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

Sinisa Dovat, Tapani Ronni, Dana Russell, Roger Ferrini, Bradley S. Cobb, Stephen T. Smale

Research output: Contribution to journalArticlepeer-review

98 Scopus citations

Abstract

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 Spl was also phosphorylated, suggesting that linker phosphorylation provides a global mechanism for inactivation of the C2H2 family.

Original languageEnglish (US)
Pages (from-to)2985-2990
Number of pages6
JournalGenes and Development
Volume16
Issue number23
DOIs
StatePublished - Dec 1 2002

All Science Journal Classification (ASJC) codes

  • Genetics
  • Developmental Biology

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