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CHEVREUX"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Smc","Programmed dna elimination","Transposable element","Endonuclease","Condensin","Ciliate"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD068119"],"tissue":["Ciliated Cell"],"sample_protocol":["LC MS/MS of PGM and PGML4a proximity labelling (2114003) Gel plugs were destained in a solution of ACN/NH4HCO3 50mM (50/50) for 15 minutes with agitation. Plugs were reduced in 10 mM DTT for 45 min at 56°C, then alkylated in 55 mM IAA for 45 min at room temperature. After a wash and dehydration step, proteins in the plugs were trypsinized overnight at 37°C in a 25 mM NH4HCO3 buffer (0.2 µg high sequencing grade trypsin from Promega in 20 µL buffer). The resulting peptides were desalted using C18 ZipTip (Pierce Biotechnology) prior to injection. Peptides were analyzed using a Q-Exactive Plus coupled to a Nano-LC Proxeon 1000, both from ThermoFisher Scientific (Waltham, MA, USA). Peptides were separated by chromatography with the following settings: Acclaim PepMap100 C18 pre-column (0.075 x 20 mm, 3 μm, 100 Å), Pepmap-RSLC Proxeon C18 column (0.075 x 500 mm, 2 μm, 100 Å), 300 nl/min flow rate, a 98-min gradient from 95% solvent A (H2O/0.1% FA) to 35 % solvent B (100 % ACN/0.1% FA) followed by column regeneration, giving a total time of 120 minutes. Peptides were analyzed in the Orbitrap cell in positive mode, at a resolution of 70,000, with a mass range of m/z 375-1500 and an AGC target of 3.106. MS/MS data were acquired in the Orbitrap cell in a Top20 mode. Peptides were selected for fragmentation by Higher-energy C-trap Dissociation (HCD) with a Normalized Collisional Energy of 27%, a dynamic exclusion of 60 seconds, and a quadrupole isolation window of 1.4 Da and an AGC target of 2.105. Peptides with unassigned charge states or monocharged peptides were excluded from the MS/MS acquisition. The maximum ion accumulation times were set to 50 ms for MS acquisition and 45 ms for MS/MS acquisition.  LC MS/MS of protein immunoprecipitates  Beads from pulldown experiments were incubated overnight at 37°C with 40 μL of 50 mM NH4HCO3 (Sigma-Aldrich) buffer containing 1 µg of sequencing-grade trypsin/Lys C mix (Promega). The digested peptides were loaded and desalted on evotips (Evosep, Odense, Denmark) according to the manufacturer’s procedure before LC-MS/MS analysis. Samples were analyzed on a timsTOF Pro 2 mass spectrometer (Bruker Daltonics, Bremen, Germany) coupled to an Evosep one system (Evosep, Odense, Denmark) operating with the 30SPD method developed by the manufacturer. Briefly, the method is based on a 44-min gradient and a total cycle time of 48 min with a C18 analytical column (0.15 x 150 mm, 1.9 µm beads, ref EV-1106) equilibrated at 40°C and operated at a flow rate of 500 nL/min. H2O/0.1 % FA was used as solvent A and ACN/ 0.1 % FA as solvent B. For the tandem affinity purification of CapD2.3 (2351001), the timsTOF Pro 2 was operated with a DIA-PASEF method comprising 12 pydiAID frames with 3 mass windows per frame resulting in a cycle time of 0.975 seconds, as described in Bruker application note LCMS 218. For the FLAG affinity purification (2337008), The timsTOF Pro 2 was operated in DDA-PASEF mode over a 1.3 sec cycle time at 60 Hz MS/MS scanning rate. Mass spectra for MS and MS/MS scans were recorded between 100 and 1700 m/z."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MS raw files (2114003) were processed using PEAKS Online X (build 1.6, Bioinformatics Solutions Inc.). The data was searched against the Paramecium tetraurelia protein database (last modified in 2017) available from ParameciumDB (https://paramecium.i2bc.paris-saclay.fr/download/Paramecium/tetraurelia/51), consisting of 40,460 entries and further modified with the addition of 6 sequences corresponding to the two bait constructs, the birA and TurboID biotin ligases, streptavidin and the FLAG peptide. Parent mass tolerance was set to 5 ppm and fragment mass tolerance to 0.05 Da. Specific tryptic cleavage was selected and a maximum of 2 missed cleavages was authorized. For identification, the following post-translational modifications were included: oxidation (M), deamidation (NQ) as variables and carbamidomethylation (C) as fixed. The maximum number of variable modifications per peptide was limited to 2. Peptide identifications were filtered based on a 1% FDR (False Discovery Rate) threshold at PSM level. Match between runs was performed with a mass error tolerance of 5 ppm, a retention time shift tolerance of 1 min and a feature intensity threshold of 100. A normalization between runs was applied based on the Total Ion Current (TIC) and protein abundance was finally inferred using a Top N label free quantification approach. Multivariate statistics on protein measurements and graphical results were generated using Qlucore Omics Explorer 3.8.9 (Qlucore AB, Lund, SWEDEN). A positive threshold value of 1 was specified to enable a log2 transformation of abundance data for normalization i.e. all abundance data values below the threshold were replaced by 1 before transformation. The transformed data were finally used for statistical comparison of groups using a Student’s bilateral t-test. Protein identification was performed for all samples together and led to the identification of 1471 protein groups (see TbID-MS table in Zenodo). Of note, two samples (Pgm-1 and CTL-8, see TbID-MS table in Zenodo) were considered as outliers because of their very low material abundance and final protein content identification, and were finally excluded from the statistical analysis.For the tandem affinity purification of CapD2.3-FLAG-HA (2351001), MS raw files were processed using Spectronaut 18 (Biognosys, Switzerland). Data were searched against the same Paramecium protein database as above, combined with the SwissProt Mus musculus database (12-2023, 17799 entries). Contaminating proteins originating from the anti-FLAG antibody-coupled beads used for IP and identified only in the Mus musculus taxonomy were excluded from the final protein list. Specific tryptic cleavages were selected and a maximum of 2 missed cleavages were allowed. The following post-translational modifications were considered for identification: Acetyl (Protein N-term) and Oxidation (M) as variable and Cys-Cys (C) as fixed. The maximum number of variable modifications was set to 5. Identifications were filtered based on a 1% precursor and protein Qvalue cutoff threshold. The protein LFQ method was set to automatic and the quantity was set at the MS2 level with a cross-run normalization applied. Multivariate statistics on protein measurements were performed as described above, using Qlucore Omics Explorer 3.9 (Qlucore AB, Lund, SWEDEN). For the affinity purification of CapD2.3 (2337008), MS raw files were processed using PEAKS Online 11 (build 1.9, Bioinformatics Solutions Inc.). Data were searched against the same Paramecium protein database as above, with PTET.51.1.P0430205 sequence modified to include the HA tag of the bait. Parent mass tolerance was set to 20 ppm, with fragment mass tolerance of 0.05 Da. Semi-specific tryptic cleavages was selected and a maximum of 1 missed cleavage was allowed. The following post-translational modifications were considered for identification: Oxidation (M), Deamidation (NQ) and Acetylation (Protein N-term) as variable and Half of a disulfide bridge (C) as fixed. Identifications were filtered to a <1% FDR (False Discovery Rate) threshold at both peptide and protein group levels. Label free quantification was performed using the PEAKS Online 11 quantification module, allowing a mass tolerance of 5 ppm, a CCS error tolerance of 0.01 and a 0.5-min retention time shift tolerance for match between runs. Protein abundance was inferred using the top N peptide method and TIC was used for normalization. Multivariate statistics, data normalization and differential statistical analysis were performed as described for the tandem affinity purification experiment."],"omics_type":["Proteomics"],"labhead":["Mireille Betermier"],"instrument_platform":[""],"labhead_affiliation":["Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198, Gif-sur-Yvette, France"],"submission_type":["PARTIAL"],"species":["Paramecium Tetraurelia"],"publication":["Not available"],"submitter_mail":["guillaume.chevreux@ijm.fr"],"submitter_affiliation":["Institut Jacques Monod, CNRS UMR7592"],"submitter_country":["France"],"additional_accession":[]},"is_claimable":false,"name":"A developmental condensin I complex assists the Paramecium PiggyMac domesticated transposase during programmed DNA elimination","description":"Prokaryotes and eukaryotes use diverse strategies to cope with invading mobile genetic elements, including programmed DNA elimination (PDE). In the ciliate Paramecium, elimination of transposable elements and their relics requires the PiggyMac (Pgm) endonuclease and its five PgmL partners, yet how this machinery is targeted to cleavage sites remains unclear. Here, we identified condensin I subunits in the proximity proteomes of Pgm and PgmL4. We show that they belong to a condensin complex that is essential for PDE and localizes to developing somatic nuclei. Depleting the development-specific subunits of this complex blocks DNA elimination, phenocopying a Pgm depletion. Developmental condensin is required for the correct nuclear localization of Pgm and some of the PgmLs. Moreover, Pgm and these PgmLs co-immunoprecipitate with condensin I. Our findings uncover functional and physical interactions between a eukaryotic DNA cleavage machinery and a specialized condensin complex that is critical for PDE in a non-dividing nucleus.","dates":{"publication":"2026-04-01","submission":"2025-09-05"},"accession":"PXD068119","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:93217","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:3134131","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:1410384","NEWT:1310173","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:135666","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:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:319224","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:387344","NEWT:657318","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:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2423","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:85698","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:34839","NEWT:476","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:1431340","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:377142","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","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:536","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:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:300641","NEWT:39655","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:37003","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:9938","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:483179","NEWT:315750","NEWT:99490","NEWT:632957","NEWT:265619","NEWT:11294","NEWT:754466","NE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