文章基本信息

标题：Phosphorylation of UBF at serine 388 is required for interaction with RNA polymerase I and activation of rDNA transcription
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作者：Renate Voit ; Ingrid Grummt
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2001
卷号：98
期号：24
页码：13631-13636
DOI：10.1073/pnas.231071698
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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 G1-specific cyclin-dependent kinase (cdk)/cyclin complexes. After G1 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.