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Saccharomyces cerevisiae Rad16 mediates ultraviolet‐dependent histone H3 acetylation required for efficient global genome nucleotide‐excision repair
Author(s) -
Teng Yumin,
Liu Hairong,
Gill Hefin W,
Yu Yachuan,
Waters Raymond,
Reed Simon H
Publication year - 2008
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7401112
Subject(s) - saccharomyces cerevisiae , histone , nucleotide excision repair , acetylation , biology , genetics , genome , nucleotide , dna , dna repair , gene
In yeast, global genome nucleotide‐excision repair (GG‐NER) requires a protein complex containing Rad7 and Rad16. Rad16 is a member of the switch/sucrose nonfermentable superfamily, and it is presumed that chromatin remodelling is its primary function during repair. We show that RAD16 is required for ultraviolet‐dependent hyperacetylation of histone H3 (Lys 9 and Lys 14) at the MFA2 promoter and throughout the genome. The yeast repressor complex Ssn6–Tup1 represses many genes including MFA2 . TUP1 deletion results in constitutive hyperacetylation of histone H3, nucleosome disruption and derepression of gene transcription in Tup1‐regulated genes. GG‐NER in the MFA2 promoter proceeds more rapidly in tup1 Δ α‐cells compared with wild type, even when transcription is inhibited. We show that elevated histone H3 acetylation levels in the MFA2 promoter in tup1 Δ α‐cells result in Rad7‐ and Rad16‐independent GG‐NER, and that Rad16 mediates the ultraviolet‐induced acetylation of histone H3, necessary for efficient GG‐NER.