This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Sawa, C. Articles by Buratowski, S. Search for Related Content PubMed PubMed Citation Articles by Sawa, C. Articles by Buratowski, S.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, June 2004, p. 4734-4742, Vol. 24, No. 11
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.11.4734-4742.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Bromodomain Factor 1 (Bdf1) Is Phosphorylated by Protein Kinase CK2

Chika Sawa,¹ Eduard Nedea,² Nevan Krogan,² Tadashi Wada,³ Hiroshi Handa,³ Jack Greenblatt,² and Stephen Buratowski^1*

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115,¹ Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6, Canada,² Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Yokohama 226-8501, Japan³

Received 21 January 2004/ Returned for modification 27 February 2004/ Accepted 16 March 2004

Bromodomain factor 1 (Bdf1) associates with Saccharomyces cerevisiae TFIID and corresponds to the C-terminal half of higher eukaryotic TAF1. It also associates with the SWR-C complex, which is important for Htz1 deposition. Bdf1 binds preferentially to acetylated histone H4. Bdf1 is phosphorylated, but the mechanism and significance of this modification have been unclear. Two distinct regions within Bdf1 are phosphorylated; one is just C terminal to the bromodomains and the other is near the C terminus. Mutational analysis shows that phosphorylation is necessary for Bdf1 function in vivo. Endogenous protein kinase CK2 purifies with Bdf1 and phosphorylates both domains. A similar mechanism may be responsible for phosphorylation of the C-terminal region of mammalian TAF1. These findings suggest that CK2 phosphorylation of Bdf1 may regulate RNA polymerase II transcription and/or chromatin structure.

---

* Corresponding author. Mailing address: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115. Phone: (617) 432-0696. Fax: (617) 738-0516. E-mail: SteveB{at}hms.harvard.edu.

---

Molecular and Cellular Biology, June 2004, p. 4734-4742, Vol. 24, No. 11
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.11.4734-4742.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Prather, D., Krogan, N. J., Emili, A., Greenblatt, J. F., Winston, F. (2005). Identification and Characterization of Elf1, a Conserved Transcription Elongation Factor in Saccharomyces cerevisiae. Mol. Cell. Biol. 25: 10122-10135 [Abstract] [Full Text]  
• Utley, R. T., Lacoste, N., Jobin-Robitaille, O., Allard, S., Cote, J. (2005). Regulation of NuA4 Histone Acetyltransferase Activity in Transcription and DNA Repair by Phosphorylation of Histone H4. Mol. Cell. Biol. 25: 8179-8190 [Abstract] [Full Text]  
• Boyer-Guittaut, M., Birsoy, K., Potel, C., Elliott, G., Jaffray, E., Desterro, J. M., Hay, R. T., Oelgeschlager, T. (2005). SUMO-1 Modification of Human Transcription Factor (TF) IID Complex Subunits: INHIBITION OF TFIID PROMOTER-BINDING ACTIVITY THROUGH SUMO-1 MODIFICATION OF hsTAF5. J. Biol. Chem. 280: 9937-9945 [Abstract] [Full Text]  
• Auty, R., Steen, H., Myers, L. C., Persinger, J., Bartholomew, B., Gygi, S. P., Buratowski, S. (2004). Purification of Active TFIID from Saccharomyces cerevisiae: EXTENSIVE PROMOTER CONTACTS AND CO-ACTIVATOR FUNCTION. J. Biol. Chem. 279: 49973-49981 [Abstract] [Full Text]