Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control.
Mol Cell
; 6(3): 637-48, 2000 Sep.
Article
em En
| MEDLINE
| ID: mdl-11030343
ABSTRACT
Cdc6/Cdc18 is a conserved and essential component of prereplication complexes. The 2.0 A 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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Base de dados:
MEDLINE
Assunto principal:
Fase S
/
Origem de Replicação
/
Proteínas de Ciclo Celular
/
Proteínas de Saccharomyces cerevisiae
Idioma:
En
Ano de publicação:
2000
Tipo de documento:
Article