@article{TrifaultMamontovaCossaetal.2024,
  author    = {Trifault, Barbara and Mamontova, Victoria and Cossa, Giacomo and Ganskih, Sabina and Wei, Yuanjie and Hofstetter, Julia and Bhandare, Pranjali and Baluapuri, Apoorva and Nieto, Blanca and Solvie, Daniel and Ade, Carsten P. and Gallant, Peter and Wolf, Elmar and Larsen, Dorthe H. and Munschauer, Mathias and Burger, Kaspar},
  title     = {Nucleolar detention of NONO shields DNA double-strand breaks from aberrant transcripts},
  series = {Nucleic Acids Research},
  volume    = {52},
  journal   = {Nucleic Acids Research},
  number    = {6},
  doi       = {10.1093/nar/gkae022},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-350208},
  pages     = {3050-3068},
  year      = {2024},
  abstract  = {RNA-binding proteins emerge as effectors of the DNA damage response (DDR). The multifunctional non-POU domain-containing octamer-binding protein NONO/p54\(^{nrb}\) marks nuclear paraspeckles in unperturbed cells, but also undergoes re-localization to the nucleolus upon induction of DNA double-strand breaks (DSBs). However, NONO nucleolar re-localization is poorly understood. Here we show that the topoisomerase II inhibitor etoposide stimulates the production of RNA polymerase II-dependent, DNA damage-inducible antisense intergenic non-coding RNA (asincRNA) in human cancer cells. Such transcripts originate from distinct nucleolar intergenic spacer regions and form DNA-RNA hybrids to tether NONO to the nucleolus in an RNA recognition motif 1 domain-dependent manner. NONO occupancy at protein-coding gene promoters is reduced by etoposide, which attenuates pre-mRNA synthesis, enhances NONO binding to pre-mRNA transcripts and is accompanied by nucleolar detention of a subset of such transcripts. The depletion or mutation of NONO interferes with detention and prolongs DSB signalling. Together, we describe a nucleolar DDR pathway that shields NONO and aberrant transcripts from DSBs to promote DNA repair.},
  language  = {en}
}
@article{RohlederHuangXueetal.2016,
  author    = {Rohleder, Florian and Huang, Jing and Xue, Yutong and Kuper, Jochen and Round, Adam and Seidman, Michael and Wang, Weidong and Kisker, Caroline},
  title     = {FANCM interacts with PCNA to promote replication traverse of DNA interstrand crosslinks},
  series = {Nucleic Acids Research},
  volume    = {44},
  journal   = {Nucleic Acids Research},
  number    = {7},
  doi       = {10.1093/nar/gkw037},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-175401},
  pages     = {3219-3232},
  year      = {2016},
  abstract  = {FANCM is a highly conserved DNA remodeling enzyme that promotes the activation of the Fanconi anemia DNA repair pathway and facilitates replication traverse of DNA interstrand crosslinks. However, how FANCM interacts with the replication machinery to promote traverse remains unclear. Here, we show that FANCM and its archaeal homolog Hef from Thermoplasma acidophilum interact with proliferating cell nuclear antigen (PCNA), an essential co-factor for DNA polymerases in both replication and repair. The interaction is mediated through a conserved PIP-box; and in human FANCM, it is strongly stimulated by replication stress. A FANCM variant carrying a mutation in the PIP-box is defective in promoting replication traverse of interstrand crosslinks and is also inefficient in promoting FANCD2 monoubiquitination, a key step of the Fanconi anemia pathway. Our data reveal a conserved interaction mode between FANCM and PCNA during replication stress, and suggest that this interaction is essential for FANCM to aid replication machines to traverse DNA interstrand crosslinks prior to post-replication repair.},
  language  = {en}
}