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TitleUnidirectional MCM translocation away from ORC drives origin licensing.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 782, Year 2025
Publish dateJan 17, 2025
AuthorsAgata Butryn / Julia F Greiwe / Alessandro Costa /
PubMed AbstractThe MCM motor of the eukaryotic replicative helicase is loaded as a double hexamer onto DNA by the Origin Recognition Complex (ORC), Cdc6, and Cdt1. ATP binding supports formation of the ORC-Cdc6- ...The MCM motor of the eukaryotic replicative helicase is loaded as a double hexamer onto DNA by the Origin Recognition Complex (ORC), Cdc6, and Cdt1. ATP binding supports formation of the ORC-Cdc6-Cdt1-MCM (OCCM) helicase-recruitment complex where ORC-Cdc6 and one MCM hexamer form two juxtaposed rings around duplex DNA. ATP hydrolysis by MCM completes MCM loading but the mechanism is unknown. Here, we used cryo-EM to characterise helicase loading with ATPase-dead Arginine Finger variants of the six MCM subunits. We report the structure of two MCM complexes with different DNA grips, stalled as they mature to loaded MCM. The Mcm2 Arginine Finger-variant stabilises DNA binding by Mcm2 away from ORC/Cdc6. The Arginine Finger-variant of the neighbouring Mcm5 subunit stabilises DNA engagement by Mcm5 downstream of the Mcm2 binding site. Cdc6 and Orc1 progressively disengage from ORC as MCM translocates along DNA. We observe that duplex DNA translocation by MCM involves a set of leading-strand contacts by the pre-sensor 1 ATPase hairpins and lagging-strand contacts by the helix-2-insert hairpins. Mutating any of the MCM residues involved impairs high-salt resistant DNA binding in vitro and double-hexamer formation assessed by electron microscopy. Thus, ATPase-powered duplex DNA translocation away from ORC underlies MCM loading.
External linksNat Commun / PubMed:39824870 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.7 Å
Structure data

EMDB-51398: OCCM maturation intermediate stalled with an Arginine Finger mutation in Mcm5: Conformer 2. Consensus map.
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-51399: OCCM maturation intermediate stalled with an Arginine Finger mutation in Mcm5: Conformer 2. ORC local refinement.
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-51400: OCCM maturation intermediate stalled with an Arginine Finger mutation in Mcm5: Conformer 2. Local MCM-Cdt1 refinement.
Method: EM (single particle) / Resolution: 3.5 Å

51401

9gjp

EMDB-51401: OCCM maturation intermediate stalled with an Arginine Finger mutation in Mcm5: Conformer 2. Composite map.
PDB-9gjp: OCCM maturation intermediate stalled with an Arginine Finger mutation in Mcm5: Conformer 2
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-51404: OCCM maturation intermediate stalled with an Arginine Finger mutation in Mcm2. Consensus map
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-51405: OCCM maturation intermediate stalled with an Arginine Finger mutation in Mcm2. ORC local refinement.
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-51406: OCCM maturation intermediate stalled with an Arginine Finger mutation in Mcm2. MCM-Cdt1 local refinement.
Method: EM (single particle) / Resolution: 3.2 Å

51407

9gjw

EMDB-51407: OCCM maturation intermediate stalled with an Arginine Finger mutation in Mcm2. Composite map.
PDB-9gjw: OCCM maturation intermediate stalled with an Arginine Finger mutation in Mcm2
Method: EM (single particle) / Resolution: 3.3 Å

51441

9gm5

EMDB-51441, PDB-9gm5:
OCCM maturation intermediate stalled with an Arginine Finger mutation in Mcm5: Conformer 1
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-ZN:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • synthetic construct (others)
KeywordsREPLICATION / AAA+ ATPase / DNA translocase / ATPase switch / DNA replication

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