Misregulated RNA Pol II C-terminal domain phosphorylation results in apoptosis
| Autor: | Orbán Komonyi, Tamas Schauer, Anita Ciurciu, I. Tombácz, Imre Boros |
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| Rok vydání: | 2009 |
| Předmět: |
Male
Apoptosis RNA polymerase II Chromosomal translocation Chromosomes Animals Genetically Modified Cellular and Molecular Neuroscience RNA interference Transcription (biology) Phosphoprotein Phosphatases Animals Drosophila Proteins Humans Transgenes Phosphorylation Molecular Biology Pharmacology Polytene chromosome biology Kinase Cell Biology biology.organism_classification Molecular biology Protein Structure Tertiary Drosophila melanogaster Caspases biology.protein Molecular Medicine Female RNA Polymerase II Tumor Suppressor Protein p53 |
| Zdroj: | Cellular and Molecular Life Sciences. 66:909-918 |
| ISSN: | 1420-9071 1420-682X |
| Popis: | Misregulation of the level of RNA polymerase II carboxyl-terminal domain (CTD) phosphatase, Fcp1, in Drosophila results in high level of caspase-mediated apoptosis. Apoptosis induction by Fcp1 misregulation requires the presence of Drosophila melanogaster (Dm)p53, but occurs without the transcriptional activation of Dmp53 proapoptotic targets rpr, ark, and hid. Overproduction of a transcription activation-defective mutant Dmp53 protein increases, while Dmp53 null background decreases significantly the level of apoptosis in Fcp1-misregulated animals. Generating the apoptotic signal does not require the function of the ATM and Rad3-related kinase (ATR), and no significant level of nucleo-cytoplasmic translocation of Dmp53 is detectable in cells expressing Fcp1 at an abnormal level. Immunostaining of larval salivary gland polytene chromosomes with anti-Dmp53 antibodies indicates Dmp53 localization at several transcriptionally active chromosomal regions in wild-type cells, while in Fcp-misregulated cells the association of Dmp53 with specific chromosomal sites is decreased. |
| Databáze: | OpenAIRE |
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