Proteomics

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The Aspartic Protease Ddi1 Contributes to DNA-Protein Crosslink Repair in Yeast


ABSTRACT: Naturally occurring and drug-induced DNA-protein crosslinks (DPCs) interfere with key DNA transactions if not timely repaired. The unique family of DPC-specific proteases Wss1/SPRTN targets DPC protein moieties for degradation, including topoisomerase-1 trapped in covalent crosslinks (Top1ccs). Here we describe that the efficient DPC disassembly requires Ddi1, another conserved predicted protease in Saccharomyces cerevisiae. We found Ddi1 in a genetic screen of the tdp1wss1 mutant defective in Top1cc processing. Ddi1 is recruited to a persistent Top1cc-like DPC lesion in an S-phase dependent manner to assist eviction of crosslinked protein from DNA. Loss of Ddi1 or its putative protease activity hypersensitize cells to DPC trapping agents independently from Wss1 and 26S proteasome, implying its broader role in DPC repair. Among potential Ddi1 targets we found the core component of RNAP II and show that its genotoxin-induced degradation is impaired in ddi1. Together, we propose that the Ddi1 protease contributes to DPC proteolysis. Yeast strains with WSS1 and DDI1 deletions were compared when either complemented with DDI1-WT or ddi1-D220A after hydroxyurea treatment by SILAC MS.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Michael Plank  

LAB HEAD: Robbie Loewith

PROVIDER: PXD016376 | Pride | 2019-11-22

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20180404_SwissProt_Scere_iRT11_MSphosphoMix1_mod.fasta Fasta
20180829_13_3LH_05ul.raw Raw
20180829_16_2HL_05ul.raw Raw
20180829_19_1LH_05ul.raw Raw
20180829_22_1LH_05ul.raw Raw
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