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The casein kinase I (CKI) gene family is a rapidly enlarging
group whose members have been implicated in the control of cytoplasmic
and nuclear processes, including DNA replication and repair. We report
here the cloning and characterization of a novel isoform of CKI from a
human placental cDNA library. The cDNA for this isoform, hCKI
Volume 270,
Number 25,
Issue of June 23, pp. 14875-14883, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
(CKI), a Novel Member of the CKI Gene Family
,
predicts a basic polypeptide of 416 amino acids and a molecular mass of
47.3 kDa. It encodes a core kinase domain of 285 amino acids and a
carboxyl-terminal tail of 123 amino acids. The kinase domain is
53-98% identical to the kinase domains of other CKI family
members and is most closely related to the
isoform. Localization
of the hCKI
gene to chromosome 22q12-13 and the hCKI
gene to chromosome 17q25 confirms that these are distinct genes in the
CKI family. Northern blot analysis shows that hCKI
is expressed in
multiple human cell lines. Recombinant hCKI
is an active enzyme
that phosphorylates known CKI substrates including a CKI-specific
peptide substrate and is inhibited by CKI-7, a CKI-specific inhibitor.
A budding yeast isoform of CKI, HRR25, has been implicated in DNA
repair responses. Expression of hCKI
but not hCKI
rescued the
slow-growth phenotype of a Saccharomyces cerevisiae strain
with a deletion of HRR25. Human CKI is a novel CKI isoform with
properties that overlap those of previously described CKI isoforms.
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