Hexameric ring structure of human MCM10 DNA replication factor

Andrei L. Okorokov, Alastair Waugh, Julie Hodgkinson, Andal Murthy, Hye Kyung Hong, Elisabetta Leo, Michael B. Sherman, Kai Stoeber, Elena V. Orlova, Gareth H. Williams

Research output: Contribution to journalArticle

30 Scopus citations

Abstract

The DNA replication factor minichromosome maintenance 10 (MCM10) is a conserved, abundant nuclear protein crucial for origin firing. During the transition from pre-replicative complexes to pre-initiation complexes, MCM10 recruitment to replication origins is required to provide a physical link between the MCM2-7 complex DNA helicase and DNA polymerases. Here, we report the molecular structure of human MCM10 as determined by electron microscopy and single-particle analysis. The MCM10 molecule is a ring-shaped hexamer with large central and smaller lateral channels and a system of inner chambers. This structure, together with biochemical data, suggests that this important protein uses its architecture to provide a docking module for assembly of the molecular machinery required for eukaryotic DNA replication.

Original languageEnglish (US)
Pages (from-to)925-930
Number of pages6
JournalEMBO reports
Volume8
Issue number10
DOIs
StatePublished - Oct 1 2007

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics

Cite this

Okorokov, A. L., Waugh, A., Hodgkinson, J., Murthy, A., Hong, H. K., Leo, E., Sherman, M. B., Stoeber, K., Orlova, E. V., & Williams, G. H. (2007). Hexameric ring structure of human MCM10 DNA replication factor. EMBO reports, 8(10), 925-930. https://doi.org/10.1038/sj.embor.7401064