{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077306/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077306/SPAC6F6-19_P3_CH_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077306/SPAC6F6-19_P2_T_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077306/SPAC6F6-19_P1_T_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077306/SPAC6F6-19_P1_T_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077306/SPAC6F6-19_P3_G_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077306/SPAC6F6-19_P2_T_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077306/SPAC6F6-19_P3_CH_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077306/SPAC6F6-19_P3_G_02.raw"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077306/mzTab.mzTab"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077306/APL_files.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["peter.barath@savba.sk"],"submitter":["Peter Barath"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["sap34","pre-mrna splicing","G-patch protein; sap34; spac6f6.19; splicing factor; pre-mrna splicing; fission yeast","spac6f6.19","fission yeast","G-patch protein","splicing factor"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077306"],"sample_protocol":["The samples were reduced with 5 mM DTT, then alkylated with 15 mM iodoacetamide, and the reaction was quenched with an additional 5 mM DTT. Parallel digestions with trypsin, GluC, and chymotrypsin were performed overnight (16 h) in the presence of phosphatase inhibitors at 37 °C, 37 °C, and 25 °C, respectively. Digestions were further processed and measured separately. Peptides were purified by microtip C18 SPE. The separation of peptides was performed by nano-HPLC Dionex UltiMate 3000 RSLCnano system (Thermo Fisher Scientific). The samples were loaded onto a trap column (PepMap100 C18, 300 μm × 5 mm, 5-μm particle size; Thermo Fisher Scientific) and separated by an EASY-Spray C18 analytical column with integrated nanospray emitter (PepMap RLSC C18, 75 μm × 500 mm, 2-μm particle size, Thermo Fisher Scientific) using a 60-min gradient (3–43% B) at a flow rate of 250 nL/min. The two mobile phases used were: 0.1% formic acid (v/v) and 80% acetonitrile (v/v) with 0.1% formic acid. Eluted peptides were sprayed directly into the Orbitrap Elite mass spectrometer (ThermoFisher Scientific). The emitter potential was set to 2.3 kV, the transfer capillary temperature to 250 °C, and the S-lens RF level to 60%. Spectral datasets were collected in a data-dependent mode using the Top15 strategy to select precursor ions for fragmentation [48]. Precursors were measured in the mass range 300–1,700 m/z with a resolution of 120,000, and fragmented by the HCD mechanism with a normalized collision energy of 25. MS/MS scans were acquired at a resolution of 15,000. Each sample was measured in technical duplicates."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The resulting datasets were processed together using MaxQuant version 1.6.17.0 with the built-in Andromeda search engine [49]. The searched database consisted of S. pombe proteomes (UniProt, downloaded 24.1.2025, isoforms included and PomBase, downloaded 23.1.2025) and a predicted N-terminally extended Sap34 amino acid sequence (with TAP tag) based on the newly defined sequence of the sap34 allele. The cleavage specificities of proteases were set as follows: trypsin – C-terminal of R and K also if P follows; GluC – C-terminal of E and D; chymotrypsin – C-terminal of F, Y, L, W, and M. The number of tolerated missed cleavages was 2 for trypsin, 4 for GluC, and 3 for chymotrypsin. Carbamidomethylation (C) was set as a permanent modification, and oxidation (M), acetylation (protein N-terminus), and phosphorylation (STY) were set as variable modifications. The precursor ion mass tolerance was set to 20 ppm in the first search and to 4.5 ppm in the main search upon recalibration, and the fragment tolerance was 20 ppm. The target-decoy database strategy was used to control for false identifications, and the false discovery rate of 1% was imposed at both the peptide-spectrum-match and protein group levels."],"omics_type":["Proteomics"],"labhead":["Peter Barath"],"instrument_platform":[""],"labhead_affiliation":["Institute of Chemistry, SAS"],"submission_type":["COMPLETE"],"species":["Schizosaccharomyces Pombe 927"],"publication":["Not available"],"submitter_mail":["peter.barath@savba.sk"],"submitter_affiliation":["Institute of Chemistry, Slovak Academy of Sciences"],"submitter_country":["Slovakia"],"doi":["10.6019/PXD077306"],"additional_accession":[]},"is_claimable":false,"name":"GPATCH11 ortholog Sap34 regulates pre-mRNA splicing by interacting with early spliceosomal complexes in Schizosaccharomyces pombe","description":"Pre-mRNA splicing is an essential step in gene expression regulation. It is mediated by the spliceosome, a large ribonucleoprotein complex that undergoes dynamic structural and compositional rearrangements during each splicing cycle. Although the mechanisms of splicing and the roles of main spliceosomal components are well defined, the identities and functions of transiently associated spliceosomal proteins remain incompletely understood. Here, we investigated the molecular function of the poorly characterized G-patch domain–containing protein SPAC6F6.19 (herein Sap34, for spliceosome-associated protein of 34 kDa) in Schizosaccharomyces pombe, an ortholog of human GPATCH11. Using affinity purification and a yeast two-hybrid assay, we analyzed its interactome and identified its interaction partners. In addition, long-read sequencing was employed to assess Sap34-dependent changes in splicing efficiency. We found that Sap34 forms a complex with components of the U2 small nuclear ribonucleoprotein (snRNP) and the U4/U6 × U5 tri-snRNP, which are required for early spliceosome assembly and activation. Furthermore, we defined the interaction specificity of Sap34 with other splicing proteins, demonstrating the importance of its C-terminal region for binding to Sap61 and Ini1, and of its G-patch domain for interaction with the ATP-dependent RNA helicase Prp43. Notably, we showed that deletion of sap34 leads to a global reduction in splicing efficiency, predominantly associated with increased intron retention. Together, these findings identify Sap34 as a previously unrecognized and important G-patch domain–containing protein regulating the early steps of pre-mRNA splicing in fission 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