Involvement of phosphatidylinositol 4,5-bisphosphate in RNA polymerase I transcription
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
23591814
DOI
10.1242/jcs.123661
PII: jcs.123661
Knihovny.cz E-resources
- Keywords
- Fibrillarin, Nucleolus, PIP2, Transcription, UBF,
- MeSH
- Cell Nucleolus genetics metabolism MeSH
- Chromosomal Proteins, Non-Histone genetics metabolism MeSH
- DNA-Binding Proteins genetics metabolism MeSH
- Phosphatidylinositol 4,5-Diphosphate genetics metabolism MeSH
- Transcription, Genetic genetics MeSH
- HeLa Cells MeSH
- Humans MeSH
- Cell Line, Tumor MeSH
- RNA Precursors genetics metabolism MeSH
- Promoter Regions, Genetic genetics MeSH
- RNA Polymerase I genetics metabolism MeSH
- Pol1 Transcription Initiation Complex Proteins genetics metabolism MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Chromosomal Proteins, Non-Histone MeSH
- DNA-Binding Proteins MeSH
- fibrillarin MeSH Browser
- Phosphatidylinositol 4,5-Diphosphate MeSH
- RNA Precursors MeSH
- RNA Polymerase I MeSH
- transcription factor UBF MeSH Browser
- Pol1 Transcription Initiation Complex Proteins MeSH
RNA polymerase I (Pol I) transcription is essential for the cell cycle, growth and protein synthesis in eukaryotes. In the present study, we found that phosphatidylinositol 4,5-bisphosphate (PIP2) is a part of the protein complex on the active ribosomal promoter during transcription. PIP2 makes a complex with Pol I and the Pol I transcription factor UBF in the nucleolus. PIP2 depletion reduces Pol I transcription, which can be rescued by the addition of exogenous PIP2. In addition, PIP2 also binds directly to the pre-rRNA processing factor fibrillarin (Fib), and co-localizes with nascent transcripts in the nucleolus. PIP2 binding to UBF and Fib modulates their binding to DNA and RNA, respectively. In conclusion, PIP2 interacts with a subset of Pol I transcription machinery, and promotes Pol I transcription.
References provided by Crossref.org
Lamin A/C and PI(4,5)P2-A Novel Complex in the Cell Nucleus
LIPRNAseq: a method to discover lipid interacting RNAs by sequencing
PIP2-Effector Protein MPRIP Regulates RNA Polymerase II Condensation and Transcription
Tidying-up the plant nuclear space: domains, functions, and dynamics
Super-Resolution Localisation of Nuclear PI(4)P and Identification of Its Interacting Proteome
Fibrillarin Ribonuclease Activity is Dependent on the GAR Domain and Modulated by Phospholipids
Nuclear Phosphoinositides-Versatile Regulators of Genome Functions
Multiple Aspects of PIP2 Involvement in C. elegans Gametogenesis
Phospholipids and inositol phosphates linked to the epigenome
Novel Ribonuclease Activity Differs between Fibrillarins from Arabidopsis thaliana
Tools for visualization of phosphoinositides in the cell nucleus
Fibrillarin methylates H2A in RNA polymerase I trans-active promoters in Brassica oleracea
Simultaneous detection of multiple targets for ultrastructural immunocytochemistry