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Originally published as MBoC in Press, 10.1091/mbc.E09-04-0264 on September 30, 2009

Vol. 20, Issue 22, 4766-4776, November 15, 2009

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Regulation of the Transcription Factor YY1 in Mitosis through Phosphorylation of Its DNA-binding Domain

Raed Rizkallah, and Myra M. Hurt

Department of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, FL 32306-4300

Submitted April 2, 2009; Revised August 18, 2009; Accepted September 22, 2009
Monitoring Editor: A. Gregory Matera

Yin-Yang 1 (YY1) is a ubiquitously expressed zinc finger transcription factor. It regulates a vast array of genes playing critical roles in development, differentiation, and cell cycle. Very little is known about the mechanisms that regulate the functions of YY1. It has long been proposed that YY1 is a phosphoprotein; however, a direct link between phosphorylation and the function of YY1 has never been proven. Investigation of the localization of YY1 during mitosis shows that it is distributed to the cytoplasm during prophase and remains excluded from DNA until early telophase. Immunostaining studies show that YY1 is distributed equally between daughter cells and rapidly associates with decondensing chromosomes in telophase, suggesting a role for YY1 in early marking of active and repressed genes. The exclusion of YY1 from DNA in prometaphase HeLa cells correlated with an increase in the phosphorylation of YY1 and loss of DNA-binding activity that can be reversed by dephosphorylation. We have mapped three phosphorylation sites on YY1 during mitosis and show that phosphorylation of two of these sites can abolish the DNA-binding activity of YY1. These results demonstrate a novel mechanism for the inactivation of YY1 through phosphorylation of its DNA-binding domain.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E09-04-0264) on September 30, 2009.

Address correspondence to: Myra M. Hurt (myra.hurt{at}med.fsu.edu)






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