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Publication : A common mechanism for mitotic inactivation of C2H2 zinc finger DNA-binding domains.

First Author  Dovat S Year  2002
Journal  Genes Dev Volume  16
Issue  23 Pages  2985-90
PubMed ID  12464629 Mgi Jnum  J:80511
Mgi Id  MGI:2445991 Doi  10.1101/gad.1040502
Citation  Dovat S, et al. (2002) A common mechanism for mitotic inactivation of C2H2 zinc finger DNA-binding domains. Genes Dev 16(23):2985-90
abstractText  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.
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