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PXD012137 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleRif1 S-acylation mediates DNA double-strand break repair at the inner nuclear membrane
DescriptionRif1 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.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterDaniel Hess
SpeciesList scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationListpalmitoylated residue
InstrumentOrbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog 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
Fontana GA, Hess D, Reinert JK, Mattarocci S, Falquet B, Klein D, Shore D, Thom, รค 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
curator keyword: Biological
submitter keyword: yeast, DNA double-strand break repair, Rif1 S-acylation,non-homologous end-joining, palmitoylation
Contact List
Ulrich Rass
contact affiliationGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton, BN1 9RQ, United Kingdom
contact emailu.w.rass@sussex.ac.uk
lab head
Daniel Hess
contact affiliationFriedrich Miescher Institute for Biomedical Research
contact emaildhess@fmi.ch
dataset submitter
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Dataset FTP location
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