Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2296-9. Epub 2003 Feb 18.

Molecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF.

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Laboratory of Molecular Biophysics and Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.

Abstract

After mRNA transcription termination in eukaryotes, the hyperphosphorylated form of RNA polymerase II (pol II0) must be recycled by TFIIF-associating C-terminal domain phosphatase (FCP1), the phosphatase responsible for dephosphorylating the C-terminal domain of the largest polymerase subunit. Transcription factor (TF)-IIF stimulates the activity of FCP1, and the RNA polymerase II-associating protein 74 subunit of TFIIF forms a complex with FCP1 in both human and yeast. Here, we report a cocrystal structure of the winged-helix domain of human RNA polymerase II-associating protein 74 bound to the alpha-helical C terminus of human FCP1 (residues 944-961). These results illustrate the molecular mechanism by which TFIIF efficiently recruits FCP1 to the pol II transcription machinery for recycling of the polymerase.

PMID:: 12591941; [PubMed - indexed for MEDLINE]
PMCID:: PMC151334

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Structures reported by this article

Crystal Structure Of Rap74 C-Terminal Domain Complexed With Fcp1 C-Terminal Peptide

PDB: 1J2X

Source: Homo sapiens, synthetic construct

Method: X-Ray Diffraction

Resolution: 2 Å

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Molecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF.
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