{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/checksum.txt"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE5_02_10_2025_Rim11_24h.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE8_02_10_2025_Cdc7_24h.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE3_02_10_2025_Cka2_2h.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE1_02_10_2025_Rim11_2h.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE4_02_10_2025_Cdc7_2h.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE6_02_10_2025_Cdc5_24h.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE2_02_10_2025_Cdc5_2h.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE7_02_10_2025_Cka2_24h.msf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE4_02_10_2025_Cdc7_2h.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE6_02_10_2025_Cdc5_24h.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE8_02_10_2025_Cdc7_24h.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE7_02_10_2025_Cka2_24h.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE5_02_10_2025_Rim11_24h.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE1_02_10_2025_Rim11_2h.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE3_02_10_2025_Cka2_2h.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074712/SAMPLE2_02_10_2025_Cdc5_2h.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["U.W.Rass@sussex.ac.uk"],"submitter":["Rowin Appanah"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Orbitrap exploris 480","Vanquish neo uhplc","Pol32","Cka2","Ddk","Cdc5","Saccharomyces cerevisiae","Break-induced replication"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074712"],"sample_protocol":["His6-tagged Trx-Pol32-RBM (RPA-binding motif) fusions were expressed in E. coli strain BL21(DE3). Transformed bacteria were cultured in Turbo Broth (Molecular Dimensions) supplemented with 50 µg/ml carbenicillin, at a temperature of 37°C, in an orbital-shaking incubator set at 200 rpm. Recombinant protein expression was induced by the addition of 0.2 mM isopropyl β-d-1-thiogalactopyranoside once the optical density at 600 nm had reached 1.5. The temperature of the incubator was then reduced to 20°C, and the cultures grown for an additional period of ~16 hours. After this, cells were harvested by centrifugation at 4000g for 20 min at 4°C and then stored at -20°C. Cell pellets corresponding to 100 ml of cell culture were lysed by thawing on ice and sonication in buffer A (50 mM HEPES pH 7.5, 250 mM NaCl, 0.5 mM TCEP, 10 mM imidazole) supplemented with protease inhibitors (Roche). Insoluble material was removed by high-speed centrifugation at 40,000g for a period of 1 h at 4°C. The resulting supernatant was passed through a 5 micrometre filter and then applied to a batch/gravity column containing 1 ml of TALON resin (TaKaRa Bio). The resin was washed with 5 column volumes of buffer A to remove unbound material, before the addition of buffer B to elute the retained protein (50 mM HEPES pH 7.5, 250 mM NaCl, 0.5 mM TCEP, 300 mM imidazole). Fractions containing the Trx-Pol32-RBM fusion proteins were identified by SDS-PAGE, pooled, and then applied to a Superdex S75 16 600 size exclusion chromatography column (Cytiva) pre-equilibrated in buffer C (20 mM HEPES pH 7.5, 250 mM NaCl, 0.5 mM TCEP). Fractions containing the recombinant protein were again confirmed by SDS-PAGE, pooled and then concentrated to ~2.5 mg/ml by use of centrifugal concentrators with a 5 kDa molecular weight cut-off (Sartorius). The purified protein was flash-frozen in aliquots and stored at -80°C until required. Yeast cell cultures of cells coding for TAP-tagged kinases were harvested at 4°C and washed sequentially with an ice-cold solution of 20 mM HEPES-KOH (pH 7.9) and a wash buffer containing 100 mM HEPES-KOH (pH 7.9), 300 mM potassium acetate, 10 mM magnesium acetate and 2 mM EDTA. Cells were centrifuged and resuspended in the same wash buffer supplemented with 2 mM sodium glycerophosphate (Johnson Matthey), 2 mM sodium fluoride (Fisher Scientific), 1 mM DTT, 1% (v/v) protease inhibitor cocktail for fungal and yeast extracts (Sigma), and 0.24% (w/v) EDTA-free complete protease inhibitor cocktail (Roche). The mixture was flash frozen in liquid nitrogen and protein immunoprecipitation was carried out. In brief, cells were lysed using a mechanical pestle and mortar (Cole-Parmer SPEX Sample Prep 6850) pre-cooled at -80°C. To each gram of thawed lysate, 0.25 ml of a solution of 50% (v/v) glycerol, 100 mM HEPES-KOH (pH 7.9), 300 mM potassium acetate, 20 mM magnesium acetate, 0.5% Igepal CA-630, 2 mM EDTA supplemented with 2 mM sodium glycerophosphate, 2 mM sodium fluoride, 1 mM DTT, 1% (v/v) protease inhibitor cocktail for fungal and yeast extracts (Sigma), and 0.24% (w/v) EDTA-free complete protease inhibitor cocktail was added. Pierce universal nuclease was added to a final concentration of 1.6 U/microlitre, and samples were agitated on a rotating platform at 4°C for 40 min. Lysates were then clarified by successive centrifugations at 4,000g and 13,000g. The remaining supernatant was incubated with 100 microlitre TAP-beads (M270 Dynabeads epoxy beads coupled with anti-sheep IgG) at 4°C for 2 h. The beads were then washed three times with 100 mM HEPES-KOH (pH 7.9), 300 mM potassium acetate, 20 mM magnesium acetate, 2 mM EDTA, 0.1% (v/v) Igepal CA-630. The first wash was supplemented with 2 mM sodium glycerophosphate, 2 mM sodium fluoride, 1 mM DTT, 1% (v/v) protease inhibitor cocktail for fungal and yeast extracts (Sigma), and 0.24% (w/v) EDTA-free complete protease inhibitor cocktail (Roche). TAP beads (containing TAP-tagged kinases) were then washed twice with 20 mM Hepes-KOH (pH 7.9), 150 mM NaCl. the TAP beads were mixed with 75 micromolar of peptide substrate (Trx-Pol32-RBM) and 2.5 mM of cold ATP in a buffer of 20 mM Hepes-KOH (pH 7.9), 150 mM NaCl, 10 mM MgCl2, 1 x PhosSTOP (Merck) and 0.5 mM TCEP, before incubation in a 30°C water bath. After 2 or 24 h, the supernatant containing the phosphorylation substrate was immediately frozen at -20°C. After thawing, the samples were reduced with 5 mM TCEP for 1.5 h and alkylated with 10 mM iodoacetamide in the absence of light. Alkylation was then quenched by addition of 5 mM DTT. The samples were desalted using PD SpinTrao G-25 columns (GE Healthcare) and digested with 2 microgram of Trypsin Gold (Promega) at 37°C. After desalting using C18 tip-columns samples were concentrated using a vacuum-concentrator. Finally, the samples were reconstituted in 40 microlitre of a solution of 0.5% acetonitrile and 1% formic acid. Optionally, phospho-peptides were enriched using titanium dioxide columns."],"repository":["pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["After in vitro phosphorylation, the Trx-Pol32-RBM proteins were appropriately reduced, alkylated and tryptic digested. These samples were analysed by mass spectrometric analysis. In total, 8 samples (including controls) were analysed (n=1). Two independent controls were used: Trx-Pol32-RBM incubated with the Rim11-TAP kinase for either 2 or 24 h. Six test samples were used: Trx-Pol32-RBM incubated for either 2 or 24 h with either Cdc5-TAP, Cka2-TAP, Cdc7-TAP. LC-MS/MS analysis was undertaken using a Vanquish Neo UHPLC coupled to an Orbitrap Exploris 480 equipped with FAIMS Pro Duo interface (Thermo Fisher Scientific), following a data-dependent MS2 experiment with internal EasyIC (RunStart) as lock mass. In summary, samples were loaded onto a PepMap Neo column (5 micron C18, 300 m x 5 mm, 100 angstrom pore size; Thermo Fisher Scientific) at a flow rate of 20 microlitre/min using 0.1% formic acid in H2O and separated on an analytical EASY-Spray PepMap Neo column (2 micrometre C18, 75 micrometre x 500 mm, 100  angstrom pore size, Thermo Fisher Scientific) with a flow rate of 350 nl/min with a linear gradient of 1 to 35% solvent B (80% (v/v) acetonitrile, 0.1% (v/v) formic acid) over 60 min. Ion source conditions were maintained at 1.75 kV positive voltage, 275°C ion transfer tube temperature and standard resolution with 3.8 l/min FAIMS carrier gas flow throughout the acquisition. Mass spectrometric data was acquired using the following configuration: MS1Orbitrap resolution was set at 60,000 (m/z 200) from a mass range of 375 to 1200 amu using a normalized automatic gain control (AGC) target of 300% and maximum injection time (maxIT) set to auto; MS2 Orbitrap resolution was set at 15,000 (m/z 200) with first acquired mass starting at 120 amu, an isolation window of 2 amu, and AGC set to standard with 40 msec maxIT. Fragmentation was carried out using higher-energy collisional dissociation (HCD) with a normalized collision energy (NCE) of 30. For the FAIMS, two compensation voltages (CV), 45 and 65 V with 2 and 1 sec cycle time, respectively, for each CV were used with a RF lens of 50%. The following mass filters were also used: MIPS (peptide mode), intensity threshold (8.0E3), charge state (2-6) and dynamic exclusion (30 sec) mass filters were used. Data was analysed using Proteome Discoverer 3.0 (Thermo Fisher Scientific) with Sequest HT and MS Amada 2.0 as the search engines. An in-house modified peptide sequences FASTA file (based on our Pol32 RBM construct) was used to search against. For both Sequest HT and Amada engine precursor and fragment mass limits were fixed at 5 ppm and 0.02 Da. Only the phosphorylation for serine, threonine, and tyrosine residues was set as dynamic modifications. The protein FDR and the peptide spectrum match were both set to 0.01."],"omics_type":["Proteomics"],"labhead":["Ulrich Rass"],"instrument_platform":[""],"labhead_affiliation":["Professor of Genome Stability, Genome Damage and Stability, School of Life Sciences, University of Sussex. Brighton. BN1 9RH."],"submission_type":["PARTIAL"],"species":["Escherichia Coli","Saccharomyces Cerevisiae (baker's Yeast)"],"submitter_mail":["rappanah@live.com"],"publication":["41951601 Jones D, Appanah R, Yates LA, Oliver AW, Rass U. Break-induced replication is enhanced by a phospho-activated RPA-binding module in Pol32. Nat Commun. 2026 17(1):5006 10.1038/s41467-026-71309-y"],"submitter_affiliation":["1.University of Sussex\n2.LBMC-ENS de Lyon"],"submitter_country":["United Kingdom"],"pubmed_abstract":["Break-induced replication (BIR) facilitates single-ended DNA double-strand break (DSB) repair. Upon homologous recombination-mediated strand invasion into a homologous repair template, BIR is catalysed by a minimal replisome comprising PCNA, DNA polymerase δ (Pol δ), and the Pif1 helicase. Here, we identify an interaction between Pol δ and single-stranded DNA (ssDNA)-binding protein RPA mediated by an RPA-binding module (RBM) within Pol δ subunit Pol32 and RPA subunit Rfa1. Pol32 RBM phosphorylation at Thr256 and Thr257 increases its affinity for Rfa1, while corresponding phospho-mimetic amino-acid substitutions promote BIR efficiency in vivo. This suggests that Pol32 functions as a rheostat whose phosphorylation enhances Pol δ's affinity for RPA-bound BIR intermediates, thereby boosting BIR efficiency. Modelling indicates that Pol32 phospho-RBM-Rfa1 interactions mirror the binding mode of RBMs in Pif1 and the FANCM helicase and BIR antagonist Mph1. This implies a key role for RPA in the dynamic orchestration of the enzymes mediating BIR."],"pubmed_title":["Break-induced replication is enhanced by a phospho-activated RPA-binding module in Pol32."],"pubmed_authors":["Jones David D, Appanah Rowin R, Yates Luke A LA, Oliver Antony W AW, Rass Ulrich U"],"additional_accession":[]},"is_claimable":false,"name":"Break-induced replication is enhanced by a phospho-activated RPA-binding module in Pol32","description":"Break-induced replication (BIR) mediates single-ended DNA double-strand break (DSB) repair. Upon strand invasion into a homologous repair template, BIR is catalysed by a minimal replisome comprising PCNA, DNA polymerase delta, and the Pif1 helicase. Here, we identify an interaction between Polymerase delta and single-stranded DNA (ssDNA)-binding protein RPA mediated by an RPA-binding module (RBM) within the Polymerase delta subunit Pol32 and RPA subunit Rfa1. Pol32 RBM phosphorylation at Thr256 and Thr257 increases its affinity for Rfa1, while corresponding phospho-mimetic amino-acid substitutions promote BIR efficiency in vivo. This suggests that Pol32 functions as a rheostat whose phosphorylation enhances the affinity of Polymerase delta for RPA-bound BIR intermediates, thereby boosting BIR efficiency. Modelling indicates that Pol32 phospho-RBM-Rfa1 interactions mirror the binding mode of a previously identified Pif1 RBM, and an RBM we identify in the BIR antagonist Mph1. This implies a key role for RPA in the dynamic orchestration of the enzymes mediating BIR.","dates":{"publication":"2026-06-15","submission":"2026-02-21"},"accession":"PXD074712","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:35231","NEWT:1774208","NEWT:8644","NEWT:1125630","NEWT:28930","NEWT:202914","NEWT:27602","NEWT:502779","NEWT:297246","NEWT:483139","NEWT:101491","NEWT:8639","NEWT:8637","NEWT:1114970","NEWT:285272","NEWT:192222","NEWT:9963","N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