ArticleThe Journal of biological chemistry2012
Structure of C-terminal tandem BRCT repeats of Rtt107 protein reveals critical role in interaction with phosphorylated histone H2A during DNA damage repair.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 51 citations in OpenAlex.
- The neuronal A-to-I RNA editome of Solenopsis invicta expands conserved recoding repertoire between two ant species.BMC genomics · 2026Article
- Mms22-Rtt107 axis attenuates the DNA damage checkpoint and the stability of the Rad9 checkpoint mediator.Nature communications · 2025Article
- NSE5 subunit interacts with distant regions of the SMC arms in the Physcomitrium patens SMC5/6 complex.The Plant journal : for cell and molecular biology · 2024Article
- The Mms22-Rtt107 axis dampens the DNA damage checkpoint by reducing the stability of the Rad9 checkpoint mediator.Research square · 2024Article
- Analysis of BRCT5 domain-containing proteins reveals a new component of DNA damage repair in Arabidopsis.Frontiers in plant science · 2022Article
- Phosphorylation-dependent assembly of DNA damage response systems and the central roles of TOPBP1.DNA repair · 2021Review
- Nse5/6 is a negative regulator of the ATPase activity of the Smc5/6 complex.Nucleic acids research · 2021Article
- Molecular Basis for Control of Diverse Genome Stability Factors by the Multi-BRCT Scaffold Rtt107.Molecular cell · 2019Article
- Recruitment, loading, and activation of the Smc5-Smc6 SUMO ligase.Current genetics · 2019Review
- Quantitative sensing and signalling of single-stranded DNA during the DNA damage response.Nature communications · 2019Article
- Brc1 Promotes the Focal Accumulation and SUMO Ligase Activity of Smc5-Smc6 during Replication Stress.Molecular and cellular biology · 2019Article
- Reading chromatin signatures after DNA double-strand breaks.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Dbf4-dependent kinase and the Rtt107 scaffold promote Mus81-Mms4 resolvase activation during mitosis.The EMBO journal · 2017Article
- Slx4 scaffolding in homologous recombination and checkpoint control: lessons from yeast.Chromosoma · 2017Review
- Multi-BRCT scaffolds use distinct strategies to support genome maintenance.Cell cycle (Georgetown, Tex.) · 2016Review
- Histone H1 Limits DNA Methylation in Neurospora crassa.G3 (Bethesda, Md.) · 2016Article
- The Rtt107 BRCT scaffold and its partner modification enzymes collaborate to promote replication.Nucleus (Austin, Tex.) · 2016Review
- Slx4 and Rtt107 control checkpoint signalling and DNA resection at double-strand breaks.Nucleic acids research · 2016Article
- Critical Function of γH2A in S-Phase.PLoS genetics · 2015Article
- Assembly of Slx4 signaling complexes behind DNA replication forks.The EMBO journal · 2015Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rtt107 (regulator of Ty1 transposition 107; Esc4) is a DNA repair protein from Saccharomyces cerevisiae that can restore stalled replication forks following DNA damage. There are six BRCT (BRCA1 C-terminal) domains in Rtt107 that act as binding sites for other recruited proteins during DNA repair. Several Rtt107 binding partners have been identified, including Slx4, Rtt101, Rad55, and the Smc5/6 (structural maintenance of chromosome) protein complex. Rtt107 can reportedly be recruited to chromatin in the presence of Rtt101 and Rtt109 upon DNA damage, but the chromatin-binding site of Rtt107 has not been identified. Here, we report our investigation of the interaction between phosphorylated histone H2A (γH2A) and the C-terminal tandem BRCT repeats (BRCT(5)-BRCT(6)) of Rtt107. The crystal structures of BRCT(5)-BRCT(6) alone and in a complex with γH2A reveal the molecular basis of the Rtt107-γH2A interaction. We used in vitro mutagenesis and a fluorescence polarization assay to confirm the location of the Rtt107 motif that is crucial for this interaction. In addition, these assays indicated that this interaction requires the phosphorylation of H2A. An in vivo phenotypic analysis in yeast demonstrated the critical role of BRCT(5)-BRCT(6) and its interaction with γH2A during the DNA damage response. Our results shed new light on the molecular mechanism by which Rtt107 is recruited to chromatin in response to stalled DNA replication forks.
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