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Montoya"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Ssdna","Helicase","Origins","Rpa","Yeast","Unwinding","Dna replication","Chip-exo","S-phase","Mcm2-7"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD080178"],"sample_protocol":["Immunoprecipitations (IPs) were processed by single-pot solid-phase-enhanced sample-preparation (SP3) technology. Eluted samples were mixed with reconstitution buffer (50 mM HEPES pH 8.0, 1% sodium dodecyl sulphate (w/v) SDS, 1% Triton X-100 (v/v), 1% NP-40 (v/v), 1% Tween 20 (v/v), 1% sodium deoxycholate (w/v), 5 mM EDTA pH 8.0, 50 mM NaCl, 1% glycerol (v/v)). Proteins were reduced using 5 mM DTT, followed by alkylation using 20 mM chloroacetamide. Reduced and alkylated protein was transferred to a new tube containing 100% EtOH pre-mixed with Sera-Mag Speedbeads (GE Healthcare, 2 uL of each per sample). Reduced and alkylated protein was added, to a final concentration of 60% EtOH. Protein-bound beads were rinsed three times with 80% EtOH using a magnetic rack, and after the final wash, beads were resuspended in digestion solution (100 mM ammonium bicarbonate pH 8.0) containing 1 ug of Trypsin Gold (Promega). After sonication to disperse the beads, digestions were incubated overnight (18 hrs) at 37°C and dried in a centrifugal evaporator. Total protein digests were dissolved in 0.1% trifluoroacetic acid by shaking (1200rpm) for 30 min and sonication for 10 min, followed by centrifugation (14,000rpm, 5°C and 10 min). LC-MS/MS analysis was carried out in technical duplicates. Chromatographic separation was performed using an Ultimate 3000 RSLC nano liquid chromatography system (Thermo Scientific) coupled to an Orbitrap Q-Exactive mass spectrometer (Thermo Scientific) via an EASY-Spray source. For LC-MS/MS analysis peptide solutions were injected and loaded onto a trapping column (Acclaim PepMap 100 C18, 100μm × 2cm) for desalting and concentration at 8 μL/min in 2% acetonitrile, 0.1% trifluoroacetic acid. Peptides were then eluted on-line to an analytical column (EASY-Spray PepMap RSLC C18, 75μm × 75cm). Eluted peptides were analysed by the mass spectrometer operating in positive polarity using a data-dependent acquisition mode. Ions for fragmentation were determined from an initial MS1 survey scan at 70,000 resolution, followed by HCD (Higher-energy Collision Induced Dissociation) of the top 12 most abundant ions at a resolution of 17,500. MS1 and MS2 scan AGC targets were set to 3e6 and 5e4 for maximum injection times of 50 ms and 50 ms respectively. A survey scan m/z range of 400 – 1800 was used, normalised collision energy set to 37% and charge exclusion enabled for unassigned and +1 ions. Dynamic exclusion was set to 30 seconds."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data were processed using the MaxQuant software platform (v1.6.10.43), with database searches carried out by Andromeda search engine against the Swissprot Saccharomyces cerevisiae database (version 20210222, number of entries: 6,049). A reverse decoy database approach was used at a 1% false discovery rate (FDR) for peptide spectrum matches. Search parameters were as follows: maximum missed cleavages set to 2, fixed modification of cysteine carbamidomethylation and variable modifications of methionine oxidation and protein N-terminal acetylation. Label-free quantification (LFQ) was enabled with an LFQ minimum ratio count of 1. ‘Match between runs’ function was used with match and alignment time limits of 0.7 and 20 min respectively. For generation of volcano plots, replicates and relative protein abundances were analysed using the Perseus software platform (v1.6.10.43). Proteins that were not present in at least three out of four replicates in at least one condition were excluded. Missing values for retained proteins were imputed from a normal distribution. Proteins associated with the Replication Initiation GO term were compared with the volcano plot function in Perseus, with an FDR of 0.1 and S0 of 0.1."],"omics_type":["Proteomics"],"labhead":["Professor Christian Speck"],"instrument_platform":[""],"labhead_affiliation":["Head of the DNA Replication Research Group"],"submission_type":["PARTIAL"],"species":["Saccharomyces Cerevisiae (baker's Yeast)"],"publication":["Not available"],"submitter_mail":["proteomics@lms.mrc.ac.uk"],"submitter_affiliation":["London Institute of Medical Sciences"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Mechanisms of MCM2-7 helicase activation and initial DNA melting at near base-pair resolution","description":"During eukaryotic DNA replication initiation, inactive MCM2-7 double-hexamers assembled at replication origins must be converted into two active CMG helicases, yet how this transition is coupled to origin DNA unwinding in vivo remains unclear. Here, we identify a DNA-bound intermediate with an extended genomic footprint that forms during helicase activation. Genome-wide mapping of initial strand separation reveals that DNA unwinding initiates near the N-terminal interface of opposing MCM2-7 hexamers. At these sites, the origin DNA exhibits a conserved AT-rich/GC-rich/AT-rich sequence architecture centred under the helicase complex, which is associated with an elevated DNA melting probability. We further show that restricting hexamer splitting delays release of the Cdc45-loading factor Sld3, demonstrating that mechanical transitions during helicase activation are tightly coupled to complex disassembly. Finally, we provide in vivo evidence that single-stranded DNA is ejected through a specialised DNA exit gate at the Mcm2/5 interface during helicase activation, which is dispensable for ongoing DNA synthesis. Together, these findings establish a mechanistic framework for how replication origins are remodelled to initiate DNA replication and reveal key intermediates and DNA transactions during helicase activation.","dates":{"publication":"2026-06-26","submission":"2026-06-25"},"accession":"PXD080178","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: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: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: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: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: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: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:8655","NEWT:5147","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","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: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: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:231490","NEWT:244704","NEWT:7725","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:72664","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:452467","NEWT:19882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