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Vol. 16, No. 23, pp. 2985-2990, December 1, 2002
1 Howard Hughes Medical Institute, Department of
Microbiology, Immunology, and Molecular Genetics, and
2 Department of Pediatrics, University of California,
Los Angeles, California 90095, USA
Many nuclear proteins are inactivated during
mitotic entry, presumably as a prerequisite to
chromatin condensation and cell division. C2H2 zinc fingers define the
largest transcription factor family in the human proteome. The linker
separating finger motifs is highly conserved and resembles TGEKP in
more than 5000 occurrences. However, the reason for this conservation
is not fully understood. We demonstrate that all three linkers in the
DNA-binding domain of Ikaros are phosphorylated during mitosis.
Phosphomimetic substitutions abolished DNA-binding and pericentromeric
localization. A linker within Sp1 was also phosphorylated, suggesting
that linker phosphorylation provides a global mechanism for
inactivation of the C2H2 family.
[Key Words: Zinc finger; mitosis; phosphorylation; Ikaros; cell cycle]
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