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J Biol Chem, Vol. 274, Issue 36, 25927-25932, September 3, 1999
From the The binding of mammalian MCM complexes to
chromatin is cell cycle-regulated and under CDC2 kinase negative
control. Here, we investigated the properties of mammalian CDC6
protein, a candidate regulator of MCM. The levels of CDC6 were
relatively constant during the HeLa cell cycle. In asynchronous cells,
CDC6 was mainly detected in the nuclei with immunostaining, but some
CDC6 was not extractable with nonionic detergent. In contrast to the
chromatin-bound MCM, this fraction of CDC6 was resistant to DNase I
treatment, suggesting that it binds to the detergent- and
nuclease-resistant nuclear structure. In S phase cells, CDC6 became
detectable in the cytoplasm with immunostaining; however, the level of
the bound CDC6 was unchanged. In G2/M phase cells,
the level of the bound CDC6 was still maintained, which was
hyperphosphorylated by CDC2 kinase. These data suggest that some CDC6
protein is associated with the specific nuclear structure throughout
the cell cycle and that major binding sites on chromatin differ between
MCM and CDC6. However, co-immunoprecipitation assays with chemical
cross-linking indicated that a small part of the chromatin-bound MCM is
present close to the bound CDC6.
Cell Cycle Regulation of Human CDC6 Protein
INTRACELLULAR LOCALIZATION, INTERACTION WITH THE HUMAN MCM
COMPLEX, AND CDC2 KINASE-MEDIATED HYPERPHOSPHORYLATION
,,,,
Laboratories of Viral Oncology and
¶ Biochemistry, Research Institute, Aichi Cancer Center,
Chikusa-ku, Nagoya 464-8681, Japan
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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