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

Biochemical and Biophysical Research Communications

Volumn 410, Issue 3, 2011, Pages 461-465

  Lawrence, Chad W ^a   Bonny, Alain ^a   Showalter, Scott A ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

Circular dichroism; FCP1; Intrinsically disordered protein; NMR; RNA polymerase; Trifluoroethanol

Indexed keywords

CELL EXTRACT; CELL PROTEIN; HELA EXTRACT; INTRINSICALLY DISORDERED PROTEIN; RAP74 PROTEIN; RNA POLYMERASE II; TFIIF ASSOCIATING COMPONENT OF THE RNA POLYMERASE II C TERMINAL DOMAIN PHOSPHATASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR IIF; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME MECHANISM; GENETIC TRANSCRIPTION; HELA CELL; HUMAN; HUMAN CELL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; SURFACE PROPERTY; THREE DIMENSIONAL IMAGING;

CELL EXTRACTS; CIRCULAR DICHROISM; DEXTRANS; HELA CELLS; HUMANS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEAR PROTEINS; PHOSPHOPROTEIN PHOSPHATASES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; TRANSCRIPTION FACTORS, TFII; UREA;

EID: 79960040425     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.05.160     Document Type: Article

References (28)

1. Dunker A.K., Oldfield C.J., Meng J., Romero P., Yang J.Y., Chen J.W., Vacic V., Obradovic Z., Uversky V.N. The unfoldomics decade: an update on intrinsically disordered proteins. BMC Genomics 2008, 9(Suppl. 2):S1.
2. Fuxreiter M., Tompa P., Simon I., Uversky V.N., Hansen J.C., Asturias F.J. Malleable machines take shape in eukaryotic transcriptional regulation. Nat. Chem. Biol. 2008, 4:728-737.
3. Sugase K., Dyson H.J., Wright P.E. Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 2007, 447:1021-1025.
4. Csermely P., Palotai R., Nussinov R. Induced fit, conformational selection and independent dynamic segments: an extended view of binding events. Trends Biochem. Sci. 2010, 35:539-546.
5. Uversky V.N. Seven lessons from one IDP structural analysis. Structure 2010, 18:1069-1071.
6. Meinhart A., Kamenski T., Hoeppner S., Baumli S., Cramer P. A structural perspective of CTD function. Genes Dev. 2005, 19:1401-1415.
7. Archambault J., Pan G.H., Dahmus G.K., Cartier M., Marshall N., Zhang S., Dahmus M.E., Greenblatt J. FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO. J. Biol. Chem. 1998, 273:27593-27601.
8. Kamada K., Roeder R.G., Burley S.K. Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF. Proc. Natl. Acad. Sci. USA 2003, 100:2296-2299.
9. Nguyen B.D., Abbott K.L., Potempa K., Kobort M.S., Archambault J., Greenblatt J., Legault P., Omichinski J.G. NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1. Proc. Natl. Acad. Sci. USA 2003, 100:5688-5693.
10. Dyson H.J., Wright P.E. Unfolded proteins and protein folding studied by NMR. Chem. Rev. 2004, 104:3607-3622.
11. Jensen M.R., Salmon L., Nodet G., Blackledge M. Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts. J. Am. Chem. Soc. 2010, 132:1270-1272.
12. Bolen D.W., Baskakov I.V. The osmophobic effect: natural selection of a thermodynamic force in protein folding. J. Mol. Biol. 2001, 310:955-963.
13. Zhou H.X., Rivas G., Minton A.P. Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences. Annu. Rev. Biophys. 2008, 37:375-397.
14. Chang Y.C., Oas T.G. Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand. Biochemistry 2010, 49:5086-5096.
15. Wells M., Tidow H., Rutherford T.J., Markwick P., Jensen M.R., Mylonas E., Svergun D.I., Blackledge M., Fersht A.R. Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain. Proc. Natl. Acad. Sci. USA 2008, 105:5762-5767.
16. Mittag T., Marsh J., Grishaev A., Orlicky S., Lin H., Sicheri F., Tyers M., Forman-Kay J.D. Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. Structure 2010, 18:494-506.
17. Mittag T., Forman-Kay J.D. Atomic-level characterization of disordered protein ensembles. Curr. Opin. Struct. Biol. 2007, 17:3-14.
18. Jensen M.R., Markwick P.R., Meier S., Griesinger C., Zweckstetter M., Grzesiek S., Bernado P., Blackledge M. Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings. Structure 2009, 17:1169-1185.
19. Bermel W., Bertini I., Felli I.C., Piccioli M., Pierattelli R. 13C-detected protonless NMR spectroscopy of proteins in solution. Prog. Nucl. Magn. Reson. Spectrosc. 2006, 48:25-45.
20. O'Hare B., Benesi A.J., Showalter S.A. Incorporating1H-chemical shift determination into13C-direct detected spectroscopy of intrinsically disordered proteins in solution. J. Magn. Reson. 2009, 200:354-358.
21. Showalter S.A. NMR assignment of the intrinsically disordered C-terminal region of Homo sapiens FCP1 in the unbound state. Biomol. NMR Assign. 2009, 3:179-181.
22. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A. Nmrpipe - a multidimensional spectral processing system based on Unix pipes. J. Biomol. NMR 1995, 6:277-293.
23. T. Goddard, D. Kneller, SPARKY 3.113, 2006.
24. Wishart D.S., Sykes B.D. The C-13 chemical-shift index - a simple method for the identification of protein secondary structure using C-13 chemical-shift data. J. Biomol. NMR 1994, 4:171-180.
25. Meszaros B., Simon I., Dosztanyi Z. Prediction of protein binding regions in disordered proteins. PLoS Comput. Biol. 2009, 5:e1000376.
26. Jiao M., Li H.T., Chen J., Minton A.P., Liang Y. Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria. Biophys. J. 2010, 99:914-923.
27. Johnson E., Showalter S.A., Brüschweiler R. A multifaceted approach to the interpretation of NMR order parameters: a case study of a dynamic alpha-helix. J. Phys. Chem. B 2008, 112:6203-6210.
28. Dosztanyi Z., Meszaros B., Simon I. ANCHOR: web server for predicting protein binding regions in disordered proteins. Bioinformatics 2009, 25:2745-2746.