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

机译：Bromodomain因子1（Bdf1）被蛋白激酶CK2磷酸化。

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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.
机译：溴结构域因子1（Bdf1）与酿酒酵母 TFIID相关，并对应于高等真核TAF1的C端一半。它还与SWR-C复合物相关，这对Htz1沉积很重要。 Bdf1优先绑定到乙酰化的组蛋白H4。 Bdf1被磷酸化，但这种修饰的机制和意义尚不清楚。 Bdf1中的两个不同区域被磷酸化;一个仅在溴结构域的C末端，另一个在C末端附近。突变分析表明磷酸化是体内Bdf1功能所必需的。内源蛋白激酶CK2用Bdf1纯化并磷酸化两个结构域。类似的机制可能是哺乳动物TAF1 C端区域磷酸化的原因。这些发现表明Bdf1的CK2磷酸化可能调节RNA聚合酶II转录和/或染色质结构。

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