- Genomics and Chromatin Dynamics
- DNA Repair Mechanisms
- RNA Research and Splicing
- Chromosomal and Genetic Variations
- DNA and Nucleic Acid Chemistry
- Protein Degradation and Inhibitors
- Microtubule and mitosis dynamics
- CRISPR and Genetic Engineering
- Enzyme Structure and Function
- Prion Diseases and Protein Misfolding
- Epigenetics and DNA Methylation
- Amino Acid Enzymes and Metabolism
- Radiation Therapy and Dosimetry
- Ubiquitin and proteasome pathways
- Cancer-related Molecular Pathways
- Nuclear Structure and Function
- Adenosine and Purinergic Signaling
- RNA and protein synthesis mechanisms
- Genetics and Neurodevelopmental Disorders
- Fungal and yeast genetics research
CEA Paris-Saclay - Etablissement de Fontenay-aux-roses
2017-2024
Université Paris Cité
2019-2024
CEA Paris-Saclay
2021-2024
Inserm
2017-2024
Université Paris-Saclay
2021-2024
Commissariat à l'Énergie Atomique et aux Énergies Alternatives
2017-2024
Institut de Radiobiologie Cellulaire et Moléculaire
2010-2023
Stabilité Génétique, Cellules Souches et Radiations
2023
Université Paris-Sud
2017-2019
Délégation Paris 7
2017
Abstract Nuclear pore complexes (NPCs) have increasingly recognized interactions with the genome, as exemplified in yeast, where they bind transcribed or damaged chromatin. By combining genome-wide approaches live imaging of model loci, we uncover a correlation between NPC association and accumulation R-loops, which are genotoxic structures formed through hybridization nascent RNAs their DNA templates. Manipulating hybrid formation demonstrates that R-loop per se, rather than transcription...
DNA double-strand breaks (DSBs) must be repaired to ensure genome stability. Crucially, DSB-ends kept together for timely repair. In Saccharomyces cerevisiae, two pathways mediate DSB end-tethering. One employs the Mre11–Rad50–Xrs2 (MRX) complex physically bridge DSB-ends. Another requires conversion of into single-strand (ssDNA) by Exo1, but bridging proteins are unknown. We uncover that cohesin, its loader and Smc5/6 act with Exo1 tether Remarkably, cohesin specifically impaired in...
Repair of a DNA double-strand break (DSB) by non-homologous end-joining (NHEJ) generally leaves an intact or minimally modified sequence. Resection initiation exposes single-stranded and directs repair towards homology-dependent pathways away from NHEJ. Therefore, NHEJ is not thought to be available pathway once the DSB resected. Here, we report that Cdc13/Stn1/Ten1 (CST) complex, well characterized for its telomere-associated functions, acts after resection mediate backup repair. We found...
Abstract Homologous recombination (HR) is essential for the repair of DNA double-strand breaks and restart stalled replication forks. A critical step in HR formation Rad51 nucleofilaments, which perform homology search strand invasion a homologous sequence required synthesis. In yeast Saccharomyces cerevisiae , Rad52 facilitates nucleofilament by mediating loading onto ssDNA counteracting dissociation filaments translocase Srs2. The molecular basis these two functions remains unclear. Our...
Abstract DNA double-strand breaks (DSB) must be repaired to ensure genome stability. Crucially, DSB ends kept together for timely repair. In Saccharomyces cerevisiae , two poorly understood pathways mediate end-tethering. One employs the Mre11-Rad50-Xrs2 (MRX) complex physically bridge ends. Another requires conversion of into single-strand (ssDNA) by Exo1, but bridging proteins are unknown. We uncover that cohesin, its loader and Smc5/6 act with Exo1 tether Remarkably, cohesin specifically...
Abstract Heterochromatin is a conserved feature of eukaryotic chromosomes, with central roles in gene expression regulation and maintenance genome stability. How heterochromatin proteins regulate DNA repair remains poorly described. In Saccharomyces cerevisiae , the Silent Information Regulator (SIR) complex assembles heterochromatin-like chromatin at subtelomeres. SIR-mediated repressive limits double strand break (DSB) resection protecting damaged chromosome ends during HR. As initiation...