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Vol. 10, Issue 8, 2631-2645, August 1999
Department of Molecular Biology, Vanderbilt University, Nashville,
Tennessee 37235; and Vanderbilt-Ingram Cancer Center, Nashville,
Tennessee 37232-6838
The Cdc6 protein of budding yeast and its homologues in other
species play an essential role in the initiation of DNA replication. A
cDNA encoding a human homologue of Cdc6 (HsCdc6) has been cloned and
expressed as a fusion protein in a soluble and functionally active
form. The purified protein bound specifically to ATP and slowly
hydrolyzed it, whereas HsCdc6 mutants containing amino acid
substitutions in the Walker A or B motifs were defective. The mutant
proteins retained the ability to bind HsOrc1 and HsCdc6 but displayed
aberrant conformations in the presence of nucleotides. Microinjection
of either mutant protein into human cells in G1 inhibited DNA
replication, suggesting that ATP binding and hydrolysis by HsCdc6 are
essential for DNA replication.
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