{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055091/LUMOS_RA_MS2s.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055091/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055091/RA_ObitrapLUMOS_20230404_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055091/RA_ObitrapLUMOS_20240316_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055091/RA_ObitrapLUMOS_20230404_15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055091/RA_ObitrapLUMOS_20240116_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055091/RA_ObitrapLUMOS_20230404_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055091/RA_ObitrapLUMOS_20240316_03.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["ruslana@bu.edu"],"submitter":["Clinton Yu"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Guide rna editosome","Rna editing catalytic complex","Mitochondria","Trypanosoma","Rna editing"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD055091"],"sample_protocol":["Parasites were cultured in 10-12 L of SDM-79 medium containing 10% fetal calf serum at 27°C until reaching a concentration of 3-4x10^7 cells/ml. Mitochondrial vesicles were isolated through hypotonic lysis, DNase digestion, and differential centrifugation 1 . The mitochondrial fraction (~20 g wet weight) was resuspended in 40 ml of a buffer containing 50 mM Tris-HCl (pH 7.6), 60 mM KCl, 10 mM MgCl 2 , and 0.4% Triton X-100. Complete EDTA-free protease inhibitors (Roche, 1 tablet) and 1000 U of DNase I were added to the lysate, which was incubated with gentle mixing for 30 minutes. Following incubation, the lysate was clarified by centrifugation at 40,000 RPM for 20 minutes in SW41 Beckman rotor. The clarified lysate was incubated with 0.5 ml of packed Avidin Sepharose resin (Sigma) to remove biotinylated proteins. The avidin resin was removed by passing the lysate through a filter-plugged 2 ml Pierce disposable column equipped with an expansion reservoir. The recovered lysate was then incubated with 0.5 ml of Strep-TactinXT 4Flow high-capacity resin (Iba Lifesciences) for 30 minutes. The mixture was transferred to a 2 ml Pierce disposable column, reloaded twice, and washed five times with 10 ml of a buffer consisting of 25 mM Tris-HCl (pH 7.6), 60 mM KCl, 10 mM MgCl 2 , and 0.1% Triton X-100. Proteins were eluted with three sequential additions of 0.5 ml of the same buffer supplemented with 100 mM biotin and 3 mM CaCl 2 . The eluted material was subsequently incubated with 0.2 ml of Anti-Protein C Affinity Matrix (Roche) for 2 hours. The resin was washed three times with 2 ml of a buffer containing 25 mM Tris-HCl (pH 7.6), 60 mM KCl, 10 mM MgCl 2 , 2 mM CaCl 2 , and 5 mM n-Octylglucoside (OG). The resin was transferred to a Pierce Spin Column and subjected to three spin-washes with 0.5 ml of the same buffer at 300 g for 10 seconds, followed by a final wash with 25 mM Tris-HCl (pH 7.6), 60 mM KCl, 1 mM CaCl 2 , and 5 mM OG. Proteins were eluted by spinning the column at 1500 g for 1 minute with 0.15 ml of a buffer containing 25 mM Tris-HCl (pH 7.6), 60 mM KCl, 5 mM OG, 2 mM EDTA, and 5 mM EGTA. The eluted material (0.1 ml) was immediately exchanged into 25 mM Tris-HCl (pH 7.6), 60 mM KCl, 5 mM OG, and 10 mM MgCl 2 buffer using a Zeba Spin Desalting Column.  Affinity-purified complexes (2-5 µg of total protein) were precipitated with 20% trichloroacetic acid and 0.2% deoxycholate, washed with cold acetone, and digested with Lys-C peptidase (1:50 protease-protein ratio) in 10 µl of 8M urea, 50 mM sodium bicarbonate, pH 8, at 37 C for four hours. Digestion was continued overnight after adding trypsin (1:100 ratio) and diluting the sample four-fold with 50 mM sodium bicarbonate, pH 8. Peptides were purified with C18 Spin columns (ThermoFisher Scientific), as recommended by the manufacturer. LC-MS/MS was carried out by nanoflow reversed-phase liquid chromatography (RPLC) using an UltiMate 3000 RSLC (Thermo Scientific) coupled online to an Orbitrap Fusion Lumos mass spectrometer (Thermo Scientific). A cycle of full FT scan mass spectrum (m/z 375-1500, resolution of 60,000 at m/z 400) was followed by MS/MS spectra acquired in the linear ion trap for 3 seconds at top speed with normalized collision energy (HCD, 30%)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Following data extraction using PAVA (UCSF), the resulting peak lists for each LC-MS/MS experiment were submitted to Protein Prospector (UCSF) for database searching against randomly concatenated T. brucei database (http://tritrypdb.org/tritrypdb/). The mass accuracies for parent ions and fragment ions were set as ± 15 ppm and 0.6 Da, respectively. Trypsin was selected as the enzyme, with a maximum of two missed cleavages allowed. Cysteine carbamidomethylation was set as a fixed modification, and protein N-terminal acetylation, methionine oxidation, and N-terminal conversion of glutamine to pyroglutamic acid were selected as variable modifications."],"omics_type":["Proteomics"],"labhead":["Ruslan Afasizhev"],"instrument_platform":[""],"labhead_affiliation":["Boston University Goldman School of Dental Medicine Boston MA, 02118, USA"],"submission_type":["PARTIAL"],"species":["Trypanosoma Brucei"],"publication":["Not available"],"submitter_mail":["clinton.yu@uci.edu"],"submitter_affiliation":["University of California, Irvine"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis of the mitochondrial RNA editing cascade in trypanosomes","description":"The discovery of RNA editing in trypanosomes introduced the concept of guide RNA (gRNA). To understand how the RECC1 and RECC2 complexes mediate gRNA-directed uridine deletions and insertions, respectively, in mitochondrial mRNAs, we determined their structures and RNA interactions. The RECC cores, consisting of distinct heterotetramers of active and inactive RNase III endonucleases, recognize gRNA–mRNA duplexes. Auxiliary zinc-finger domains distinguish deletion from insertion editing sites, while asymmetrical catalytic centers cleave the mRNA. Three peripheral heterotetramers composed of oligonucleotide-binding (OB-fold) proteins flexibly tether exonuclease, TUTase, and ligase enzymes to the cores, facilitating trimming or extension of cleaved mRNA and strand repair. An architectural tRNA stabilizes the RNase III–OB-fold interface. These findings illuminate the organization of the enzymatic cascade and suggest a mechanism for editing site recognition.","dates":{"publication":"2026-06-15","submission":"2024-08-22"},"accession":"PXD055091","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:111205","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:111225","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:294607","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: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:51329","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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