The disordered C-terminus of the RNA Polymerase II phosphatase FCP1 is partially helical in the unbound state

Chad W. Lawrence, Alain Bonny, Scott A. Showalter

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Intrinsically disordered proteins (IDPs) lack unique 3D structures under native conditions and yet retain critical functions. Recycling of RNA Polymerase II after transcription is promoted by an interaction between the winged helix domain of RAP74, a component of the general transcription factor IIF (TFIIF), and the C-terminus of the TFIIF-associating CTD phosphatase (FCP1). Sixteen residues from the C-terminus of FCP1 form an α-helix in the complex, but the protein is otherwise agreed in the literature to be intrinsically disordered. Here we show through CD and recently developed carbon-detected NMR that, although FCP1 is intrinsically disordered, the above 16 residues composing the RAP74 binding surface form nascent α-helical structure in the unbound state. We further show retention of general FCP1 disorder and the nascent helical content in HeLa extract, establishing cellular relevance. The conformational bias observed leads to a mechanistic proposal for FCP1's transition from a disordered ensemble to an ordered conformation upon binding.

Original languageEnglish (US)
Pages (from-to)461-465
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume410
Issue number3
DOIs
StatePublished - Jul 8 2011

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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