk