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

Ling Zhang, Hua Chen, Xin Bi, Feng Gong

Research output: Contribution to journalArticle

2 Scopus citations

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 languageEnglish (US)
Pages (from-to)2435-2442
Number of pages8
JournalCell Cycle
Volume12
Issue number15
DOIs
StatePublished - Aug 1 2013

Keywords

  • Heterochromatin
  • HML
  • Nucleotide excision repair
  • Rad4p
  • SIR complex

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Developmental Biology

Fingerprint Dive into the research topics of 'Detection of an altered heterochromatin structure in the absence of the nucleotide excision repair protein Rad4 in Saccharomtyces cerevisiae'. Together they form a unique fingerprint.

  • Cite this