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Xenopus Cdc6 performs separate functions in initiating DNA replication.

Natalya S Frolova¹, Nancy Schek, Nadia Tikhmyanova

¹Molecular Oncology Program, Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111, USA.

Molecular Biology of the Cell

|April 16, 2002

Summary

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Cdc6 protein

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Cdc6 is crucial for initiating eukaryotic DNA replication.
It recruits the minichromosome maintenance (MCM) complex to DNA.

Purpose of the Study:

To investigate the distinct functional roles of ATP binding (Walker A) and hydrolysis (Walker B) motifs in Xenopus Cdc6 (Xcdc6).
To explore the multimeric nature of Cdc6 and its implications in DNA replication.

Main Methods:

Immunodepletion/add-back experiments in Xenopus egg extracts.
Analysis of mutant Xcdc6 proteins with defects in ATP binding or hydrolysis.
Assessment of chromatin association and MCM loading by mutant Cdc6 proteins.

Main Results:

Related Experiment Videos

Both Walker A and Walker B motifs are essential for Xcdc6 function, with distinct roles.
Walker B mutants associate with chromatin, while Walker A mutants show poor chromatin binding.
Neither mutant protein effectively loads MCM onto DNA, suggesting a role beyond simple binding.
Evidence indicates Cdc6 functions as a multimer, with potential in trans ATP activity.

Conclusions:

ATP binding to Cdc6 promotes chromatin association, and ATP hydrolysis facilitates MCM loading.
Cdc6 multimerization is critical for its function in DNA replication initiation.
ATP binding and hydrolysis may occur in trans between Cdc6 subunits within the multimer.