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Showing 1–7 of 7 results
Advanced filters: Author: Julia F. Greiwe Clear advanced filters
  • Biochemical and structural studies of the human MCM replicative DNA helicase complex show differences from the yeast complex and provide insights into mechanisms of double hexamer assembly on sequence-independent replication origins.

    • Florian Weissmann
    • Julia F. Greiwe
    • Alessandro Costa
    ResearchOpen Access
    Nature
    Volume: 636, P: 499-508
  • A cryo-EM structure of the Dbf4-dependent kinase (DDK) in the act of phosphorylating an Mcm2-7 helicase complex reveals how DDK selectively targets DNA-loaded MCM double hexamers to trigger replication origin activation. Checkpoint kinase Rad53 blocks origin firing by impairing double hexamer engagement by DDK.

    • Julia F. Greiwe
    • Thomas C. R. Miller
    • Alessandro Costa
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 29, P: 10-20
  • Here the authors used cryogenic electron microscopy and biochemistry to understand how yeast Mcm10 exerts its essential role in DNA replication initiation, finding that it splits the double Cdc45-MCM-GINS-Polε structure. The lagging-strand template is ejected from each MCM ring as the central channel of the helicase becomes too tight to accommodate two DNA strands.

    • Sarah S. Henrikus
    • Marta H. Gross
    • Alessandro Costa
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 31, P: 1265-1276
  • When the MCM motor of the replicative helicase becomes loaded onto chromatin, origin DNA is licensed for replication. Here, the authors show why the ATPase function of MCM is needed in this process. Powered by ATP hydrolysis, MCM steps away from its own loader, tracking along both DNA strands.

    • Agata Butryn
    • Julia F. Greiwe
    • Alessandro Costa
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15
  • Cryo-electron microscopy structures of the sequential assembly of the CMG replicative helicase on a chromatinized origin of replication provide insights into the mechanism through which DNA melting is initiated by ATP binding.

    • Jacob S. Lewis
    • Marta H. Gross
    • Alessandro Costa
    ResearchOpen Access
    Nature
    Volume: 606, P: 1007-1014