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Vol. 13, Issue 5, 1462-1472, May 2002
Department of Biology, Graduate School of Science, Osaka
University, Osaka 560-0043, Japan
Initiation of DNA replication in eukaryotic cells is regulated
through the ordered assembly of replication complexes at origins of
replication. Association of Cdc45 with the origins is a crucial step in
assembly of the replication machinery, hence can be considered a target
for the regulation of origin activation. To examine the process
required for SpCdc45 loading, we isolated fission yeast SpSld3, a
counterpart of budding yeast Sld3 that interacts with Cdc45. SpSld3
associates with the replication origin during G1-S phases and this
association depends on Dbf4-dependent (DDK) kinase activity. In
the corresponding period, SpSld3 interacts with minichromosome maintenance (MCM) proteins and then with SpCdc45. A
temperature-sensitive sld3-10 mutation suppressed by the
multicopy of the sna41+ encoding
SpCdc45 impairs loading of SpCdc45 onto chromatin. In addition, this
mutation leads to dissociation of preloaded Cdc45 from chromatin in the
hydroxyurea-arrested S phase, and DNA replication upon removal of
hydroxyurea is retarded. Thus, we conclude that SpSld3 is required for
stable association of Cdc45 with chromatin both in initiation and
elongation of DNA replication. The DDK-dependent origin association
suggests that SpSld3 is involved in temporal regulation of origin firing.
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