期刊
NUCLEIC ACIDS RESEARCH
卷 43, 期 17, 页码 8258-8267出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkv740
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资金
- Japan Science and Technology Agency
- Japan Society for the Promotion of Science [25711001]
- Takeda Science Foundation
- Kanae Foundation for the Promotion of Medical Science
- Astellas Foundation for Research on Metabolic Disorders
- Human Frontier Science Program [RGY0080/2013]
- Grants-in-Aid for Scientific Research [25711001] Funding Source: KAKEN
Phosphorylation of the C-terminal domain of the largest subunit of RNA polymerase II (Pol II), especially Ser2 and Ser5 residues, plays important roles in transcription and mRNA processing, including 5' end capping, splicing and 3' end processing. These phosphorylation events stimulate mRNA processing, however, it is not clear whether splicing activity affects the phosphorylation status of Pol II. In this study, we found that splicing inhibition by potent splicing inhibitors spliceostatin A (SSA) and pladienolide B or by antisense oligos against snRNAs decreased phospho-Ser2 level, but had little or no effects on phospho-Ser5 level. In contrast, transcription and translation inhibitors did not decrease phospho-Ser2 level, therefore inhibition of not all the gene expression processes cause the decrease of phospho-Ser2. SSA treatment caused early dissociation of Pol II and decrease in phospho-Ser2 level of chromatin-bound Pol II, suggesting that splicing inhibition causes downregulation of phospho-Ser2 through at least these two mechanisms.
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