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Experimental designD. melanogaster S2 cells were seeded in SFX medium (HyClone, Logan, UT, USA) at 25 °C. 5*107 cells were washed with ice-cold PBS and homogenized with a Dounce homogenizer (tight pestle, 20 strokes) in lysis buffer (20 mM Tris-HCl 7.5, 10 mM KCl, 10 mM MgCl2, 2 mM EDTA, 10% glycerol, 1% Triton X-100, 1mM DTT, 1 mM PMSF, and 1xHalt Protease Inhibitor Cocktail), incubated on ice for 10 min, and centrifuged at 3000 x g to separate the cytoplasm fraction from the nuclei. The nuclei were resuspended in the same buffer and sonicated in a Bioruptor (Diagenode, USA) for 3 min on setting L (30 sec ON/30 sec OFF). NaCl was added to a final concentration of 500 mM, and the suspension was incubated on ice for an additional 60 minutes with periodic mixing. Sonication was repeated as above to reduce viscosity. Cell debris was pelleted by centrifugation at 10,000 g for 30 min at 4°C, the supernatant was diluted to 250 mM of NaCl with incubation buffer-0 (20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, 10% glycerol, 0.1% NP-40, 0.5 mM PMSF, 2 mM Ribonucleoside Vanadyl Complex, and 1xHalt Protease Inhibitor Cocktail) and maintained for subsequent incubation with RNA-streptavidin magnetic beads. Dynabeads MyOne Streptavidin T1 magnetic beads (ThermoFisher) (20 µl per sample) were washed twice with buffer A (100 mM NaOH, 50 mM NaCl), with buffer B (100 mM NaCl), twice with buffer C (20 mM Tris-HCl pH 7.5). Beads were resuspended with RNA-binding buffer (20 mM Tris-HCl pH 7.5, 1M NaCl, 1mM EDTA). Biotinylated RNAs were heated at 90°C for 2 minutes and placed immediately on ice. Then RNA was added to Streptavidin T1 magnetic beads and incubated at room temperature for 30 minutes. RNA–streptavidin magnetic beads were washed twice with buffer C and with RNA-protein buffer (20 mM Tris-HCl pH 7.5, 50 mM NaCl, 2 mM MgCl2, 0.1% tween-20). Then 300 µl of protein extract was mixed with 150 µl of 50% glycerol and 50 µl of 10xRNA-protein buffer (200 mM Tris-HCl pH 7.5, 500 mM NaCl, 02 mM MgCl2, 1% tween-20). This mix was incubated with RNA–streptavidin magnetic beads overnight at 4°C. After 3 rounds of washing with wash buffer (10 mM Tris-HCl, pH 8.0; 150 mM NaCl, 2 M Urea), the proteins were eluted with elution buffer (10 mM Tris-HCl, pH 8.0; 8 M Urea).In-solution Trypsin DigestionProtein concentrations in biological samples after RNA affinity purification were determined Quick Start Bradford protein assay (Bio-Rad) according to the manufacturer's standard protocol (bovine serum albumin was used as the standard). Disulfide bonds of each sample were reduced with DTT (final concentration 5 mM) for 30 min at room temperature (RT). Afterwards, Iodoacetamide was added to a final concentration of 10 mM. The samples were incubated at RT for 20 min in the dark, and the reaction was stopped by adding DTT to a final concentration of 5 mM for 20 min. Then, samples was diluted with Ammonium Bicarbonate solution to reduce Urea concentration to 4 M. LysC (Promega) was added at the ratio of 1:100 w/w and the samples were incubated for 4 h at 37°C. Then, samples were diluted with Ammonium Bicarbonate solution to reduce urea concentration to 2 M and trypsin (Promega) was added at the ratio of 1:100 w/w and the samples were incubated for 14 h at 37°C. After that, the reaction was stopped by the addition of Trifluoroacetic acid (TFA) to the final concentration of 0.5%. The tryptic peptides were desalted using SDB-RPS membrane (SigmaAldrich, 66886-U) and vacuum-dried, and stored at −80°C before LC-MS/MS analysis. Prior to LC-MS/MS analysis samples were redissolved in 5% Acetonitrile (ACN) with 0.1% TFA solution and sonicated.LC-MS/MS AnalysisProteomic analysis was performed using a Q Exactive HF mass-spectrometer. Samples were loaded onto 50-cm columns packed in-house with C18 3 μM Acclaim PepMap 100 (Thermo Fisher), with an Ultimate 3000 Nano LC System (Thermo Fisher) coupled to the MS (Q Exactive HF, Thermo Fisher). Peptides were loaded onto the column thermostatically controlled at 40°C in buffer A (0.2% Formic acid) and eluted with a linear (120 min) gradient of 4 to 55% buffer B (0.1% Formic acid, 80% Acetonitrile) in A at a flow rate of 350 nl/min. Mass spectrometric data were stored during automatic switching between MS1 scans and up to 15 MS/MS scans (topN method). The target value for MS1 scanning was set to 3×106 in the range 300–1200 m/z with a maximum ion injection time of 60 ms and a resolution of 60000. The precursor ions were isolated at a window width of 1.4 m/z and a fixed first mass of 100.0 m/z. Precursor ions were fragmented by high-energy dissociation with a normalized collision energy of 28 eV. MS/MS scans were saved with a resolution of 15000 at 400 m/z and at a value of 1×105 for target ions in the range of 200-2000 m/z with a maximum ion injection time of 30 ms."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Protein identification and spectral countingRaw data files acquired on the Q Exactive HF-X were converted to Mascot generic format (mgf) peak lists using MSConvert (ProteoWizard Software Foundation) with the following parameters: “--mgf --filter peakPicking true [1,2]”. The resulting peak lists were searched against the UniProt Knowledgebase (taxon 7227 Drosophila melanogaster; downloaded 13/04/2026 with 44174 protein sequences) concatenated with a reversed decoy set using MASCOT (version 2.5.1, Matrix Science Ltd., UK) and X! Tandem (ALANINE, 2017.02.01, The Global Proteome Machine Organization). For both search engines, precursor and fragment mass tolerances were set to 20 ppm and 50 ppm, respectively. Database-searching parameters included the following: tryptic digestion with one possible missed cleavage, static modification for carbamidomethyl (C), and dynamic/flexible modifications for oxidation (M). For X! Tandem we also selected parameters that allowed a quick check for protein N-terminal residue acetylation, peptide N-terminal glutamine ammonia loss, or peptide N-terminal glutamic acid water loss. Result files were submitted to Scaffold 5 software (version 5.1.0) for validation and meta-analysis. We used the local false discovery rate scoring algorithm with standard experiment-wide protein grouping. For the evaluation of peptide and protein hits, a false discovery rate of 5% was selected for both. False positive identifications were based on reverse database analysis."],"omics_type":["Proteomics"],"labhead":["Georgij Arapidi"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Head of System Biology Lab. at Lopukhin Federal Research and Clinical Center of Physical-Chemical Medicine of Federal Medical Biological Agency"],"species":["Drosophila Melanogaster (fruit Fly)"],"publication":["Not available"],"submitter_mail":["arapidi@gmail.com"],"submitter_affiliation":["System Biology Lab. at Lopukhin Federal Research and Clinical Center of Physical-Chemical Medicine of Federal Medical Biological Agency"],"submitter_country":["Russia"],"doi":["10.6019/PXD079014"],"additional_accession":[]},"is_claimable":false,"name":"Multiple intron motifs have redundant functions in trans-splicing of the mod(mdg4) locus","description":"In contrast to canonical cis-splicing, trans-splicing combines exons from two distinct transcripts, yielding chimeric mRNAs. One striking example is the ubiquitously expressed modifier of mdg4 (mod(mdg4)) locus in Drosophila, where all mRNAs spanning over 30 isoforms are generated exclusively by trans-splicing. This process combines common constitutive exons with one of many alternative 3′ variable exons transcribed from independent promoters. Here, we demonstrate that trans-splicing is determined by an approximately 600-bp region located in the proximal part of the last common intron. Deletion analysis in a model system and directly within the endogenous mod(mdg4) locus revealed that this intronic region contains multiple redundant motifs for RNA-binding proteins (RBPs), which collectively determine the level of trans-splicing. By affinity purification of the in vitro transcribed proximal part of the intronic RNA, we identified specific binding of a large group of spliceosome-associated RBPs, some of which were found to have binding motifs in the intronic region of mod(mdg4) RNA, which is critical for trans-splicing.","dates":{"publication":"2026-05-28","submission":"2026-05-28"},"accession":"PXD079014","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:231490","NEWT:244704","NEWT:7725","NE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