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DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2019-04-15
  • AnnouncementXML: Submission_2019-06-14_00:30:08.xml
  • DigitalObjectIdentifier:
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Unsupported dataset by repository
  • PrimarySubmitter: Daniel Hess
  • Title: Rif1 S-acylation mediates DNA double-strand break repair at the inner nuclear membrane
  • Description: 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-resection, and DSB repair by non-homologous end-joining (NHEJ). These findings identify S-acylation as a posttranslational modification regulating DNA repair. S-acylated Rif1 mounts a localized DNA-damage response proximal to the inner nuclear membrane, revealing a mechanism of compartmentalized DSB repair pathway choice by sequestration of a fatty acylated repair factor at the inner nuclear membrane.
  • SpeciesList: scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
  • ModificationList: palmitoylated residue
  • Instrument: Orbitrap Fusion

Dataset History

VersionDatetimeStatusChangeLog Entry
02018-12-20 07:43:32ID requested
12019-04-15 06:34:47announced
22019-06-14 00:30:09announcedUpdated publication reference for PubMed record(s): 31182712.

Publication List

  1. Fontana GA, Hess D, Reinert JK, Mattarocci S, Falquet B, Klein D, Shore D, Thomä NH, Rass U, Rif1 S-acylation mediates DNA double-strand break repair at the inner nuclear membrane. Nat Commun, 10(1):2535(2019) [pubmed]

Keyword List

  1. curator keyword: Biological
  2. submitter keyword: yeast, DNA double-strand break repair, Rif1 S-acylation,non-homologous end-joining, palmitoylation

Contact List

    Ulrich Rass
    • contact affiliation: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton, BN1 9RQ, United Kingdom
    • contact email: u.w.rass@sussex.ac.uk
    • lab head:
    Daniel Hess
    • contact affiliation: Friedrich Miescher Institute for Biomedical Research
    • contact email: dhess@fmi.ch
    • dataset submitter:

Full Dataset Link List

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