Bromodomain factor 1 (Bdf1) is phosphorylated by protein kinase CK2.
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.
Sawa
Chika
C
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Nedea
Eduard
E
Krogan
Nevan
N
Wada
Tadashi
T
Handa
Hiroshi
H
Greenblatt
Jack
J
Buratowski
Stephen
S
D047390:Casein Kinase II; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D035362:Transcription Factor TFIID / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*; D000092468:Bromodomain Containing Proteins
D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases; D029701:Saccharomyces cerevisiae Proteins; D035362:Transcription Factor TFIID; D014157:Transcription Factors; C091342:BDF1 protein, S cerevisiae; D000092468:Bromodomain Containing Proteins