Rif1 S-acylation mediates DNA double-strand break repair at the inner nuclear membrane

@article{Fontana2019Rif1SM,
  title={Rif1 S-acylation mediates DNA double-strand break repair at the inner nuclear membrane},
  author={Gabriele A Fontana and Daniel Hess and Julia K Reinert and Stefano Mattarocci and Beno{\^i}t Falquet and Dominique Klein and David Shore and Nicolas H. Thom{\"a} and Ulrich Rass},
  journal={Nature Communications},
  year={2019},
  volume={10}
}
Rif1 is involved in telomere homeostasis, DNA replication timing, and DNA double-strand break (DSB) repair pathway choice from yeast to human. The molecular mechanisms that enable Rif1 to fulfill its diverse roles remain to be determined. Here, we demonstrate that Rif1 is S-acylated within its conserved N-terminal domain at cysteine residues C466 and C473 by the DHHC family palmitoyl acyltransferase Pfa4. Rif1 S-acylation facilitates the accumulation of Rif1 at DSBs, the attenuation of DNA end… 

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