TFIIF-associating carboxyl-terminal domain phosphatase dephosphorylates phosphoserines 2 and 5 of RNA polymerase II
- PMID: 12351650
- DOI: 10.1074/jbc.M208588200
TFIIF-associating carboxyl-terminal domain phosphatase dephosphorylates phosphoserines 2 and 5 of RNA polymerase II
Abstract
The carboxyl-terminal domain (CTD) of the largest RNA polymerase (RNAP) II subunit undergoes reversible phosphorylation throughout the transcription cycle. The unphosphorylated form of RNAP II is referred to as IIA, whereas the hyperphosphorylated form is known as IIO. Phosphorylation occurs predominantly at serine 2 and serine 5 within the CTD heptapeptide repeat and has functional implications for RNAP II with respect to initiation, elongation, and transcription-coupled RNA processing. In an effort to determine the role of the major CTD phosphatase (FCP1) in regulating events in transcription that appear to be influenced by serine 2 and serine 5 phosphorylation, the specificity of FCP1 was examined. FCP1 is capable of dephosphorylating heterogeneous RNAP IIO populations of HeLa nuclear extracts. The extent of dephosphorylation at specific positions was assessed by immunoreactivity with monoclonal antibodies specific for phosphoserine 2 or phosphoserine 5. As an alternative method to assess FCP1 specificity, RNAP IIO isozymes were prepared in vitro by the phosphorylation of purified calf thymus RNAP IIA with specific CTD kinases and used as substrates for FCP1. FCP1 dephosphorylates serine 2 and serine 5 with comparable efficiency. Accordingly, the specificity of FCP1 is sufficiently broad to dephosphorylate RNAP IIO at any point in the transcription cycle irrespective of the site of serine phosphorylation within the consensus repeat.
Similar articles
-
Dephosphorylation of RNA polymerase II by CTD-phosphatase FCP1 is inhibited by phospho-CTD associating proteins.J Mol Biol. 2004 Jan 9;335(2):415-24. doi: 10.1016/j.jmb.2003.10.036. J Mol Biol. 2004. PMID: 14672652
-
Enhanced binding of RNAP II CTD phosphatase FCP1 to RAP74 following CK2 phosphorylation.Biochemistry. 2005 Mar 1;44(8):2732-45. doi: 10.1021/bi047958h. Biochemistry. 2005. PMID: 15723518
-
FCP1 phosphorylation by casein kinase 2 enhances binding to TFIIF and RNA polymerase II carboxyl-terminal domain phosphatase activity.J Biol Chem. 2002 Sep 27;277(39):36061-7. doi: 10.1074/jbc.M205192200. Epub 2002 Jul 22. J Biol Chem. 2002. PMID: 12138108
-
Regulation of RNA polymerase II activity by CTD phosphorylation and cell cycle control.J Cell Physiol. 2002 Feb;190(2):160-9. doi: 10.1002/jcp.10058. J Cell Physiol. 2002. PMID: 11807820 Review.
-
Cell cycle regulation and RNA polymerase II.Front Biosci. 2000 Feb 1;5:D244-57. doi: 10.2741/bregman. Front Biosci. 2000. PMID: 10704151 Review.
Cited by
-
TFIIH: when transcription met DNA repair.Nat Rev Mol Cell Biol. 2012 May 10;13(6):343-54. doi: 10.1038/nrm3350. Nat Rev Mol Cell Biol. 2012. PMID: 22572993 Review.
-
Arabidopsis C-terminal domain phosphatase-like 1 and 2 are essential Ser-5-specific C-terminal domain phosphatases.Proc Natl Acad Sci U S A. 2004 Oct 5;101(40):14539-44. doi: 10.1073/pnas.0403174101. Epub 2004 Sep 23. Proc Natl Acad Sci U S A. 2004. PMID: 15388846 Free PMC article.
-
Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes.Mol Cell Biol. 2008 Jan;28(2):609-18. doi: 10.1128/MCB.01356-07. Epub 2007 Nov 12. Mol Cell Biol. 2008. PMID: 17998332 Free PMC article.
-
The structure of Fcp1, an essential RNA polymerase II CTD phosphatase.Mol Cell. 2008 Nov 21;32(4):478-90. doi: 10.1016/j.molcel.2008.09.021. Mol Cell. 2008. PMID: 19026779 Free PMC article.
-
Functional interactions of RNA-capping enzyme with factors that positively and negatively regulate promoter escape by RNA polymerase II.Proc Natl Acad Sci U S A. 2004 May 18;101(20):7572-7. doi: 10.1073/pnas.0401493101. Epub 2004 May 10. Proc Natl Acad Sci U S A. 2004. PMID: 15136722 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Research Materials
