Getting a grip on licensing: mechanism of stable Mcm2-7 loading onto replication origins.
A recent Molecular Cell paper by Randell et al. (2006) sheds light on the role of ATP hydrolysis by Cdc6 in promoting the stable loading of the Mcm2-7 complex onto origins of DNA replication.
Cvetic
Christin A
CA
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02446, USA.
Walter
Johannes C
JC
D000255:Adenosine Triphosphate; D018797:Cell Cycle Proteins / Q000378:metabolism*; D002868:Chromosomal Proteins, Non-Histone; D004261:DNA Replication; D004268:DNA-Binding Proteins / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D064168:Minichromosome Maintenance Complex Component 7; D008954:Models, Biological; D009687:Nuclear Proteins / Q000378:metabolism*; D051738:Origin Recognition Complex / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
C066503:CDC6 protein, S cerevisiae; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D009687:Nuclear Proteins; D051738:Origin Recognition Complex; D029701:Saccharomyces cerevisiae Proteins; D000255:Adenosine Triphosphate; C069199:MCM2 protein, S cerevisiae; C491088:MCM7 protein, S cerevisiae; D064168:Minichromosome Maintenance Complex Component 7