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Kadavá"],"technology_type":["Mass Spectrometry","Chemical cross-linking coupled with mass spectrometry proteomics","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Metabolic flux","Metabolon","Coenzyme q","Cross-linking and bottom-up mass spectrometry","Microscale thermophoresis","Protein-protein interactions","Langevin dynamics simulations"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062263"],"sample_protocol":["Bottom-up proteomics was performed for various COQ assemblies separated by the analytical size-exclusion chromatography. Each fraction was diluted with a buffer to achieve 100 mM Tris, pH 8.5, 10 mM TCEP, 40 mM CAA, 1% SCD (all final concentrations), and incubated for 30 min at RT. After, the sample was 10x diluted with 50 mM ammonium bicarbonate, pH 8.5. Sample digestion was performed with trypsin 1:20 (w/w) and LysC 1:50 (w/w) at 37 °C for 16 h. The digestion was quenched by TFA (0.5 % (v/v), final concentration), and samples were desalted on an Oasis HLB µElution Plate (Waters Corp) using a vendor-provided protocol. The solvent was fully evaporated, and samples dissolved in 2% (v/v) FA prior to the liquid chromatography-mass spectrometry (LC-MS) analysis.The LC-MS analysis was performed in triplicate on an UltiMate 3000 UHPLC system coupled to an Orbitrap Exploris 480 (Thermo Fisher Scientific Inc). The peptides were analyzed in 90 min gradient. First, the peptides were trapped on an PepMap No Trap C18 (5 mm × 0.3 mm, 5 μm, Thermo Fisher Scientific Inc) for 1 min at a flow rate of 30 μL/min, solvent A (0.1% FA v/v in H2O). The trapping was followed by separation on an analytical column packed in-house (Reprosil 2.4 μm, 75 μm × 50 cm) at a flow rate of 0.3 μL/min using a gradient starting from 9% solvent B (80% acetonitrile (ACN) v/v, 0.1% FA v/v) at 0–1 min, 13% B at 2 min, 44% B at 67 min, 55% B 72 min, 99% B 75 min, and equilibrated for the next run in 9% B at 80–90 min. MS1 scans were collected with the following parameters: resolution = 60000, mass range = 375-1600 Th, standard AGC target, automatic maximum injection time, cycle time = 1 s. MS2 scans were collected in data-dependent mode for precursors with charge state 2-6, with the following parameters: isolation window = 1.4 Th, resolution = 15000, mass range = 120-2000 Th, HCD collision energy = 28 %. Precursors that were once selected for fragmentation were excluded from MS2 for 14 seconds. Cross-linking mass spectrometry (XL-MS) experiments were performed both in-solution, and in-gel in an experimental triplicate. Based on the prior optimization, 0.5 μg/μL (~3 μM) COQ sample in 50 mM Hepes pH 7.5 was cross-linked with 0.5 mM DSS or 2.5 mM DMTMM for 1 h at room temperature (RT). The reaction was quenched by addition of 1 M Tris, pH 8.5 to achieve 25 μM final concentration. The samples were processed as described above for bottom-up proteomics with the only difference in enzyme:protein ratios adjusted to 1:20 trypsin (w/w), 1:50 LysC (w/w). In gel cross-linking was performed for different assemblies of COQ proteins separated by Blue native-PAGE, as previously described [Hevler et al., 2021]. Briefly, the bands of interest were excised, washed with cold PBS pH 7.5 and submerged in 50 mM Hepes pH 7.5 containing either 1.5 mM DSS or 5 mM DMTMM for 1 h at RT. The reaction was quenched by addition of 1 M Tris pH 8 to achieve 25 μM final concentration. The bands were washed with MQ H2O and dehydrated by 100% ACN. After, the samples were reduced by 6.5 mM dithiothreitol in 50 mM ammonium bicarbonate pH 8.5 (1 h, 60 °C). After reduction, the samples were dehydrated by 100% ACN and alkylated by 55 mM iodoacetamide in 50 mM ammonium bicarbonate pH  8.5 (30 min, RT, in dark). The alkylation was followed by washing and dehydrating the pieces two times with 50 mM ammonium bicarbonate, pH = 8.5. Importantly, each dehydration step involved submerging the gel pieces in 100% ACN (15 min, RT). The dehydrated gel pieces were submerged in trypsin solution (3 ng/μL in 50 mM ammonium acetate, pH 8.5) and incubated (90 min, on ice). After, 25 μL of 50 mM ammonium bicarbonate pH 8.5 was added to each sample and incubated (16 h, 37 °C). Next, the supernatant with digested peptides was collected, and gel pieces were dehydrated with 100% ACN. The supernatants were combined, and the solvent was fully evaporated. Dry peptides were dissolved in 2% FA prior to the LC-MS/MS analysis. Peptides from in-gel and in-solution cross-linking were processed by LC-MS as described above for bottom-up proteomics. The XL-MS method included several adjustments: charge states selected for MS2 = 3-8, MS2 scan range = 200-2000 m/z, MS2 resolution = 30000, HCD collision energies = 24, 28, 33 %, and precursors that were once selected for fragmentation were excluded from MS2 for 30 seconds."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The bottom-up proteomics data were searched in FragPipe 22.0 [Kong et al., 2017] against reviewed human FASTA (UniProt, accessed 13-10-2023 with common contaminants), where the COQ3-7, 8B, and 9 were replaced by the recombinant ancestral protein sequences. The peptide mass and length were set to be between 500-5000 Da and 7-50 amino acids, respectively. Precursor and fragment tolerances were set to 10 ppm and 20 ppm, respectively. Carbamidomethylation [C] was set as fixed modification, and oxidation [M] was allowed as variable modification. Results were filtered for 1% FDR and quantified using label free quantification (LFQ).  The XL-MS raw data were searched using pLink 2.0 [Chen et al., 2019] against a database containing sequences of ancestral COQ3:7 and COQ9 sequences and common contaminants. The linker mass for DSS (K-K) and DMTMM (E|D–K) was set to be 158.004 Da and -18.011, respectively. N-terminus linkage was allowed. Trypsin was set as the enzyme, cleaving at the C-terminal of K and R with up to 3 allowed missed cleavages. The peptide mass and length were set to be between 600-6000 Da and 6-60 amino acids, respectively. Precursor and fragment mass tolerances were set to be 20 ppm. Carbamidomethylation [C] was set as fixed modification, and oxidation [M] as variable modification. The results were filtered for 1% FDR and scores <10e-4. A cross-linked peptide pair was considered only if it was detected in at least 2 out of 3 experimental replicates."],"omics_type":["Proteomics"],"labhead":["Albert J.R. Heck"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht"],"species":["Synthetic Construct"],"publication":["Not available"],"submitter_mail":["t.kadava@uu.nl"],"submitter_affiliation":["Utrecht University, Biomolecular Mass Spectrometry and Proteomics"],"submitter_country":["Netherlands"],"additional_accession":[]},"is_claimable":false,"name":"Mechanistic Insights into Metabolon Formation and Substrate Channeling in Coenzyme Q Biosynthesis","description":"Metabolons - transient assemblies of sequential metabolic enzymes - facilitate the reactions of multi-step metabolic pathways. They represent crucial metabolic fineries, yet, how they mechanistically bolster metabolic flux remains enigmatic. Here, we investigate the molecular determinants of metabolon formation and substrate channeling using coarse-grained molecular dynamics simulations and biophysical approaches to coenzyme Q biosynthesis. The COQ metabolon is fastenedsecured by predominantly weak protein-protein interactions and wherein the COQ6-COQ3 enzyme pair is a critical structural hub for metabolon genesis. Selectively disrupting protein-protein associations demonstrates that protein-proximity is imperative for substrate channeling. Randomly shuffling the interaction network nodes reveals that the specific spatial arrangement of consecutive enzymes has minimal effects on product yield. Rather than specific catalytic activities or fine architectural features, proximity between enzymes in complete clusters is pivotal for metabolic flux. We conclude that the COQ metabolon is evolutionarily optimized to generate complete enzyme clusters without strict requirements for specific spatial arrangements. These findings provide mechanistic insights into how metabolic enzymes are spatially organized to achieve enhance efficient multi-step biosynthesis.","dates":{"publication":"2026-06-08","submission":"2025-03-26"},"accession":"PXD062263","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:46429","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:2736291","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:166340","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:2767846","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:468822","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:342808","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:709964","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:156974","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:1538","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:9014","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:29022","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:9006","NEWT:33548","NEWT:52299","NEWT:1883426","NEWT:8165","NEWT:96794","NEWT:10401","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:215451","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:329032","NEWT:56636","NEWT:2499525","NEWT:55307","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:141469","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:1578","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:291146","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:911022","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:717989","NEWT:33952","NEWT:1255232","NEWT:11723","NEWT:445","NEWT:153009","NEWT:1004879","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:156981","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292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