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J. Biol. Chem., Vol. 276, Issue 28, 26189-26196, July 13, 2001

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Essential Role of Sna41/Cdc45 in Loading of DNA Polymerase  onto Minichromosome Maintenance Proteins in Fission Yeast^*

Masashi Uchiyama^§, Dominic Griffiths^¶, Ken-ichi Arai, and Hisao Masai^**

From the  Department of Molecular and Developmental Biology, Institute for Medical Science, The University of Tokyo, 4-6-1 Shirokanedai Minato-ku, Tokyo 108-8639, Japan, ^¶ Imperial Cancer Research Fund, 44 Lincolns Inn Fields, London WC2A 3PX, United Kingdom, and  Core Research for Evolutional Science and Technology (CREST), Tokyo 108-8639, Japan

Assembly of replication complexes at the replication origins is strictly regulated. Cdc45p is known to be a part of the active replication complexes. In Xenopus egg extracts, Cdc45p was shown to be required for loading of DNA polymerase  onto chromatin. The fission yeast cdc45 homologue was identified as a suppressor for nda4 and named sna41. Nevertheless, it is not known how Cdc45p facilitates loading of DNA polymerase  onto chromatin, particularly to prereplicative complexes. To gain novel insight into the function of this protein in fission yeast, we characterized the fission yeast Cdc45 homologue, Sna41p. We have constructed C-terminally epitope-tagged Sna41p and Polp and replaced the endogenous genes with the corresponding tagged genes. Analyses of protein-protein interactions in vivo by the use of these tagged strains revealed the following: Sna41p interacts with Polp throughout the cell cycle, whereas it interacts with Mis5p/Mcm6p in the chromatin fractions at the G₁-S boundary through S phase. In an initiation-defective sna41 mutant, sna41^goa1, interaction of Polp with Mis5p is not observed, although Polp loading onto the chromatin that occurs before G₁ START is not affected. These results show that fission yeast Sna41p facilitates the loading of Polp onto minichromosome maintenance proteins. Our results are consistent with a model in which loading of Polp onto replication origins occurs through two steps, namely, loading onto chromatin at preSTART and association with prereplicative complexes at G₁-S through Sna41p, which interacts with minichromosome maintenance proteins in a cell cycle-dependent manner.

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