UBF在丝氨酸388处的磷酸化是与RNA聚合酶I相互作用及rDNA转录激活所必需的。
Phosphorylation of UBF at serine 388 is required for interaction with RNA polymerase I and activation of rDNA transcription.
作者信息
Voit R, Grummt I
机构信息
Division of Molecular Biology of the Cell II, German Cancer Research Center, D-69120 Heidelberg, Germany.
出版信息
Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13631-6. doi: 10.1073/pnas.231071698. Epub 2001 Nov 6.
Abstract
Modulation of the activity of the upstream binding factor (UBF) plays a key role in cell cycle-dependent regulation of rRNA synthesis. Activation of rDNA transcription on serum stimulation requires phosphorylation of UBF at serine 484 by G(1)-specific cyclin-dependent kinase (cdk)/cyclin complexes. After G(1) progression UBF is phosphorylated at serine 388 by cdk2/cyclin E and cdk2/cyclin A. Conversion of serine 388 to glycine abolishes UBF activity, whereas substitution by aspartate enhances the transactivating function of UBF. Protein-protein interaction studies reveal that phosphorylation at serine 388 is required for the interaction between RNA polymerase I and UBF. The results suggest that phosphorylation of UBF represents a powerful means of modulating the assembly of the transcription initiation complex in a proliferation- and cell cycle-dependent fashion.
摘要
上游结合因子（UBF）活性的调节在rRNA合成的细胞周期依赖性调控中起关键作用。血清刺激时rDNA转录的激活需要G(1)特异性细胞周期蛋白依赖性激酶（cdk）/细胞周期蛋白复合物将UBF的丝氨酸484磷酸化。在G(1)期进展后，UBF被cdk2/细胞周期蛋白E和cdk2/细胞周期蛋白A在丝氨酸388处磷酸化。丝氨酸388转换为甘氨酸会消除UBF活性，而天冬氨酸替代则增强UBF的反式激活功能。蛋白质-蛋白质相互作用研究表明，RNA聚合酶I与UBF之间的相互作用需要丝氨酸388处的磷酸化。结果表明，UBF的磷酸化是以增殖和细胞周期依赖性方式调节转录起始复合物组装的有力手段。
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本文引用的文献
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Cell cycle-dependent regulation of RNA polymerase I transcription: the nucleolar transcription factor UBF is inactive in mitosis and early G1.RNA聚合酶I转录的细胞周期依赖性调控：核仁转录因子UBF在有丝分裂和G1早期无活性。
Proc Natl Acad Sci U S A. 1999 May 25;96(11):6096-101. doi: 10.1073/pnas.96.11.6096.
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Phosphorylation by G1-specific cdk-cyclin complexes activates the nucleolar transcription factor UBF.G1特异性细胞周期蛋白依赖性激酶-细胞周期蛋白复合物的磷酸化作用激活核仁转录因子UBF。
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