Journal
MOLECULAR CELL
Volume 6, Issue 3, Pages 637-648Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(00)00062-9
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Funding
- NCI NIH HHS [CA17542] Funding Source: Medline
- NIGMS NIH HHS [GM07232] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA017542, R37CA017542] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM007232] Funding Source: NIH RePORTER
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Cdc6/Cdc18 is a conserved and essential component of prereplication complexes. The 2.0 Angstrom crystal structure of an archaeal Cdc6 ortholog, in conjunction with a mutational analysis of the homologous Cdc18 protein from Schizosaccharomyces pombe, reveals novel aspects of Cdc6/Cdc18 function. Two domains of Cdc6 form an AAA(+)-type nucleotide binding fold that is observed bound to Mg ADP. A third domain adopts a winged-helix fold similar to known DNA binding modules. Sequence comparisons show that the winged-helix domain is conserved in Orc1, and mutagenesis data demonstrate that this region of Cdc6/Cdc18 is required for function in vivo. Additional mutational analyses suggest that nucleotide binding and/or hydrolysis by Cdc6/Cdc18 is required not only for progression through S phase, but also for maintenance of checkpoint control during S phase.
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