Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1α/ERRγ complex

Proceedings of the National Academy of Sciences of the United States of America

Volumn 108, Issue 46, 2011, Pages 18678-18683

  Devarakonda, Srikripa ^a   Gupta, Kushol ^b   Chalmers, Michael J ^c   Hunt, John F ^d   Griffin, Patrick R ^c   Van Duyne, Gregory D ^b   Spiegelman, Bruce M ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

^d Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ESTROGEN RELATED RECEPTOR GAMMA; LIGAND; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; STEROID RECEPTOR; UNCLASSIFIED DRUG;

AEROBIC METABOLISM; AMINO TERMINAL SEQUENCE; ARTICLE; BIOCHEMISTRY; BIOPHYSICS; CONFORMATIONAL TRANSITION; DEUTERIUM HYDROGEN EXCHANGE; DISORDER TO ORDER TRANSITION; LIGAND BINDING; MITOCHONDRION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; SMALL ANGLE SCATTERING; TRANSCRIPTION REGULATION;

BIOPHYSICS; HEAT-SHOCK PROTEINS; HUMANS; LIGANDS; MITOCHONDRIA; MODELS, MOLECULAR; MOLECULAR CONFORMATION; OXYGEN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, ESTROGEN; SCATTERING, RADIATION; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC; X-RAYS;

EID: 81755187015     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1113813108     Document Type: Article

References (40)

1. Lin J, Handschin C, Spiegelman BM (2005) Metabolic control through the PGC-1 family of transcription coactivators. Cell Metab 1:361-370. (Pubitemid 43960626)
2. Ventura-Clapier R, Garnier A, Veksler V (2008) Transcriptional control of mitochondrial biogenesis: The central role of PGC-1alpha. Cardiovasc Res 79:208-217. (Pubitemid 351951611)
3. Jornayvaz FR, Shulman GI (2010) Regulation of mitochondrial biogenesis. Essays Biochem 47:69-84.
4. Olesen J, Kiilerich K, Pilegaard H (2010) PGC-1alpha-mediated adaptations in skeletal muscle. Pflugers Arch 460:153-162.
5. Giguere V (2008) Transcriptional control of energy homeostasis by the estrogen-related receptors. Endocr Rev 29:677-696.
6. Dufour CR, et al. (2007) Genome-wide orchestration of cardiac functions by the orphan nuclear receptors ERRalpha and gamma. Cell Metab 5:345-356. (Pubitemid 46667756)
7. Huss JM, Kopp RP, Kelly DP (2002) Peroxisome proliferator-activated receptor coactivator-1alpha (PGC-1alpha) coactivates the cardiac-enriched nuclear receptors estrogen-related receptor-alpha and -gamma. Identification of novel leucine-rich interaction motif within PGC-1alpha. J Biol Chem 277:40265-40274. (Pubitemid 35215598)
8. Liu D, Zhang Z, Teng CT (2005) Estrogen-related receptor-gamma and peroxisome proliferator-activated receptor-gamma coactivator-1alpha regulate estrogen-related receptor-alpha gene expression via a conserved multi-hormone response element. J Mol Endocrinol 34:473-487. (Pubitemid 40585196)
9. Xu L, Glass CK, RosenfeldMG (1999) Coactivator and corepressor complexes in nuclear receptor function. Curr Opin Genet Dev 9:140-147. (Pubitemid 29158546)
10. Bourdoncle A, et al. (2005) The nuclear receptor coactivator PGC-1alpha exhibits modes of interaction with the estrogen receptor distinct from those of SRC-1. J Mol Biol 347:921-934. (Pubitemid 40387444)
11. Greschik H, et al. (2008) Communication between the ERRalpha homodimer interface and the PGC-1alpha binding surface via the helix 8-9 loop. J Biol Chem 283:20220-20230.
12. Kallen J, et al. (2004) Evidence for ligand-independent transcriptional activation of the human estrogen-related receptor alpha (ERRalpha): Crystal structure of ERRalpha ligand binding domain in complex with peroxisome proliferator-activated receptor coactivator-1alpha. J Biol Chem 279:49330-49337. (Pubitemid 39625820)
13. Li Y, Kovach A, Suino-Powell K, Martynowski D, Xu HE (2008) Structural and biochemical basis for the binding selectivity of peroxisome proliferator-activated receptor gamma to PGC-1alpha. J Biol Chem 283:19132-19139.
14. Puigserver P, et al. (1999) Activation of PPARgamma coactivator-1 through transcription factor docking. Science 286:1368-1371.
15. Rha GB, Wu G, Shoelson SE, Chi YI (2009) Multiple binding modes between HNF4alpha and the LXXLL motifs of PGC-1alpha lead to full activation. J Biol Chem 284:35165-35176.
16. Jin KS, et al. (2008) Small-angle X-ray scattering studies on structures of an estrogen-related receptor alpha ligand binding domain and its complexes with ligands and coactivators. J Phys Chem B 112:9603-9612.
17. Siegel LM, Monty KJ (1966) Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases. Biochim Biophys Acta 112:346-362.
18. Uversky VN (1993) Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry 32:13288-13298.
19. Hyeon C, Dima RI, Thirumalai D (2006) Size, shape, and flexibility of RNA structures. J Chem Phys 125:194905.
20. Damaschun G, et al. (1992) Streptokinase is a flexible multi-domain protein. Eur Biophys J 20:355-361.
21. Gast K, et al. (1994) Compactness of protein molten globules: Temperature-induced structural changes of the apomyoglobin folding intermediate. Eur Biophys J 23:297-305. (Pubitemid 24331693)
22. Feigin L, Svergun DI (1987) Structural Analysis by Small-Angle X-ray and Neutron Scattering (Plenum, New York).
23. Glatter O, Kratky O (1982) Small Angle X-ray Scattering (Academic, London).
24. Semisotnov GV, et al. (1996) Protein globularization during folding. A study by synchrotron small-angle X-ray scattering. J Mol Biol 262:559-574. (Pubitemid 26341174)
25. Uversky VN, et al. (1998) Anion-induced folding of Staphylococcal nuclease: Characterization of multiple equilibrium partially folded intermediates. J Mol Biol 278:879-894. (Pubitemid 28224903)
26. Rambo RP, Tainer JA (2011) Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law. Biopolymers 95:559-571.
27. Dyson HJ, Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6:197-208. (Pubitemid 40314921)
28. Fong JH, et al. (2009) Intrinsic disorder in protein interactions: Insights from a comprehensive structural analysis. PLoS Comput Biol 5:e1000316.
29. Svergun DI (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 76:2879-2886.
30. Svergun DI, Petoukhov MV, Koch MH (2001) Determination of domain structure of proteins from X-ray solution scattering. Biophys J 80:2946-2953. (Pubitemid 32521666)
31. Bernado P (2010) Effect of interdomain dynamics on the structure determination of modular proteins by small-angle scattering. Eur Biophys J 39:769-780.
32. Bernado P, Mylonas E, Petoukhov MV, Blackledge M, Svergun DI (2007) Structural characterization of flexible proteins using small-angle X-ray scattering. J Am Chem Soc 129:5656-5664. (Pubitemid 46697655)
33. Svergun DI, Nierhaus KH (2000) A map of protein-rRNA distribution in the 70 S Escherichia coli ribosome. J Biol Chem 275:14432-14439. (Pubitemid 30339729)
34. Nolte RT, et al. (1998) Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature 395:137-143. (Pubitemid 28425645)
35. Zhang J, et al. (2011) DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex. Nat Struct Mol Biol 18:556-564.
36. Huang P, Chandra V, Rastinejad F (2010) Structural overview of the nuclear receptor superfamily: Insights into physiology and therapeutics. Annu Rev Physiol 72:247-272.
37. Bulynko YA, O'Malley BW (2011) Nuclear receptor coactivators: Structural and functional biochemistry. Biochemistry 50:313-328.
38. Schuck P (2004) A model for sedimentation in inhomogeneous media. I. Dynamic density gradients from sedimenting co-solutes. Biophys Chem 108:187-200.
39. Chalmers MJ, et al. (2006) Probing protein ligand interactions by automated hydrogen/deuterium exchange mass spectrometry. Anal Chem 78:1005-1014. (Pubitemid 43271829)
40. Semenyuk AV, Svergun DI (1991) Gnom - a program package for small-angle scattering data-processing. J Appl Crystallogr 24:537-540.