ArticleNucleic acids research2007
The checkpoint Saccharomyces cerevisiae Rad9 protein contains a tandem tudor domain that recognizes DNA.
Article in Nucleic acids research, 2007. 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, 30 citations in OpenAlex.
- TPI and GAPDH Interact with Rad9, Linking Glycolytic Enzymes to Cancer.International journal of molecular sciences · 2026Article
- Yeast Nat4 regulates DNA damage checkpoint signaling through its N-terminal acetyltransferase activity on histone H4.PLoS genetics · 2024Article
- Modified chromosome structure caused by phosphomimetic H2A modulates the DNA damage response by increasing chromatin mobility in yeast.Journal of cell science · 2021Article
- Distinct associations of the Saccharomyces cerevisiae Rad9 protein link Mac1-regulated transcription to DNA repair.Current genetics · 2020Article
- The structure of a highly-conserved picocyanobacterial protein reveals a Tudor domain with an RNA-binding function.The Journal of biological chemistry · 2019Article
- Article
- Rad9 interacts with Aft1 to facilitate genome surveillance in fragile genomic sites under non-DNA damage-inducing conditions in S. cerevisiae.Nucleic acids research · 2014Article
- Retinoblastoma-binding protein 1 has an interdigitated double Tudor domain with DNA binding activity.The Journal of biological chemistry · 2014Article
- The histone methyltransferase Dot1/DOT1L as a critical regulator of the cell cycle.Cell cycle (Georgetown, Tex.) · 2014Review
- Eukaryotic DNA damage checkpoint activation in response to double-strand breaks.Cellular and molecular life sciences : CMLS · 2012Review
- Inviability of a DNA2 deletion mutant is due to the DNA damage checkpoint.Cell cycle (Georgetown, Tex.) · 2011Article
- Mad2 prolongs DNA damage checkpoint arrest caused by a double-strand break via a centromere-dependent mechanism.Current biology : CB · 2010Article
- Chromatin remodeling finds its place in the DNA double-strand break response.Nucleic acids research · 2009Review
- An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks.Molecular and cellular biology · 2009Article
- Di-methyl H4 lysine 20 targets the checkpoint protein Crb2 to sites of DNA damage.The Journal of biological chemistry · 2008Article
- The Multifaceted Role of Rad9 in the DNA Damage Response of Saccharomyces cerevisiae.Yeast (Chichester, England)Review
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Authors and funding
15 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA damage checkpoints are signal transduction pathways that are activated after genotoxic insults to protect genomic integrity. At the site of DNA damage, 'mediator' proteins are in charge of recruiting 'signal transducers' to molecules 'sensing' the damage. Budding yeast Rad9, fission yeast Crb2 and metazoan 53BP1 are presented as mediators involved in the activation of checkpoint kinases. Here we show that, despite low sequence conservation, Rad9 exhibits a tandem tudor domain structurally close to those found in human/mouse 53BP1 and fission yeast Crb2. Moreover, this region is important for the resistance of Saccharomyces cerevisiae to different genotoxic stresses. It does not mediate direct binding to a histone H3 peptide dimethylated on K79, nor to a histone H4 peptide dimethylated on lysine 20, as was demonstrated for 53BP1. However, the tandem tudor region of Rad9 directly interacts with single-stranded DNA and double-stranded DNAs of various lengths and sequences through a positively charged region absent from 53BP1 and Crb2 but present in several yeast Rad9 homologs. Our results argue that the tandem tudor domains of Rad9, Crb2 and 53BP1 mediate chromatin binding next to double-strand breaks. However, their modes of chromatin recognition are different, suggesting that the corresponding interactions are differently regulated.
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