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Details on Person Genetic studies in S. cerevisiae indicate that wild-type Cdc...
| Class:Id | Summation:68851 |
|---|---|
| _displayName | Genetic studies in S. cerevisiae indicate that wild-type Cdc... |
| _timestamp | 0000-00-00 00:00:00 |
| literatureReference | [LiteratureReference:68852] Persistent initiation of DNA replication and chromatin-bound MCM proteins during the cell cycle in cdc6 mutants. [LiteratureReference:68692] ATPase switches controlling DNA replication initiation. [LiteratureReference:68854] The Cdc6 nucleotide-binding site regulates its activity in DNA replication in human cells. [LiteratureReference:68858] Xenopus Cdc6 performs separate functions in initiating DNA replication [LiteratureReference:68863] Mechanisms of DNA replication. |
| text | Genetic studies in S. cerevisiae indicate that wild-type Cdc6 function is required for correctly timed loading of Mcm2-7 onto ORC. Biochemical studies indicate that the human and Xenopus Cdc6 proteins likewise are required for Mcm2-7 loading, and that they are ATPase switches. Specifically, Cdc6 may function as a clamp loader, assembling Mcm2-7 onto DNA in an ATP-dependent reaction. All known Cdc6 proteins have the Walker A and Walker B sequence motifs characteristic of the AAA+ superfamily of ATPases. As expected for an AAA+ protein, human Cdc6 binds and slowly hydrolyzes ATP in vitro. ATP hydrolysis was disrupted by mutations of the Walker B motif, while both binding and hydrolysis were disrupted by Walker A mutations. Microinjection of either mutant protein into HeLa cells blocked their progression through S phase. Both wild-type and mutant proteins can dimerize in vitro, and studies with Xenopus egg extracts suggest that Cdc6 functions in vivo as a dimer or larger multimer. In Xenopus extracts depleted of Cdc6 and reconstituted with either mutant protein, recruitment of Mcm2-7 to chromatin failed. |
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