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M100007200v1
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Papers In Press, published online ahead of print May 8, 2001
J. Biol. Chem, 10.1074/jbc.M100007200
Submitted on January 2, 2001
Revised on May 8, 2001
Accepted on May 7, 2001

Essential role of Sna41/Cdc45 in loading of DNA polymerase a onto MCM in fission yeast

Masashi Uchiyama, Domonic Griffiths, Ken-ichi Arai, and Hisao Masai

Molecular and Developmental Biology, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639

Corresponding Author: hisao{at}ims.u-tokyo.ac.jp

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 a onto chromatin. The fission yeast cdc45 homologue was identified as a suppressor for nda4, and was named sna41. Nevertheless, it is not known how Cdc45p facilitates loading of DNA polymerase a onto chromatin, in particular to prereplicative complexes. To gain novel insight into function of this protein in fission yeast, we characterized the fission yeast Cdc45 homologue, Sna41p. We have constructed C-terminally epitope tagged Sna41p and Polap 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 followings. Sna41p interacts with Polap throughout 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, sna41goa1, interaction of Polap with Mis5p is not observed, although Polap loading onto the chromatin which occurs before G1-START is not affected. These results show that fission yeast Sna41p facilitates the loading of Polap onto MCM proteins. Our results are consistent with a model that loading of Polap 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 MCM in a cell cycle dependent manner.


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