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DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
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DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
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DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
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The cell cycle is a series of events leading to DNA duplication followed by the division of cell content to form two daughter cells. The cell cycle progresses in four stages—the cell increases in size (gap 1 or G1-phase), duplicates its DNA (synthesis or S-phase), prepares to divide (gap 2 or G2-phase), and divides (mitosis or M-phase).
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Related Experiment Video

Updated: Apr 26, 2026

Author Spotlight: Investigating the Motion Dynamics of the Eukaryotic Replisome Components at the Single-Molecule Level
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Multiple functions for Mcm2-7 ATPase motifs during replication initiation.

Sukhyun Kang1, Megan D Warner1, Stephen P Bell1

  • 1Howard Hughes Medical Institute, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

Molecular Cell
|August 5, 2014
PubMed
Summary

The Mcm2-7 helicase

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The Mcm2-7 complex is a crucial replicative helicase in eukaryotes.
  • Its six ATPase sites' roles in DNA replication initiation are not fully understood.

Purpose of the Study:

  • To investigate the specific functions of the Mcm2-7 ATPase active sites during DNA replication.
  • To elucidate the roles of Mcm2-7 and Cdc6 ATPases in helicase loading and activation.

Main Methods:

  • Utilized ATPase-motif mutations in Mcm2-7 complexes.
  • Compared Mcm2-7 mutants with Cdc6 ATPase mutants.
  • Assessed helicase loading, recruitment, Cdt1 release, and activation events.

Main Results:

  • Mcm2-7 ATP binding and hydrolysis are essential for helicase loading.

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  • Cdc6 ATP hydrolysis is not required for loading but removes incompletely loaded complexes.
  • Mcm2-7 mutants showed defects in replication initiation, DNA association, GINS recruitment, and unwinding.

    • Conclusions:

    • The six Mcm2-7 ATPase active sites are specialized for distinct functions in helicase loading and activation.
    • This specialization is consistent with the heterohexameric structure of the Mcm2-7 complex.