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CTD-Phosphatase
ββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββ
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Die CTD-Phosphatase (FCP1) (genauer TFIIF-assoziierende CTD-Phosphatase) ist das Enzym, das in Eukaryoten wΓ€hrend der Transkription die Phosphatreste von Serin-2 und Serin-5 der Polymerase II entfernt, womit die Polymerase fΓΌr die Elongation (re-)aktiviert wird. Es handelt sich also um eine Phosphatase. Das Enzym ist beim Menschen in allen Gewebetypen zu finden. Mutationen im entsprechenden CTDP1-Gen kΓΆnnen zu erblichen multiplen EntwicklungsstΓΆrungen mit Katarakt, dem sogenannten CCFDN-Syndrom fΓΌhren.cite-ref-2[2]
Um ihre volle AktivitΓ€t zu erhalten, wird die CTD-Phosphatase selbst von Caseinkinase 2 phosphoryliert, und benΓΆtigt die RAP74-Untereinheit von TFIIF als Cofaktor.cite-ref-3[3]cite-ref-4[4]
Contents
β’ Weblinks
β’ Einzelnachweise
ββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββ
Weblinks
β’ Eintrag zu Kongenitale Katarakt-Gesichtsdysmorphie-Neuropathie-Syndrom. In: Orphanet (Datenbank fΓΌr seltene Krankheiten)
β’ Gopinathrao / reactome: Hypophosphorylation of RNA Pol II CTD by FCP1P protein
Einzelnachweise
cite-note-11. InterPro-Eintrag
cite-note-33. β Ao Yang, Karen L. Abbott, Alexandre Desjardins, Paola Di Lello, James G. Omichinski, Pascale Legault: NMR Structure of a Complex Formed by the Carboxyl-Terminal Domain of Human RAP74 and a Phosphorylated Peptide from the Central Domain of the FCP1 Phosphatase. In: Biochemistry. 48. Jahrgang, Nr. 9, 10. MΓ€rz 2009, S. 1964β1974, doi:10.1021/bi801549m, PMID 19215094 (englisch).
cite-note-44. β Karen L. Abbott, Matthew B. Renfrow, Michael J. Chalmers, Bao D. Nguyen, Alan G. Marshall, Pascale Legault, James G. Omichinski: Enhanced Binding of RNAP II CTD Phosphatase FCP1 to RAP74 Following CK2 Phosphorylation. In: Biochemistry. 44. Jahrgang, Nr. 8, 1. MΓ€rz 2005, S. 2732β2745, doi:10.1021/bi047958h, PMID 15723518 (englisch).
cite-note-55. β Benoit Palancade, Nicholas F. Marshall, Alexandre Tremeau-Bravard, Olivier Bensaude, Michael E. Dahmus, Marie-Francoise Dubois: Dephosphorylation of RNA Polymerase II by CTD-phosphatase FCP1 is Inhibited by Phospho-CTD Associating Proteins. In: Journal of Molecular Biology. 335. Jahrgang, Nr. 2, 9. Januar 2004, S. 415β24, doi:10.1016/j.jmb.2003.10.036, PMID 14672652 (englisch).
cite-note-66. β Stefano Amente, Giuliana Napolitano, Paolo Licciardo, Maria Monti, Piero Pucci, Luigi Lania, Barbara Majello: Identification of proteins interacting with the RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylation. In: FEBS Letters. 579. Jahrgang, Nr. 3, 31. Januar 2005, S. 683β689, doi:10.1016/j.febslet.2004.12.045, PMID 15670829 (englisch).
cite-note-77. β Karen L. Abbott, Jacques Archambault, Hua Xiao, Bao D. Nguyen, Robert G. Roeder, Jack Greenblatt, James G. Omichinski, Pascale Legault: Interactions of the HIV-1 Tat and RAP74 Proteins with the RNA Polymerase II CTD Phosphatase FCP1β . In: Biochemistry. 44. Jahrgang, Nr. 8, 1. MΓ€rz 2005, S. 2716β2731, doi:10.1021/bi047957p, PMID 15723517 (englisch).