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MBC in Press, published online ahead of print March 15, 2006
Mol. Biol. Cell 10.1091/mbc.E05-10-0923

A more recent version of this article appeared on June 1, 2006 Originally published as MBC in Press, 10.1091/mbc.E05-10-0923 on April 5, 2006
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Submitted on October 5, 2005
Revised on February 27, 2006
Accepted on March 7, 2006

Compartmentation of the Nucleolar Processing Proteins in the Granular Component is a CK2-driven Process

Emilie Louvet,* Henriette Roberte Junéra,* Isabelle Berthuy, and Danièle Hernandez-Verdun

Institut Jacques Monod, CNRS, University Paris VI and Paris VII, 75251 Paris Cedex 05, France

Monitoring Editor: A. Gregory Matera

To analyze the compartmentation of nucleolar protein complexes, the mechanisms controlling targeting of nucleolar processing proteins onto rRNA transcription sites has been investigated. We studied the reversible disconnection of transcripts and processing proteins using digitonin-permeabilized cells in assays capable of promoting nucleolar reorganization. The assays show that the dynamics of nucleolar reformation is ATP/GTP-dependent, sensitive to temperature, and CK2-driven. We further demonstrate the role of CK2 on the rRNA processing protein B23. Mutation of the major CK2 site on B23 induces reorganization of nucleolar components that separate from each other. This was confirmed in assays using extracts containing B23 mutated in the CK2 binding sites. We propose that phosphorylation controls the compartmentation of the rRNA processing proteins and that CK2 is involved in this process.

*These authors contributed equally to this work.

Address correspondence to: Danièle Hernandez-Verdun (dhernand{at}ccr.jussieu.fr)




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