{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_M55_P97i_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_Gem_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_M55_UT_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_M45_P97i_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_M55_UT_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_I45_P97i_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_M45_UT_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_M55_P97i_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_I55_P97i_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_I45_P97i_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_M45_UT_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_Gem_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_I55_P97i_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_Gem_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_M45_P97i_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_M45_UT_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_I45_P97i_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_M55_UT_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_M55_P97i_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_I55_P97i_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/20230831_HF1_MaRa_SA_P0200_M45_P97i_01.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/txt.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD055299/andromeda.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["raeschle@rhrk.uni-kl.de"],"submitter":["Markus Räschle"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Replication termination genomic stabilitym itosis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD055299"],"tissue":["Cell Culture"],"sample_protocol":["Xenopus Egg Extracts and DNA Replication DNA replication and preparation of Xenopus egg extracts were as described (Knipscheer et al., 2012). For replication reactions sperm chromatin (3.3x103 sperm/l final) was incubated for 20 minutes with HSS, followed by addition of two volumes of NPE. For inhibitor studies the following reagents were added as indicated: To monitor geminin sensitivity, HSS was preincubated with geminin (0.5 M) for 10 minutes.   MS sample preparation For chromatin isolation, 12 l of the total reaction was mixed with 80 l ELB (10 mM HEPES/KOH at pH7.7, 50 mM KCl, 2.5 mM MgCl2) containing 0.2% Triton X-100 and layered over a 180 l ELB containing 500 mM sucrose in 5x44 mm microcentrifuge tubes (Beckman). Chromatin was sedimented by centrifugation (8000 rpm, 40 sec) in a swing-out rotor (Eppendorf, A-8-11). The chromatin pellet was washed twice with 200 ml ELB containing 250 mM sucrose and resuspended in 50 l denaturation buffer (8 M Urea, 100 mM Tris pH=8.0). Cysteine residues were reduced (1 mM DTT, 45 minutes at RT) and alkylated (5 mM iodoacetamide, 45 min at RT). Proteins were digested with 2.5 g LysC (Wako) for 3 hours at RT. Samples were diluted 1:4 with ABC (50 mM ammonium bicarbonate). 2.5 mg trypsin was added an incubated 16 hours at 30 °C. NaCl was added to 400 mM final concentration and peptides were acidified and purified by stage tipping on C18 material (Rappsilber et al., 2003).  LC-MS/MS analysis Peptides were separated on reversed phase columns (50 cm, 75 m inner diameter, packed in-house with ReproSil-Pur C18-AQ 1.8 m resin (Dr. Maisch GmbH) and directly injected into a quadrupol orbitrap mass spectrometer (Q Exactive HF, Thermo Scientific, Germany). Using a nanoflow HPLC (Thermo Scientific, Odensee) peptides were loaded in buffer A (0.5% acetic acid) and eluted with a four hour non-linear gradient from 5-95% buffer B (80% acetonitrile, 0.5% acetic acid) at a constant flow rate of 250 nl/min. For the reversed phase separation, the column was maintained at a constant temperature of 60 °C. The mass spectrometer was operated in a data dependent fashion using a top 15 method for peptide sequencing."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["MS Data processing Raw data were analyzed with the MaxQuant software (version 2.0.1.0) (Cox and Mann, 2008). A false discovery rate (FDR) of 0.01 for proteins and peptides and a minimum peptide length of 7 amino acids were required. MS/MS spectra were searched against a non-redundant Xenopus database (see Räschle et al, Science 2015 for details). For the Andromeda search trypsin allowing for cleavage N-terminal to proline was chosen as enzyme specificity. Cysteine carbamidomethylation was selected as a fixed modification, while protein N-terminal acetylation and methionine oxidation were selected as variable modifications. Maximally two missed cleavages were allowed. Initial mass deviation of precursor ion was up to 7 ppm, mass deviation for fragment ions was 0.5 Dalton. Protein identification required one unique peptide to the protein group. Raw intensities were normalized using the label free quantification (LFQ) algorithm implemented in MaxQuant. Match between run was enabled to transfer identities between all runs."],"omics_type":["Proteomics"],"labhead":["Markus Räschle"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Molecular Genetics"],"species":["Xenopus Laevis (african Clawed Frog)"],"publication":["10.1126/science.aeh1834","10.1126/SCIENCE.AEH1834"],"submitter_mail":["raeschle@rhrk.uni-kl.de"],"submitter_affiliation":["Technical University Kaiserslautern"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"A CDK1 phospho-switch reprograms TRAIP to unload replisomes in mitosis","description":"Cells entering mitosis with incompletely replicated DNA face catastrophic chromosome segregation failure. During interphase, the replisome-associated E3 ubiquitin ligase TRAIP ubiquitylates barriers in front of the fork to allow replisome progression. In mitosis, TRAIP is reprogrammed from a trans-acting to a cis-acting ligase that can ubiquitylate the replisome itself. This enables the processing of unreplicated DNA by promoting replisome disassembly, fork breakage, and joining of the broken chromosome arms. Here, we describe a mechanism for this reprogramming: the ATPase TTF2 is recruited to the replisome, where its noncatalytic N-terminal domain tethers Cyclin B-CDK1-phosphorylated TRAIP to the leading strand DNA polymerase ε in a geometry that allows replisome ubiquitylation. Thus, a phospho-regulated architectural switch alters replisome organization in mitosis to safeguard genome integrity before chromosome 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