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

doi:10.1038/sj.embor.7401064

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

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

33 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 language	English (US)
Pages (from-to)	925-930
Number of pages	6
Journal	EMBO reports
Volume	8
Issue number	10
DOIs	https://doi.org/10.1038/sj.embor.7401064
State	Published - Oct 2007

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Genetics

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10.1038/sj.embor.7401064

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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.",

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AU - Okorokov, Andrei L.

AU - Waugh, Alastair

AU - Hodgkinson, Julie

AU - Murthy, Andal

AU - Hong, Hye Kyung

AU - Leo, Elisabetta

AU - Sherman, Michael B.

AU - Stoeber, Kai

AU - Orlova, Elena V.

AU - Williams, Gareth H.

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AB - 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.

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Hexameric ring structure of human MCM10 DNA replication factor

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