메뉴 건너뛰기




Volumn 6, Issue , 2017, Pages

Genetically tunable frustration controls allostery in an intrinsically disordered transcription factor

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOCORTICOID RECEPTOR; INTRINSICALLY DISORDERED PROTEIN; ISOPROTEIN; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR;

EID: 85036494586     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.30688     Document Type: Article
Times cited : (77)

References (49)
  • 1
    • 27244437952 scopus 로고    scopus 로고
    • Predicting the energetics of osmolyte-induced protein folding/unfolding
    • Auton M, Bolen DW. 2005. Predicting the energetics of osmolyte-induced protein folding/unfolding. PNAS 102: 15065-15068. DOI:https://doi.org/10.1073/pnas.0507053102
    • (2005) PNAS , vol.102 , pp. 15065-15068
    • Auton, M.1    Bolen, D.W.2
  • 2
    • 84964733917 scopus 로고    scopus 로고
    • Modulation of intrinsically disordered protein function by post-translational modifications
    • Bah A, Forman-Kay JD. 2016. Modulation of intrinsically disordered protein function by post-translational modifications. Journal of Biological Chemistry 291:6696-6705. DOI:https://doi.org/10.1074/jbc.R115.695056
    • (2016) Journal of Biological Chemistry , vol.291 , pp. 6696-6705
    • Bah, A.1    Forman-Kay, J.D.2
  • 3
    • 84883237242 scopus 로고    scopus 로고
    • Determinants of the heightened activity of glucocorticoid receptor translational isoforms
    • Bender IK, Cao Y, Lu NZ, Nz L. 2013. Determinants of the heightened activity of glucocorticoid receptor translational isoforms. Molecular Endocrinology 27:1577-1587. DOI:https://doi.org/10.1210/me.2013-1009
    • (2013) Molecular Endocrinology , vol.27 , pp. 1577-1587
    • Bender, I.K.1    Cao, Y.2    Lu, N.Z.3    Nz, L.4
  • 4
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson JD, Wolynes PG. 1987. Spin glasses and the statistical mechanics of protein folding. PNAS 84:7524-7528. DOI:https://doi.org/10.1073/pnas.84.21.7524
    • (1987) PNAS , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 5
    • 84862992463 scopus 로고    scopus 로고
    • Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networks
    • Buljan M, Chalancon G, Eustermann S, Wagner GP, Fuxreiter M, Bateman A, Babu MM. 2012. Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networks. Molecular Cell 46:871-883. DOI:https://doi.org/10.1016/j.molcel.2012.05.039
    • (2012) Molecular Cell , vol.46 , pp. 871-883
    • Buljan, M.1    Chalancon, G.2    Eustermann, S.3    Wagner, G.P.4    Fuxreiter, M.5    Bateman, A.6    Babu, M.M.7
  • 6
    • 84876489239 scopus 로고    scopus 로고
    • Glucocorticoid receptor translational isoforms underlie maturational stage-specific glucocorticoid sensitivities of dendritic cells in mice and humans
    • Cao Y, Bender IK, Konstantinidis AK, Shin SC, Jewell CM, Cidlowski JA, Schleimer RP, Lu NZ, Nz L. 2013. Glucocorticoid receptor translational isoforms underlie maturational stage-specific glucocorticoid sensitivities of dendritic cells in mice and humans. Blood 121:1553-1562. DOI:https://doi.org/10.1182/blood-2012-05-432336
    • (2013) Blood , vol.121 , pp. 1553-1562
    • Cao, Y.1    Bender, I.K.2    Konstantinidis, A.K.3    Shin, S.C.4    Jewell, C.M.5    Cidlowski, J.A.6    Schleimer, R.P.7    Lu, N.Z.8    Nz, L.9
  • 7
    • 0030822523 scopus 로고    scopus 로고
    • Protein-protein interactions are implied in glucocorticoid receptor mutant 465*-mediated cell death
    • Chen H, Srinivasan G, Thompson EB. 1997. Protein-protein interactions are implied in glucocorticoid receptor mutant 465*-mediated cell death. Journal of Biological Chemistry 272:25873-25880. DOI:https://doi.org/10.1074/jbc.272.41.25873
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 25873-25880
    • Chen, H.1    Srinivasan, G.2    Thompson, E.B.3
  • 8
    • 0028292958 scopus 로고
    • Delineation of a small region within the major transactivation domain of the human glucocorticoid receptor that mediates transactivation of gene expression
    • Dahlman-Wright K, Almlöf T, McEwan IJ, Gustafsson JA, Wright AP. 1994. Delineation of a small region within the major transactivation domain of the human glucocorticoid receptor that mediates transactivation of gene expression. PNAS 91:1619-1623. DOI:https://doi.org/10.1073/pnas.91.5.1619
    • (1994) PNAS , vol.91 , pp. 1619-1623
    • Dahlman-Wright, K.1    Almlöf, T.2    McEwan, I.J.3    Gustafsson, J.A.4    Wright, A.P.5
  • 9
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson HJ, Wright PE. 2002. Coupling of folding and binding for unstructured proteins. Current Opinion in Structural Biology 12:54-60. DOI:https://doi.org/10.1016/S0959-440X(02)00289-0
    • (2002) Current Opinion in Structural Biology , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 10
    • 84879327823 scopus 로고    scopus 로고
    • Modulation of allostery by protein intrinsic disorder
    • Ferreon AC, Ferreon JC, Wright PE, Deniz AA. 2013. Modulation of allostery by protein intrinsic disorder. Nature 498:390-394. DOI:https://doi.org/10.1038/nature12294
    • (2013) Nature , vol.498 , pp. 390-394
    • Ferreon, A.C.1    Ferreon, J.C.2    Wright, P.E.3    Deniz, A.A.4
  • 11
    • 0030771214 scopus 로고    scopus 로고
    • Involvement of the transcription factor IID protein complex in gene activation by the N-terminal transactivation domain of the glucocorticoid receptor in vitro
    • Ford J, McEwan IJ, Wright AP, Gustafsson JA. 1997. Involvement of the transcription factor IID protein complex in gene activation by the N-terminal transactivation domain of the glucocorticoid receptor in vitro. Molecular Endocrinology 11:1467-1475. DOI:https://doi.org/10.1210/mend.11.10.9995
    • (1997) Molecular Endocrinology , vol.11 , pp. 1467-1475
    • Ford, J.1    McEwan, I.J.2    Wright, A.P.3    Gustafsson, J.A.4
  • 14
    • 0023150589 scopus 로고
    • Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement
    • Godowski PJ, Rusconi S, Miesfeld R, Yamamoto KR. 1987. Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement. Nature 325:365-368. DOI:https://doi.org/10.1038/325365a0
    • (1987) Nature , vol.325 , pp. 365-368
    • Godowski, P.J.1    Rusconi, S.2    Miesfeld, R.3    Yamamoto, K.R.4
  • 16
    • 68049144731 scopus 로고    scopus 로고
    • Allosteric effects govern nuclear receptor action: DNA appears as a player
    • Gronemeyer H, Bourguet W. 2009. Allosteric effects govern nuclear receptor action: DNA appears as a player. Science Signaling 2:pe34. DOI:https://doi.org/10.1126/scisignal.273pe34
    • (2009) Science Signaling , vol.2 , pp. pe34
    • Gronemeyer, H.1    Bourguet, W.2
  • 17
    • 84860863700 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Bound RNAs identify features and components of cellular assemblies
    • Han TW, Kato M, Xie S, Wu LC, Mirzaei H, Pei J, Chen M, Xie Y, Allen J, Xiao G, McKnight SL. 2012. Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. Cell 149: 768-779. DOI:https://doi.org/10.1016/j.cell.2012.04.016
    • (2012) Cell , vol.149 , pp. 768-779
    • Han, T.W.1    Kato, M.2    Xie, S.3    Wu, L.C.4    Mirzaei, H.5    Pei, J.6    Chen, M.7    Xie, Y.8    Allen, J.9    Xiao, G.10    McKnight, S.L.11
  • 18
    • 0024357799 scopus 로고
    • A simple method for site-directed mutagenesis using the polymerase chain reaction
    • Hemsley A, Arnheim N, Toney MD, Cortopassi G, Galas DJ. 1989. A simple method for site-directed mutagenesis using the polymerase chain reaction. Nucleic Acids Research 17:6545-6551. DOI:https://doi.org/10.1093/nar/17.16.6545
    • (1989) Nucleic Acids Research , vol.17 , pp. 6545-6551
    • Hemsley, A.1    Arnheim, N.2    Toney, M.D.3    Cortopassi, G.4    Galas, D.J.5
  • 20
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • Hilser VJ, Thompson EB. 2007. Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. PNAS 104:8311-8315. DOI:https://doi.org/10.1073/pnas.0700329104
    • (2007) PNAS , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 21
    • 81155132258 scopus 로고    scopus 로고
    • Structural dynamics, intrinsic disorder, and allostery in nuclear receptors as transcription factors
    • Hilser VJ, Thompson EB. 2011. Structural dynamics, intrinsic disorder, and allostery in nuclear receptors as transcription factors. Journal of Biological Chemistry 286:39675-39682. DOI:https://doi.org/10.1074/jbc.R111.278929
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 39675-39682
    • Hilser, V.J.1    Thompson, E.B.2
  • 22
    • 84861371612 scopus 로고    scopus 로고
    • Structural and energetic basis of allostery
    • Hilser VJ, Wrabl JO, Motlagh HN. 2012. Structural and energetic basis of allostery. Annual Review of Biophysics 41:585-609. DOI:https://doi.org/10.1146/annurev-biophys-050511-102319
    • (2012) Annual Review of Biophysics , vol.41 , pp. 585-609
    • Hilser, V.J.1    Wrabl, J.O.2    Motlagh, H.N.3
  • 23
    • 0023794190 scopus 로고
    • Multiple and cooperative trans-activation domains of the human glucocorticoid receptor
    • Hollenberg SM, Evans RM. 1988. Multiple and cooperative trans-activation domains of the human glucocorticoid receptor. Cell 55:899-906. DOI:https://doi.org/10.1016/0092-8674(88)90145-6
    • (1988) Cell , vol.55 , pp. 899-906
    • Hollenberg, S.M.1    Evans, R.M.2
  • 24
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland DE, Némethy G, Filmer D. 1966. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5:365-385. DOI:https://doi.org/10.1021/bi00865a047
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, D.E.1    Némethy, G.2    Filmer, D.3
  • 25
    • 0026582055 scopus 로고
    • Structure of the DNA-binding domain of zinc GAL4
    • Kraulis PJ, Raine AR, Gadhavi PL, Laue ED. 1992. Structure of the DNA-binding domain of zinc GAL4. Nature 356:448-450. DOI:https://doi.org/10.1038/356448a0
    • (1992) Nature , vol.356 , pp. 448-450
    • Kraulis, P.J.1    Raine, A.R.2    Gadhavi, P.L.3    Laue, E.D.4
  • 26
    • 67649968884 scopus 로고    scopus 로고
    • Frustrated bistability as a means to engineer oscillations in biological systems
    • Krishna S, Semsey S, Jensen MH. 2009. Frustrated bistability as a means to engineer oscillations in biological systems. Physical Biology 6:036009. DOI:https://doi.org/10.1088/1478-3975/6/3/036009
    • (2009) Physical Biology , vol.6 , pp. 036009
    • Krishna, S.1    Semsey, S.2    Jensen, M.H.3
  • 27
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin JA, Yamamoto KR. 1998. Allosteric effects of DNA on transcriptional regulators. Nature 392:885-888. DOI:https://doi.org/10.1038/31860
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 28
    • 84864545860 scopus 로고    scopus 로고
    • Thermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor
    • Li J, Motlagh HN, Chakuroff C, Thompson EB, Hilser VJ. 2012. Thermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor. Journal of Biological Chemistry 287:26777-26787. DOI:https://doi.org/10.1074/jbc.M112.355651
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 26777-26787
    • Li, J.1    Motlagh, H.N.2    Chakuroff, C.3    Thompson, E.B.4    Hilser, V.J.5
  • 30
    • 20844437424 scopus 로고    scopus 로고
    • Translational regulatory mechanisms generate N-terminal glucocorticoid receptor isoforms with unique transcriptional target genes
    • Lu NZ, Cidlowski JA. 2005. Translational regulatory mechanisms generate N-terminal glucocorticoid receptor isoforms with unique transcriptional target genes. Molecular Cell 18:331-342. DOI:https://doi.org/10.1016/j.molcel.2005.03.025
    • (2005) Molecular Cell , vol.18 , pp. 331-342
    • Lu, N.Z.1    Cidlowski, J.A.2
  • 31
    • 33745090483 scopus 로고    scopus 로고
    • Glucocorticoid receptor isoforms generate transcription specificity
    • Lu NZ, Cidlowski JA. 2006. Glucocorticoid receptor isoforms generate transcription specificity. Trends in Cell Biology 16:301-307. DOI:https://doi.org/10.1016/j.tcb.2006.04.005
    • (2006) Trends in Cell Biology , vol.16 , pp. 301-307
    • Lu, N.Z.1    Cidlowski, J.A.2
  • 32
    • 84856303585 scopus 로고    scopus 로고
    • Long-range modulation of chain motions within the intrinsically disordered transactivation domain of tumor suppressor p53
    • Lum JK, Neuweiler H, Fersht AR. 2012. Long-range modulation of chain motions within the intrinsically disordered transactivation domain of tumor suppressor p53. Journal of the American Chemical Society 134: 1617-1622. DOI:https://doi.org/10.1021/ja2078619
    • (2012) Journal of the American Chemical Society , vol.134 , pp. 1617-1622
    • Lum, J.K.1    Neuweiler, H.2    Fersht, A.R.3
  • 33
    • 65249167505 scopus 로고    scopus 로고
    • DNA binding site sequence directs glucocorticoid receptor structure and activity
    • Meijsing SH, Pufall MA, So AY, Bates DL, Chen L, Yamamoto KR. 2009. DNA binding site sequence directs glucocorticoid receptor structure and activity. Science 324:407-410. DOI:https://doi.org/10.1126/science.1164265
    • (2009) Science , vol.324 , pp. 407-410
    • Meijsing, S.H.1    Pufall, M.A.2    So, A.Y.3    Bates, D.L.4    Chen, L.5    Yamamoto, K.R.6
  • 34
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux JP. 1965. On the nature of allosteric transitions: A plausible model. Journal of Molecular Biology 12:88-118. DOI:https://doi.org/10.1016/S0022-2836(65)80285-6
    • (1965) Journal of Molecular Biology , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 35
    • 84858234186 scopus 로고    scopus 로고
    • Agonism/antagonism switching in allosteric ensembles
    • Motlagh HN, Hilser VJ. 2012. Agonism/antagonism switching in allosteric ensembles. PNAS 109:4134-4139. DOI:https://doi.org/10.1073/pnas.1120519109
    • (2012) PNAS , vol.109 , pp. 4134-4139
    • Motlagh, H.N.1    Hilser, V.J.2
  • 36
    • 84898993517 scopus 로고    scopus 로고
    • The ensemble nature of allostery
    • Motlagh HN, Wrabl JO, Li J, Hilser VJ. 2014. The ensemble nature of allostery. Nature 508:331-339. DOI:https://doi.org/10.1038/nature13001
    • (2014) Nature , vol.508 , pp. 331-339
    • Motlagh, H.N.1    Wrabl, J.O.2    Li, J.3    Hilser, V.J.4
  • 37
    • 4544241529 scopus 로고    scopus 로고
    • cDNA cloning and characterization of a secreted luciferase from the luminous Japanese ostracod, Cypridina noctiluca
    • Nakajima Y, Kobayashi K, Yamagishi K, Enomoto T, Ohmiya Y. 2004. cDNA cloning and characterization of a secreted luciferase from the luminous Japanese ostracod, Cypridina noctiluca. Bioscience, Biotechnology, and Biochemistry 68:565-570. DOI:https://doi.org/10.1271/bbb.68.565
    • (2004) Bioscience, Biotechnology, and Biochemistry , vol.68 , pp. 565-570
    • Nakajima, Y.1    Kobayashi, K.2    Yamagishi, K.3    Enomoto, T.4    Ohmiya, Y.5
  • 38
    • 0037059739 scopus 로고    scopus 로고
    • Allosteric effects of dexamethasone and RU486 on glucocorticoid receptor-DNA interactions
    • Pandit S, Geissler W, Harris G, Sitlani A. 2002. Allosteric effects of dexamethasone and RU486 on glucocorticoid receptor-DNA interactions. Journal of Biological Chemistry 277:1538-1543. DOI:https://doi.org/10.1074/jbc.M105438200
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 1538-1543
    • Pandit, S.1    Geissler, W.2    Harris, G.3    Sitlani, A.4
  • 39
    • 70849084011 scopus 로고    scopus 로고
    • Hidden dynamic allostery in a PDZ domain
    • Petit CM, Zhang J, Sapienza PJ, Fuentes EJ, Lee AL. 2009. Hidden dynamic allostery in a PDZ domain. PNAS 106:18249-18254. DOI:https://doi.org/10.1073/pnas.0904492106
    • (2009) PNAS , vol.106 , pp. 18249-18254
    • Petit, C.M.1    Zhang, J.2    Sapienza, P.J.3    Fuentes, E.J.4    Lee, A.L.5
  • 40
    • 77952046404 scopus 로고    scopus 로고
    • Hormone binding and co-regulator binding to the glucocorticoid receptor are allosterically coupled
    • Pfaff SJ, Fletterick RJ. 2010. Hormone binding and co-regulator binding to the glucocorticoid receptor are allosterically coupled. Journal of Biological Chemistry 285:15256-15267. DOI:https://doi.org/10.1074/jbc.M110.108118
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 15256-15267
    • Pfaff, S.J.1    Fletterick, R.J.2
  • 42
    • 79955685287 scopus 로고    scopus 로고
    • Allostery in a disordered protein: Oxidative modifications to α-synuclein act distally to regulate membrane binding
    • Sevcsik E, Trexler AJ, Dunn JM, Rhoades E. 2011. Allostery in a disordered protein: oxidative modifications to α-synuclein act distally to regulate membrane binding. Journal of the American Chemical Society 133:7152-7158. DOI:https://doi.org/10.1021/ja2009554
    • (2011) Journal of the American Chemical Society , vol.133 , pp. 7152-7158
    • Sevcsik, E.1    Trexler, A.J.2    Dunn, J.M.3    Rhoades, E.4
  • 44
    • 14044250981 scopus 로고    scopus 로고
    • Codon-optimized gaussia luciferase cDNA for mammalian gene expression in culture and in vivo
    • Tannous BA, Kim DE, Fernandez JL, Weissleder R, Breakefield XO. 2005. Codon-optimized gaussia luciferase cDNA for mammalian gene expression in culture and in vivo. Molecular Therapy 11:435-443. DOI:https://doi.org/10.1016/j.ymthe.2004.10.016
    • (2005) Molecular Therapy , vol.11 , pp. 435-443
    • Tannous, B.A.1    Kim, D.E.2    Fernandez, J.L.3    Weissleder, R.4    Breakefield, X.O.5
  • 45
    • 70450191983 scopus 로고    scopus 로고
    • Dynamic activation of an allosteric regulatory protein
    • Tzeng SR, Kalodimos CG. 2009. Dynamic activation of an allosteric regulatory protein. Nature 462:368-372. DOI:https://doi.org/10.1038/nature08560
    • (2009) Nature , vol.462 , pp. 368-372
    • Tzeng, S.R.1    Kalodimos, C.G.2
  • 46
    • 84864651001 scopus 로고    scopus 로고
    • Protein activity regulation by conformational entropy
    • Tzeng SR, Kalodimos CG. 2012. Protein activity regulation by conformational entropy. Nature 488:236-240. DOI:https://doi.org/10.1038/nature11271
    • (2012) Nature , vol.488 , pp. 236-240
    • Tzeng, S.R.1    Kalodimos, C.G.2
  • 47
    • 0009791166 scopus 로고
    • Theory of the frustration effect. II. Ising spins on a square lattice
    • Vannimenus J, Toulouse G. 1977. Theory of the frustration effect. II. Ising spins on a square lattice. Journal of Physics C: Solid State Physics 10:L537-L542. DOI:https://doi.org/10.1088/0022-3719/10/18/008
    • (1977) Journal of Physics C: Solid State Physics , vol.10 , pp. L537-L542
    • Vannimenus, J.1    Toulouse, G.2
  • 48
    • 36149045781 scopus 로고
    • Two-level systems in a spin-glass model. I. General formalism and two-dimensional model
    • Villain J. 1977. Two-level systems in a spin-glass model. I. General formalism and two-dimensional model. Journal of Physics C: Solid State Physics 10:4793-4803. DOI:https://doi.org/10.1088/0022-3719/10/23/013
    • (1977) Journal of Physics C: Solid State Physics , vol.10 , pp. 4793-4803
    • Villain, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.