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J Biol Chem, Vol. 273, Issue 34, 22083-22090, August 21, 1998
From the Department of Molecular Biology and Genetics, Johns
Hopkins University School of Medicine, Baltimore, Maryland 21205
Members of the Cdc7 family of protein kinases are
essential for the initiation of DNA replication in all eukaryotes, but
their precise biochemical function is unclear. We have purified the fission yeast Cdc7 homologue Hsk1 approximately 30,000-fold, to near
homogeneity. Purified Hsk1 has protein kinase activity on several
substrates and is capable of autophosphorylation. Point mutations in
highly conserved regions of Hsk1 inactivate the kinase in
vitro and in vivo. Overproduction of two of the
mutant hsk1 alleles blocks initiation of DNA replication
and deranges the mitotic checkpoint, a phenotype consistent with a role
for Hsk1 in the early stages of initiation. The purified Hsk1 kinase
can be separated into two active forms, a Hsk1 monomer and a
heterodimer consisting of Hsk1 complexed with a co-purifying
polypeptide, Dfp1. Association with Dfp1 stimulates phosphorylation of
exogenous substrates but has little effect on autokinase activity. We
have identified Dfp1 as the fission yeast homologue of budding yeast Dbf4. Purified Hsk1 phosphorylates the Cdc19 (Mcm2) subunit of the
six-member minichromosome maintenance protein complex purified from
fission yeast. Since minichromosome maintenance proteins have been
implicated in the initiation of DNA replication, the essential function
of Hsk1 at the G1/S transition may be mediated by
phosphorylation of Cdc19. Furthermore, the phosphorylation of critical
substrates by Hsk1 kinase is likely regulated by association with a
Dbf4-like co-factor.
Purification of Hsk1, a Minichromosome Maintenance Protein Kinase
from Fission Yeast
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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