ArticleThe Journal of biological chemistry2011
Transcriptional regulation by Asf1: new mechanistic insights from studies of the DNA damage response to replication stress.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Article
- Review
- Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation.Nucleic acids research · 2019Article
- Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.Nucleic acids research · 2018Article
- Dot1 regulates nucleosome dynamics by its inherent histone chaperone activity in yeast.Nature communications · 2018Article
- ATR checkpoint kinase and CRL1βTRCP collaborate to degrade ASF1a and thus repress genes overlapping with clusters of stalled replication forks.Genes & development · 2014Article
- Characterization of two different Asf1 histone chaperones with distinct cellular localizations and functions in Trypanosoma brucei.Nucleic acids research · 2014Article
- Genome-wide mapping of yeast histone chaperone anti-silencing function 1 reveals its role in condensin binding with chromatin.PloS one · 2014Article
- ANTI-SILENCING FUNCTION1 proteins are involved in ultraviolet-induced DNA damage repair and are cell cycle regulated by E2F transcription factors in Arabidopsis.Plant physiology · 2013Article
- Characterization of the Pneumocystis carinii histone acetyltransferase chaperone proteins PcAsf1 and PcVps75.Infection and immunity · 2013Article
- The C terminus of the histone chaperone Asf1 cross-links to histone H3 in yeast and promotes interaction with histones H3 and H4.Molecular and cellular biology · 2013Article
- Article
- Sen1p contributes to genomic integrity by regulating expression of ribonucleotide reductase 1 (RNR1) in Saccharomyces cerevisiae.PloS one · 2013Article
- Promoter regulation by distinct mechanisms of functional interplay between lysine acetylase Rtt109 and histone chaperone Asf1.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Identification of a replication-independent replacement histone H3 in the basidiomycete Ustilago maydis.The Journal of biological chemistry · 2011Article
- SWI/SNF and Asf1 independently promote derepression of the DNA damage response genes under conditions of replication stress.PloS one · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Asf1 is a conserved histone H3/H4 chaperone. We find that Asf1 in budding yeast promotes an essential cellular response to replication stress caused by the ribonucleotide reductase inhibitor hydroxyurea. That is, Asf1 stimulates derepression of DNA damage response (DDR) genes during the S phase. Derepression of DDR genes strongly correlates with Asf1 binding to their promoters. Having identified the C terminus and histone-binding domains of Asf1 as molecular determinants of its constitutive and inducible association with chromatin, we tested whether Asf1 binding to DDR genes is mechanistically important for their derepression. Our results provide little support for this hypothesis. Rather, the contribution of Asf1 to DDR gene derepression depends on its ability to stimulate H3K56 acetylation by lysine acetyltransferase Rtt109. The precise regulation of H3K56 acetylation in the promoters of DDR genes is unexpected: DDR gene promoters are occupied by H3K56-acetylated nucleosomes under repressing conditions, and the steady state level of H3K56 promoter acetylation does not change upon derepression. We propose that replication-coupled deposition of Lys(56)-acetylated H3 poises the DDR genes in newly synthesized daughter duplexes for derepression during the S phase. In this model, the presence of a histone mark that destabilizes nucleosomes is compatible with suppression of transcription because in the uninduced state, DDR gene promoters are constitutively occupied by a potent repressor-corepressor complex.
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