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Stengel"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Chemical cross-linking coupled with mass spectrometry proteomics"],"software":["Not available"],"submitter_keywords":["Ribosome","Xl-ms","Rna repair","Rlig1"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067615"],"sample_protocol":["17,5 µM Rlig1-AMP or apo-Rlig1 K57A was gently mixed with 67 nM 80S ribosomes in cross-linking buffer (50 mM HEPES pH 7.50, 5 mM MgCl2, 100 mM KCl). The mixture was incubated without agitation to allow complex formation (30 min, 37°C). Afterwards, 1.5 mM BS3-H12/D12 crosslinker (Creative Molecules Inc.) was added and the reaction mixture was incubated with gentle agitation (30 min, 37°C, 350 rpm). After the crosslinking, unreacted linker was quenched by the addition of NH4HCO3 (50 mM, 15 min). The samples were dried and subsequently dissolved in 8 M urea. The sample was reduced with Tris(2-carboxyethyl)phosphine (2.5 mM, 30 min, 37°C), alkylated with iodoacetamide (5 mM, 30 min, RT, in the dark) and digested with trypsin (Promega, 1:50 enzyme-to-substrate, 16 h, 37°C). The peptides were desalted (C18 Sep-Pak cartridges (Waters)) and crosslinked peptides were enriched by size exclusion chromatography using an ÄKTAmicro chromatography system (GE Healthcare) equipped with a SuperdexTM Peptide 3.2/30 column. Fractions containing peptides were collected and combined to four fractions. LC-MS2 analysis was performed on an Orbitrap Tribrid Fusion mass spectrometer coupled to an EASY-nLC 1200 system (Thermo Scientific). Peptides were separated across a 75 min gradient on an Acclaim PepMap column (150x0.05 mm, 2 µm, Thermo Scientific, P/N 164943). MS measurement was performed in data-dependent mode with a maximum cycle time of 3 sec. Full scans were acquired in the Orbitrap at a resolution of 120’000, in the scan range of 400-1500 m/z, AGC target 2e5 and a maximum injection time of 50 ms. For precursor selection, monoisotopic precursor selection was set to peptides, dynamic exclusion to 60 sec and only precursor ions with charge states 3-8 were isolated for MS/MS acquisition. Precursor ions were fragmented with 35 % CID activation and MS/MS scan was acquired in the iontrap in rapid scan mode."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Crosslink analysis was done with xQuest/xProphet (Leitner et al., 2014) in ion-tag mode with a precursor mass tolerance of 10 ppm. For matching of fragment ions, tolerances of 0.2 Da for common ions and 0.3 Da for crosslinked ions were applied. The database was compiled of the Rlig1 protein sequence as well as proteins that are part of the mature cytosolic ribosome. An FDR was estimated by xProphet and only hits with an FDR below 0.01 were used. The experiment was performed as biological triplicate with two technical replicates each. Crosslinks identified with ld-score ≥ 25 and deltaS < 0.95 were retained for further analysis and interlinks were filtered with the mi-filter.(Chen et al., 2022)"],"omics_type":["Proteomics"],"labhead":["Florian Stengel"],"instrument_platform":[""],"labhead_affiliation":["Department of Biology University of Konstanz Universitätsstrasse 10 78457 Konstanz Germany"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["florian.stengel@uni-konstanz.de"],"submitter_affiliation":["Universität Konstanz"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Human RNA ligase 1 as a novel regulator of ribosome function and translation under oxidative stress","description":"Human RNA ligase 1 (Rlig1) is a recently identified human 5’-3’ RNA ligase essential for maintaining 28S rRNA integrity and promoting cell survival under oxidative stress. Although the enzymatic activity of Rlig1 implies a role in RNA maintenance or repair, its broader molecular context remains insufficiently characterised. Here we identify cellular interactors of Rlig1 using affinity enrichment coupled to mass spectrometry in a HEK293 Rlig1-KO model. Our approach revealed several RNA and DNA surveillance, degradation and repair proteins as well as a diverse set of RNA binding and RNA processing enzymes as potential interactors. Notably, ribosomal proteins were highly enriched, suggesting a link between Rlig1 and the translational machinery. Cross-linking coupled to mass spectrometry confirmed that Rlig1 interacts with 80S ribosomes in vitro and preferentially binds the large ribosomal subunit near the 28S rRNA. Polysome profiling corroborated this interaction, as Rlig1 was recruited to ribosomal fractions containing the large ribosomal subunit in response to oxidative stress. Moreover, Rlig1-deficient cells exhibited earlier polysome loss and significantly impaired translational activity compared to their WT counterparts under these conditions. These results highlight a potential novel role for Rlig1 in safeguarding translation during oxidative stress.","dates":{"publication":"2026-05-25","submission":"2025-08-22"},"accession":"PXD067615","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:625351","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:1582","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","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:3714","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","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:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","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:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","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:3728","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:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","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:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","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:52639","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1045775","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:1028307","NEWT:13489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