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Stumpe"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["proximity labelling","bcl1","ribosomal protein","dedicated chaperone","nuclear import","yeast","proxiome.","Acl1; bcl1; ul1; dedicated chaperone; ribosomal protein; ribosome biogenesis; nuclear import; importin; karyopherin; yeast; turboid; proximity labelling; proxiome.","karyopherin","turboid","Acl1","importin","ul1","ribosome biogenesis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070550"],"sample_protocol":["Plasmids expressing C-terminally or N-terminally TurboID-tagged ribosomal proteins, dedicated chaperones, Acl1 (Ycr051w), or Bcl1 (Ynl035c) and the yEGFP-TurboID, the SV40NLS-yEGFP-TurboID, the TurboID-yEGFP or the SV40NLS-TurboID-yEGFP control proteins under the control of the copper-inducible CUP1 promoter were transformed into a wild-type yeast strain (YDK11-5A) (Kressler et al. Mol Cell Biol. 1999, PMID: 10567587, DOI: 10.1128/MCB.19.12.8633, . The TurboID-based proximity-labelling experiment, sample processing, and data acquisition by mass spectrometry were carried out as previously described (Steiner et al. Biomolecules 2023; PMID: 37509163; DOI: 10.3390/biom13071127)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["LC-MS/MS measurements were performed on a Q Exactive HF-X (Thermo Scientific) coupled to an EASY-nLC 1200 nanoflow-HPLC (Thermo Scientific). HPLC-column tips (fused silica) with 75 µm inner diameter were self-packed with ReproSil-Pur 120 C18-AQ, 1.9 ?m particle size (Dr. Maisch GmbH) to a length of 20 cm. Samples were directly applied onto the column without a pre-column. A gradient of A (0.1% formic acid in H2O) and B (0.1% formic acid in 80% acetonitrile in H2O) with increasing organic proportion was used for peptide separation (loading of sample with 0% B; separation ramp: from 5-30% B within 85 min). The flow rate for sample application was 600 nL/min and for sample separation 250 nL/min. The mass spectrometer was operated in the data-dependent mode and switched automatically between MS (max. of 1 x 106 ions) and MS/MS. Each MS scan was followed by a maximum of ten MS/MS scans using a normalized collision energy of 25% and a target value of 1000. Parent ions with a charge state form z = 1 and unassigned charge states were excluded for fragmentation. The mass range for MS was m/z = 370-1750. The resolution for MS was set to 70,000 and for MS/MS to 17,500. MS parameters were as follows: spray voltage 2.3 kV, no sheath and auxiliary gas flow, ion-transfer tube temperature 250°C.    The MS raw data files were analysed with the MaxQuant software package version 1.6.2.10 (Tyanova et al. Nat Protoc. 2016, PMID: 27809316, DOI: 10.1038/nprot.2016.136) for peak detection, generation of peak lists of mass-error-corrected peptides, and database searches. The UniProt Saccharomyces cerevisiae database (version March 2016), additionally including common contaminants, trypsin, TurboID, and GFP, was used as reference. Carbamidomethylcysteine was set as fixed modification and protein amino-terminal acetylation, oxidation of methionine, and biotin were set as variable modifications. Four missed cleavages were allowed, enzyme specificity was Trypsin/P, and the MS/MS tolerance was set to 20 ppm. Peptide lists were further used by MaxQuant to identify and relatively quantify proteins using the following parameters: peptide and protein false discovery rates, based on a forward-reverse database, were set to 0.01, minimum peptide length was set to seven, and minimum number of unique peptides for identification and quantification of proteins was set to one. The ‘match-between-run’ option (0.7 min) was used.    For quantification, missing iBAQ (intensity-based absolute quantification) values in the two control purifications from cells expressing either the GFP-TurboID or the NLS-GFP-TurboID (controls for C-terminally TurboID-tagged bait proteins) or the TurboID-GFP or the NLS-TurboID-GFP (controls for N-terminally TurboID-tagged bait proteins) were imputed in Perseus (Tyanova et al. Nat Methods. 2016, PMID: 27348712, DOI: 10.1038/nmeth.3901). For normalization of intensities in each independent purification, iBAQ values were divided by the median iBAQ value, derived from all nonzero values, of the respective purification. To calculate the enrichment of a given protein compared to its average abundance in the two control purifications, the normalized iBAQ values were log2-transformed and those of the control purifications were subtracted from the ones of each respective bait purification. In the case of the TurboID series with the DC baits, the enrichment of a given protein was calculated compared to its median abundance in the two control purifications and the remaining DC purifications, except for the Acl1 and Bcl1 TurboID assays where these two were reciprocally excluded. For graphical presentation, the normalized iBAQ value (log10 scale) of each protein detected in a bait purification was plotted against its relative abundance (log2-transformed enrichment compared to the control purifications). For the bar graph representation, the log2-transformed enrichment of a given protein in the indicated TurboID assays is represented by bars, while its median normalized log2-transformed enrichment across the different TurboID assays is shown as a dotted line."],"omics_type":["Proteomics"],"labhead":["Dieter Kressler"],"instrument_platform":[""],"labhead_affiliation":["Department of Biology, University of Fribourg, 1700 Fribourg, Switzerland"],"submission_type":["PARTIAL"],"species":["Saccharomyces Cerevisiae (baker's Yeast)"],"submitter_mail":["michael.stumpe@unifr.ch"],"publication":["10.1093/NAR/GKAG264"],"submitter_affiliation":["Department of Biology,\nUniversity of Fribourg"],"submitter_country":["Switzerland"],"additional_accession":[]},"is_claimable":false,"name":"Exploration of the proxiOME of large subunit ribosomal proteins reveals Acl1 and Bcl1 as cooperating dedicated chaperones of Rpl1","description":"In eukaryotes, most newly synthesized ribosomal proteins (r-proteins) need to rapidly and safely get into the nucleus to reach their assembly site on pre-ribosomal particles. However, only for few r-proteins tailored support mechanisms involving so-called dedicated chaperones could so far be revealed. Here, with the primary aim of identifying novel dedicated chaperones, we performed TurboID-based proximity labelling with all 46 large subunit r-proteins of Saccharomyces cerevisiae, which unveiled the fungi-specific Acl1 and the conserved Bcl1 as candidate dedicated chaperones of Rpl1. We show that the functionally cooperating Acl1 and Bcl1 both directly interact with Rpl1, form a trimeric Acl1-Rpl1-Bcl1 complex, and enable the nuclear import of Rpl1. Moreover, our crystal structure of the minimal Acl1-Rpl1 complex reveals how Acl1’s ankyrin repeat domain shields a positively charged rRNA-binding surface of Rpl1. Our proximity labelling approach also permitted to establish novel interactions between four r-proteins and distinct importins and to illuminate r-protein neighbourhoods on successive pre-60S particles. Additionally, reciprocal proximity labelling with the known dedicated chaperones indicates that almost all appear to be transiently associated with pre-ribosomal particles. Our study provides for the first time comprehensive insight into the physical proximities of large subunit r-proteins along their entire life cycle.","dates":{"publication":"2026-04-14","submission":"2025-11-10"},"accession":"PXD070550","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","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:6819","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:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:36630","NEWT:383379","NCBITaxon:12721","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:410658","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: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:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","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:491","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","NEWT:748693","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:33940","NEWT:550","NEWT:554","NEWT:451516","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:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","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:28550","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:441772","NEWT:48106","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","NCBI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