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Benstead-Hume"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Aml","Terminal uridylyl-transferases","Hspc"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077084"],"sample_protocol":["Cell pellets were lysed in a buffer containing 1% sodium deoxycholate (SDC), 100 mM triethylammonium bicarbonate (TEAB), 10% isopropanol and 50 mM NaCl, freshly supplemented with 5 mM TCEP (Thermo, Bond-breaker), 10 mM iodoacetamide, universal nuclease 1:2000 vol/vol (Pierce, #88700) and Halt protease and phosphatase inhibitor cocktail (Thermo, #78442, 100X) with 5 min of bath sonication. Protein concentration was measured with the Quick Start Bradford protein assay (Bio-Rad). Aliquots of 30 μg of total protein were digested overnight with trypsin (Pierce, 1:20) at room temperature. Peptides were labelled with the TMTpro reagents (Thermo) by adding 5 μL of the reagent (25 μg/μL) into 12.5 μL of sample volume. The TMTpro mixture was acidified with formic acid at 2% and the precipitated SDC was removed by centrifugation. The peptide pool was fractionated with high-pH Reversed-Phase chromatography using the XBridge C18 column (2.1 × 150 mm, 3.5 μm, Waters) on an UltiMate 3000 HPLC system over a 1% gradient in 35 min. Mobile phase A was 0.1% (v/v) ammonium hydroxide and mobile phase B was 0.1% ammonium hydroxide (v/v) in acetonitrile.  LC-MS analysis was performed on a Vanquish Neo UHPLC system coupled to the Orbitrap Ascend mass spectrometer (Thermo) using a 25 cm capillary column (Waters, nanoE MZ PST BEH130 C18, 1.7 μm, 75 μm × 250 mm) over a 100 min gradient 5%-35% of mobile phase B composed of 80% acetonitrile, 0.1% formic acid. Peptides were preconcentrated onto a PEPMAP 100 C18 5 μm 0.3 × 5 mm 1500 Bar trapping column and the analytical column was connected to a stainless-steel emitter on the Nanospray Flex ion source. MS spectra were collected at Orbitrap mass resolution of 120k and precursors were selected for HCD fragmentation in the top speed mode (3 sec) with collision energy 32% and iontrap detection in turbo scan rate. MS3 scans were triggered by Real Time Search (RTS) against a fasta file containing UniProt Mus musculus reviewed canonical and isoform sequences with Synchronous Precursor Selection (SPS) isolation (10 notches) and HCD fragmentation with collision energy 55% at 45k Orbitrap resolution. Selected precursors were dynamically excluded from further activation for 45 seconds with 10 ppm mass tolerance and RTS close-out was enabled with max 4 peptides per protein. Static modifications for RTS were TMTpro16plex at K/n-term (+304.2071), Carbamidomethyl at C (+57.0215) and variable modifications were Deamidated NQ (+0.984) and Oxidation of M (+15.9949) with maximum 1 missed-cleavage and 2 variable modifications per peptide. An additional injection of each fraction was conducted by including Farnesyl (+204.188 Da) and GeranylGeranyl (+272.250 Da) at C, as well as Carbamidomethyl at C (+57.0215) as variable modifications in the RTS analysis."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The Sequest HT and Comet nodes in Proteome Discoverer 3.0 (Thermo) were used to search the raw mass spectra against a fasta file containing reviewed UniProt Mus musculus entries. The precursor mass tolerance was set at 20 ppm and the fragment ion mass tolerance at 0.5 Da (or 1 Da for Comet) with up to 2 trypsin missed-cleavages allowed. TMTpro at N-terminus/K were defined as static modifications. Dynamic modifications were Oxidation of M (+15.995 Da), Deamidation of N/Q (+0.984 Da), Farnesyl (+204.188 Da) at C, GeranylGeranyl (+272.250 Da) at C and Carbamidomethyl (+57.0215) at C. Peptide confidence was estimated with the Percolator node and peptide FDR was set at 0.01 based on target-decoy search. Only unique peptides were used for quantification, considering protein groups for peptide uniqueness. Peptides with average reporter signal-to-noise greater than 3 were used for protein quantification."],"omics_type":["Proteomics"],"labhead":["Jyoti Choudhary"],"instrument_platform":[""],"labhead_affiliation":["Functional Proteomics, ICR"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["ghume@icr.ac.uk"],"submitter_affiliation":["ICR"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"RNA Terminal Uridylyl-Transferases Are Druggable Vulnerabilities in AML, but are Dispensable for Normal Hematopoiesis","description":"Acute myeloid leukemia (AML) is an aggressive hematological malignancy arising from hematopoietic stem and progenitor cells (HSPCs). Current treatments often fail to eradicate AML, therefore, new therapeutic strategies are essential. Here, we reveal that RNA Terminal-Uridylyl-Transferase-Enzymes 4 and 7 (TUT4/7) as novel druggable therapeutic targets, whose genetic deletion in AML suppresses growth, induces apoptosis and improves the survival of leukemic mice. Notably, a pre-clinical TUT4/7 inhibitor promotes cell death in AML patient samples and synergizes with Venetoclax. Mechanistically, TUT4/7 inactivation disrupts cellular metabolism and suppresses mevalonate pathway gene expression, compromising the prenylation and cholesterol synthesis pathways. Current AML therapies often cause severe hematopoietic toxicity. Although Tut4/7 deletion results in inflammatory activation throughout the hematopoietic system, this is permissive to a normal lifespan and Tut4/7-deficiency does not compromise HSPC function. Thus, we reveal TUT4/7 as druggable targets, whose inactivation suppresses AML while sparing normal hematopoiesis.  In combination with Venetoclax this represents a novel and promising therapeutic strategy.","dates":{"publication":"2026-06-24","submission":"2026-04-13"},"accession":"PXD077084","cross_references":{"TAXONOMY":["NEWT:3555","NEWT:71647","NEWT:330879","NEWT:35554","NEWT:32046","NEWT:544496","NEWT:2042546","NEWT:32049","NEWT:1392696","NEWT:259447","NEWT:295546","NEWT:45351","NEWT:445974","NEWT:43179","NEWT:180454","NEWT:5722","NCBITaxon:1280","NEWT:1129","NEWT:309807","NEWT:10245","NEWT:55153","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:43186","NEWT:428146","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:498019","NEWT:1351","NEWT:1438992","NEWT:1352","NEWT:2649997","NEWT:1147161","NEWT:661410","NEWT:638632","NEWT:263737","NEWT:224326","NEWT:1333499","NCBITaxon:79857","NEWT:1096976","NEWT:5702","NEWT:95648","NEWT:1589","NEWT:135622","NEWT:1349","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:1401257","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:44491","NEWT:641809","NEWT:27933","NEWT:556484","NEWT:317447","NEWT:4688","NEWT:7955","NEWT:7959","NEWT:2261","NEWT:31156","NEWT:3112","NEWT:79329","NEWT:4442","NEWT:192875","NEWT:1214915","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:1316931","NEWT:224308","NEWT:3347","NEWT:511145","NEWT:160621","NEWT:212790","NEWT:931281","NEWT:4432","NEWT:5762","NEWT:5763","NEWT:658457","NEWT:1310161","NEWT:77133","NEWT:295358","NEWT:145481","NCBITaxon:79824","NEWT:2246","NEWT:2652724","NEWT:5757","NCBITaxon:4563","NEWT:5755","NEWT:44689","NEWT:44447","NEWT:752555","NEWT:498211","NEWT:5759","NEWT:1736231","NEWT:5518","NEWT:398007","NEWT:1392","NEWT:498217","NEWT:498216","NEWT:2242","NEWT:11320","NEWT:286","NEWT:391619","NEWT:246196","NEWT:287","NEWT:246197","NEWT:145458","NEWT:633149","NEWT:1149786","NEWT:10239","NEWT:68895","NEWT:44685","NEWT:161934","NEWT:4897","NEWT:1148","NEWT:5744","NEWT:5508","NEWT:3329","NEWT:5507","NEWT:410661","NEWT:55571","NEWT:35500","NEWT:1235816","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:4896","NEWT:1287689","NEWT:1390","NEWT:11557","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:294","NEWT:1773","NEWT:1182590","NEWT:3712","NEWT:82380","NEWT:3711","NEWT:935293","NEWT:375146","NEWT:2065263","NEWT:1772","NEWT:118698","NEWT:1616117","NEWT:263","NEWT:118696","NEWT:52283","NEWT:11988","NEWT:284812","NEWT:8175","NEWT:400667","NEWT:43330","NEWT:1603293","NEWT:408169","NEWT:44664","NEWT:47946","NEWT:459758","NEWT:3702","NEWT:1245466","NEWT:243277","NEWT:1246791","NEWT:7067","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:33548","NEWT:274","NEWT:7070","NCBITaxon:287","NEWT:408172","NEWT:408170","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1436733","NEWT:460519","NEWT:1247411","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:9483","NEWT:333760","NEWT:56636","NEWT:1513458","NEWT:1233681","NCBITaxon:40559","NEWT:506599","NEWT:2853422","NEWT:81077","NEWT:84588","NEWT:1679718","NEWT:480","NEWT:65349","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:300852","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:508771","NEWT:1883446","NEWT:253","NCBITaxon:2759","NEWT:1233435","NEWT:93061","NEWT:93062","NCBITaxon:4932","NEWT:109760","NEWT:943274","NEWT:644223","NEWT:235443","NEWT:108458","NEWT:5936","NEWT:272623","NEWT:272624","NEWT:320637","NEWT:983964","NEWT:118499","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:1130798","NEWT:55529","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:476272","NEWT:3747","NEWT:195051","NEWT:3988","NEWT:1116234","NEWT:1255228","NEWT:649908","NEWT:410289","NEWT:373153","NEWT:3983","NEWT:352472","NEWT:1071661","NEWT:1202532","NEWT:360094","NEWT:470","NEWT:41364","NEWT:1313","NEWT:1218097","NCBITaxon:50557","NEWT:39251","NEWT:39491","NCBITaxon:5811","NEWT:29491","NEWT:101841","NEWT:2014887","NEWT:33952","NEWT:153009","NEWT:261756","NEWT:571256","NEWT:40483","NEWT:63366","NEWT:63367","NEWT:688333","NEWT:215402","NCBITaxon:548681","NEWT:318586","NEWT:272634","NEWT:198107","NEWT:9031","NEWT:1872122","NEWT:1308","NEWT:7091","NEWT:1034015","NEWT:760568","NEWT:141262","NEWT:108931","NEWT:1055524","NEWT:4087","NEWT:9778","NEWT:306","NEWT:150475","NEWT:303","NEWT:267872","NEWT:97477","NEWT:7111","NEWT:347515","NEWT:172269","NEWT:9534","NEWT:6269","NEWT:5180","NEWT:256737","NEWT:4090","NEWT:4092","NEWT:9541","NEWT:8694","NEWT:4093","NEWT:4096","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:941442","NEWT:536088","NEWT:13076","NEWT:1226408","NEWT:7108","NEWT:40479","NEWT:43989","NEWT:4076","NEWT:142615","NEWT:317","NEWT:1006581","NEWT:885318","NEWT:39488","NEWT:550","NEWT:4081","NEWT:273068","NEWT:554","NEWT:98334","NEWT:451516","NEWT:4084","NEWT:63577","NEWT:36185","NEWT:1225786","NEWT:7574","NEWT:1715256","NEWT:30640","NEWT:575412","NEWT:929793","NEWT:29204","NEWT:28112","NEWT:114155","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643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