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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

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Structural and mechanistic insights into Mcm2-7 double-hexamer assembly and function.

Jingchuan Sun¹, Alejandra Fernandez-Cid², Alberto Riera²

¹Biosciences Department, Brookhaven National Laboratory, Upton, New York 11973, USA;

Genes & Development

|October 17, 2014

Summary

This summary is machine-generated.

Eukaryotic cells license DNA replication origins using minichromosome maintenance proteins (Mcm2-7) double hexamers. This study reveals how these complexes assemble and regulate helicase activity for cell cycle control and genome stability.

Keywords:

DNA replication initiation electron microscopy origin recognition complex prereplication complex replicative helicase

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Area of Science:

Molecular Biology
Cell Biology
Structural Biology

Background:

Eukaryotic DNA replication initiates at origins licensed in G1 phase by prereplication complexes containing Mcm2-7 double hexamers.
The precise mechanisms of origin licensing and the activation of Mcm2-7 (minichromosome maintenance proteins 2-7) as a DNA helicase remain incompletely understood.
Recruitment of the second Mcm2-7 hexamer to form the double-hexamer structure is a key, yet poorly elucidated, step in licensing.

Purpose of the Study:

To elucidate the structural mechanisms underlying DNA replication origin licensing.
To understand how the Mcm2-7 double-hexamer is assembled and regulated.
To provide insights into the activation of DNA helicase activity and its implications for cell cycle control.

Main Methods:

Structural analysis of intermediate complexes involved in Mcm2-7 double-hexamer formation.
Detailed structural characterization of the loaded Mcm2-7 double-hexamer complex bound to DNA.
Biochemical assays to assess ATP hydrolysis activity and protein interactions.

Main Results:

Structural evidence for intermediate complexes, including ORC-Cdc6-Mcm2-7 and ORC-Cdc6-Mcm2-7-Mcm2-7, provides insights into DNA licensing.
The Mcm2-7 double hexamer is interlocked, misaligned on DNA, and lacks basal ATP hydrolysis activity.
Juxtaposition of the Mcm2-7 double hexamer creates a binding site for an S-phase protein kinase, crucial for replication activation.

Conclusions:

The study reveals the structural basis for Mcm2-7 double-hexamer assembly during DNA replication licensing.
Regulation of Mcm2-7 helicase activity is intrinsically linked to its assembly state and interactions with regulatory kinases.
These findings have significant implications for understanding cell cycle control of DNA replication and maintaining genome stability.