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Volumn 23, Issue 2, 2013, Pages 213-224

Intermolecular recognition revealed by the complex structure of human CLOCK-BMAL1 basic helix-loop-helix domains with E-box DNA

Author keywords

BMAL1; circadian; CLOCK; crystal structure; non canonical E box; phosphorylation

Indexed keywords

DNA; HELIX LOOP HELIX PROTEIN; TRANSCRIPTION FACTOR ARNTL; TRANSCRIPTION FACTOR CLOCK;

EID: 84873738229     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2012.170     Document Type: Article
Times cited : (81)

References (55)
  • 1
    • 0037118077 scopus 로고    scopus 로고
    • Circadian rhythms from fies to human
    • Panda S, Hogenesch JB, Kay SA. Circadian rhythms from fies to human. Nature 2002; 417:329-335.
    • (2002) Nature , vol.417 , pp. 329-335
    • Panda, S.1    Hogenesch, J.B.2    Kay, S.A.3
  • 2
    • 0037194790 scopus 로고    scopus 로고
    • Coordination of circadian timing in mammals
    • Reppert SM, Weaver DR. Coordination of circadian timing in mammals. Nature 2002; 418:935-941.
    • (2002) Nature , vol.418 , pp. 935-941
    • Reppert, S.M.1    Weaver, D.R.2
  • 4
    • 77649138576 scopus 로고    scopus 로고
    • Circadian rhythms and metabolic syndrome: From experimental genetics to human disease
    • Maury E, Ramsey KM, Bass J. Circadian rhythms and metabolic syndrome: from experimental genetics to human disease. Circ Res 2010; 106:447-462.
    • (2010) Circ Res , vol.106 , pp. 447-462
    • Maury, E.1    Ramsey, K.M.2    Bass, J.3
  • 5
    • 0033593306 scopus 로고    scopus 로고
    • Molecular bases for circadian clocks
    • Dunlap JC. Molecular bases for circadian clocks. Cell 1999; 96:271-290.
    • (1999) Cell , vol.96 , pp. 271-290
    • Dunlap, J.C.1
  • 6
    • 77958504804 scopus 로고    scopus 로고
    • Clocks not winding down: Unravelling circadian networks
    • Zhang EE, Kay SA. Clocks not winding down: unravelling circadian networks. Nat Rev Mol Cell Biol 2010; 11:764-776.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 764-776
    • Zhang, E.E.1    Kay, S.A.2
  • 7
    • 0032510778 scopus 로고    scopus 로고
    • The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors
    • Hogenesch JB, Gu YZ, Jain S, Bradfeld CA. The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors. Proc Natl Acad Sci USA 1998; 95:5474-5479.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5474-5479
    • Hogenesch, J.B.1    Gu, Y.Z.2    Jain, S.3    Bradfeld, C.A.4
  • 8
    • 0032486330 scopus 로고    scopus 로고
    • Role of the CLOCK protein in the mammalian circadian mechanism
    • Gekakis N, Staknis D, Nguyen HB, et al. Role of the CLOCK protein in the mammalian circadian mechanism. Science 1998; 280:1564-1569.
    • (1998) Science , vol.280 , pp. 1564-1569
    • Gekakis, N.1    Staknis, D.2    Nguyen, H.B.3
  • 9
    • 0033980393 scopus 로고    scopus 로고
    • Helix-loop-helix proteins: Regulators of transcription in eucaryotic organisms
    • Massari ME, Murre C. Helix-loop-helix proteins: regulators of transcription in eucaryotic organisms. Mol Cell Biol 2000; 20:429-440.
    • (2000) Mol Cell Biol , vol.20 , pp. 429-440
    • Massari, M.E.1    Murre, C.2
  • 10
    • 0028307093 scopus 로고
    • Structure and function of helix-loop-helix proteins
    • Murre C, Bain G, van Dijk MA, et al. Structure and function of helix-loop-helix proteins. Biochim Biophys Acta 1994; 1218:129-135.
    • (1994) Biochim Biophys Acta , vol.1218 , pp. 129-135
    • Murre, C.1    Bain, G.2    Van Dijk, M.A.3
  • 11
    • 0035001937 scopus 로고    scopus 로고
    • The basic helix-loop-helix protein family: Comparative genomics and phylogenetic analysis
    • Ledent V, Vervoort M. The basic helix-loop-helix protein family: comparative genomics and phylogenetic analysis. Genome Res 2001; 11:754-770.
    • (2001) Genome Res , vol.11 , pp. 754-770
    • Ledent, V.1    Vervoort, M.2
  • 12
    • 0037669486 scopus 로고    scopus 로고
    • The circadian E-box: When perfect is not good enough
    • Munoz E, Baler R. The circadian E-box: when perfect is not good enough. Chronobiol Int 2003; 20:371-388.
    • (2003) Chronobiol Int , vol.20 , pp. 371-388
    • Munoz, E.1    Baler, R.2
  • 13
    • 0021928806 scopus 로고
    • B lineage-specific interactions of an immunoglobulin enhancer with cellular factors in vivo
    • Ephrussi A, Church GM, Tonegawa S, Gilbert W. B lineage-specific interactions of an immunoglobulin enhancer with cellular factors in vivo. Science 1985; 227:134-140.
    • (1985) Science , vol.227 , pp. 134-140
    • Ephrussi, A.1    Church, G.M.2    Tonegawa, S.3    Gilbert, W.4
  • 14
    • 0024554495 scopus 로고
    • A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins
    • Murre C, McCaw PS, Baltimore D. A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins. Cell 1989; 56:777-783.
    • (1989) Cell , vol.56 , pp. 777-783
    • Murre, C.1    McCaw, P.S.2    Baltimore, D.3
  • 15
    • 0024378079 scopus 로고
    • Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifcally to a common DNA sequence
    • Murre C, McCaw PS, Vaessin H, et al. Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifcally to a common DNA sequence. Cell 1989; 58:537-544.
    • (1989) Cell , vol.58 , pp. 537-544
    • Murre, C.1    McCaw, P.S.2    Vaessin, H.3
  • 16
    • 0028865103 scopus 로고
    • DNA binding speci-fcities and pairing rules of the Ah receptor, ARNT, and SIM proteins
    • Swanson HI, Chan WK, Bradfeld CA. DNA binding speci-fcities and pairing rules of the Ah receptor, ARNT, and SIM proteins. J Biol Chem 1995; 270:26292-26302.
    • (1995) J Biol Chem , vol.270 , pp. 26292-26302
    • Swanson, H.I.1    Chan, W.K.2    Bradfeld, C.A.3
  • 17
    • 0036682099 scopus 로고    scopus 로고
    • A transcription factor response element for gene expression during circadian night
    • Ueda HR, Chen W, Adachi A, et al. A transcription factor response element for gene expression during circadian night. Nature 2002; 418:534-539.
    • (2002) Nature , vol.418 , pp. 534-539
    • Ueda, H.R.1    Chen, W.2    Adachi, A.3
  • 18
    • 0037007625 scopus 로고    scopus 로고
    • Extensive and divergent circadian gene expression in liver and heart
    • Storch KF, Lipan O, Leykin I, et al. Extensive and divergent circadian gene expression in liver and heart. Nature 2002; 417:78-83.
    • (2002) Nature , vol.417 , pp. 78-83
    • Storch, K.F.1    Lipan, O.2    Leykin, I.3
  • 19
    • 18444414586 scopus 로고    scopus 로고
    • Coordinated transcription of key pathways in the mouse by the circadian clock
    • Panda S, Antoch MP, Miller BH, et al. Coordinated transcription of key pathways in the mouse by the circadian clock. Cell 2002; 109:307-320.
    • (2002) Cell , vol.109 , pp. 307-320
    • Panda, S.1    Antoch, M.P.2    Miller, B.H.3
  • 20
    • 20044396172 scopus 로고    scopus 로고
    • A noncanonical E-box enhancer drives mouse Period2 circadian oscillations in vivo
    • Yoo SH, Ko CH, Lowrey PL, et al. A noncanonical E-box enhancer drives mouse Period2 circadian oscillations in vivo. Proc Natl Acad Sci USA 2005; 102:2608-2613.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2608-2613
    • Yoo, S.H.1    Ko, C.H.2    Lowrey, P.L.3
  • 21
    • 79952255290 scopus 로고    scopus 로고
    • Genome-wide pro-fling of the core clock protein bmal1 targets reveals a strict relationship with metabolism
    • Hatanaka F, Matsubara C, Myung J, et al. Genome-wide pro-fling of the core clock protein BMAL1 targets reveals a strict relationship with metabolism. Mol Cell Biol 2010; 30:5636-5648.
    • (2010) Mol Cell Biol , vol.30 , pp. 5636-5648
    • Hatanaka, F.1    Matsubara, C.2    Myung, J.3
  • 22
    • 79952261359 scopus 로고    scopus 로고
    • Genome-wide and phase-specific DNA-binding rhythms of BMAL1 control circadian output functions in mouse liver
    • Rey G, Cesbron F, Rougemont J, Reinke H, Brunner M, Naef F. Genome-wide and phase-specific DNA-binding rhythms of BMAL1 control circadian output functions in mouse liver. PLoS Biol 2011; 9:e1000595.
    • (2011) PLoS Biol , vol.9
    • Rey, G.1    Cesbron, F.2    Rougemont, J.3    Reinke, H.4    Brunner, M.5    Naef, F.6
  • 23
    • 39849084068 scopus 로고    scopus 로고
    • A direct repeat of E-box-like elements is required for cell-autonomous circadian rhythm of clock genes
    • Nakahata Y, Yoshida M, Takano A, et al. A direct repeat of E-box-like elements is required for cell-autonomous circadian rhythm of clock genes. BMC Mol Biol 2008; 9:1.
    • (2008) BMC Mol Biol , vol.9 , pp. 1
    • Nakahata, Y.1    Yoshida, M.2    Takano, A.3
  • 24
    • 84863751285 scopus 로고    scopus 로고
    • Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex
    • Huang N, Chelliah Y, Shan Y, et al. Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex. Science 2012; 337:189-194.
    • (2012) Science , vol.337 , pp. 189-194
    • Huang, N.1    Chelliah, Y.2    Shan, Y.3
  • 25
    • 0037462459 scopus 로고    scopus 로고
    • X-ray structures of Myc-Max and MadMax recognizing DNA: Molecular bases of regulation by proto-oncogenic transcription factors
    • Nair SK, Burley SK. X-ray structures of Myc-Max and MadMax recognizing DNA: molecular bases of regulation by proto-oncogenic transcription factors. Cell 2003; 112:193-205.
    • (2003) Cell , vol.112 , pp. 193-205
    • Nair, S.K.1    Burley, S.K.2
  • 27
    • 0031569798 scopus 로고    scopus 로고
    • The crystal structure of an intact human Max-DNA complex: New insights into mechanisms of transcriptional control
    • Brownlie P, Ceska T, Lamers M, et al. The crystal structure of an intact human Max-DNA complex: new insights into mechanisms of transcriptional control. Structure 1997; 5:509-520.
    • (1997) Structure , vol.5 , pp. 509-520
    • Brownlie, P.1    Ceska, T.2    Lamers, M.3
  • 28
    • 0032524465 scopus 로고    scopus 로고
    • Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 Å resolution
    • Parraga A, Bellsolell L, Ferre-D'Amare AR, Burley SK. Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 Å resolution. Structure 1998; 6:661-672.
    • (1998) Structure , vol.6 , pp. 661-672
    • Parraga, A.1    Bellsolell, L.2    Ferre-D'Amare, A.R.3    Burley, S.K.4
  • 29
    • 0028215362 scopus 로고
    • Crystal structure of MyoD bHLH domain-DNA complex: Perspectives on DNA recognition and implications for transcriptional activation
    • Ma PC, Rould MA, Weintraub H, Pabo CO. Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation. Cell 1994; 77:451-459.
    • (1994) Cell , vol.77 , pp. 451-459
    • Ma, P.C.1    Rould, M.A.2    Weintraub, H.3    Pabo, C.O.4
  • 30
    • 0027910469 scopus 로고
    • Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
    • Ferre-D'Amare AR, Prendergast GC, Ziff EB, Burley SK. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature 1993; 363:38-45.
    • (1993) Nature , vol.363 , pp. 38-45
    • Ferre-D'Amare, A.R.1    Prendergast, G.C.2    Ziff, E.B.3    Burley, S.K.4
  • 31
    • 0030794453 scopus 로고    scopus 로고
    • Crystal structure of PHO4 bHLH domain-DNA complex: Fanking base recognition
    • Shimizu T, Toumoto A, Ihara K, et al. Crystal structure of PHO4 bHLH domain-DNA complex: fanking base recognition. EMBO J 1997; 16:4689-4697.
    • (1997) EMBO J , vol.16 , pp. 4689-4697
    • Shimizu, T.1    Toumoto, A.2    Ihara, K.3
  • 32
    • 37849019258 scopus 로고    scopus 로고
    • Crystal structure of E47-NeuroD1/beta2 bHLH domain-DNA complex: Heterodimer selectivity and DNA recognition
    • Longo A, Guanga GP, Rose RB. Crystal structure of E47-NeuroD1/beta2 bHLH domain-DNA complex: heterodimer selectivity and DNA recognition. Biochemistry 2008; 47:218-229.
    • (2008) Biochemistry , vol.47 , pp. 218-229
    • Longo, A.1    Guanga, G.P.2    Rose, R.B.3
  • 33
    • 84863751285 scopus 로고    scopus 로고
    • Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex
    • Huang N, Chelliah Y, Shan Y, et al. Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex. Science 2012; 337:189-194.
    • (2012) Science , vol.337 , pp. 189-194
    • Huang, N.1    Chelliah, Y.2    Shan, Y.3
  • 34
    • 0035919479 scopus 로고    scopus 로고
    • Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofac-tors
    • Rutter J, Reick M, Wu LC, McKnight SL. Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofac-tors. Science 2001; 293:510-514.
    • (2001) Science , vol.293 , pp. 510-514
    • Rutter, J.1    Reick, M.2    Wu, L.C.3    McKnight, S.L.4
  • 35
    • 65549128208 scopus 로고    scopus 로고
    • Circadian rhythms. A circadian loop asSIRTs itself
    • Wijnen H. Circadian rhythms. A circadian loop asSIRTs itself. Science 2009; 324:598-599.
    • (2009) Science , vol.324 , pp. 598-599
    • Wijnen, H.1
  • 38
    • 67650094963 scopus 로고    scopus 로고
    • Roles of CLOCK phosphorylation in suppression of E-box-dependent transcription
    • Yoshitane H, Takao T, Satomi Y, Du NH, Okano T, Fukada Y. Roles of CLOCK phosphorylation in suppression of E-box-dependent transcription. Mol Cell Biol 2009; 29:3675-3686.
    • (2009) Mol Cell Biol , vol.29 , pp. 3675-3686
    • Yoshitane, H.1    Takao, T.2    Satomi, Y.3    Du, N.H.4    Okano, T.5    Fukada, Y.6
  • 39
    • 64049083872 scopus 로고    scopus 로고
    • CK2alpha phospho-rylates BMAL1 to regulate the mammalian clock
    • Tamaru T, Hirayama J, Isojima Y, et al. CK2alpha phospho-rylates BMAL1 to regulate the mammalian clock. Nat Struct Mol Biol 2009; 16:446-448.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 446-448
    • Tamaru, T.1    Hirayama, J.2    Isojima, Y.3
  • 40
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom N, Gammeltoft S, Brunak S. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 1999; 294:1351-1362.
    • (1999) J Mol Biol , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 41
    • 2942598149 scopus 로고    scopus 로고
    • PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation
    • Hornbeck PV, Chabra I, Kornhauser JM, Skrzypek E, Zhang B. PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation. Proteomics 2004; 4:1551-1561.
    • (2004) Proteomics , vol.4 , pp. 1551-1561
    • Hornbeck, P.V.1    Chabra, I.2    Kornhauser, J.M.3    Skrzypek, E.4    Zhang, B.5
  • 42
    • 11144353910 scopus 로고    scopus 로고
    • PERIOD2:: LU-CIFERASE real-time reporting of circadian dynamics reveals persistent circadian oscillations in mouse peripheral tissues
    • Yoo SH, Yamazaki S, Lowrey PL, et al. PERIOD2:: LU-CIFERASE real-time reporting of circadian dynamics reveals persistent circadian oscillations in mouse peripheral tissues. Proc Natl Acad Sci USA 2004; 101:5339-5346.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5339-5346
    • Yoo, S.H.1    Yamazaki, S.2    Lowrey, P.L.3
  • 44
    • 31944443125 scopus 로고    scopus 로고
    • Molecular mechanism of cell-autonomous circadian gene expression of Pe-riod2, a crucial regulator of the mammalian circadian clock
    • Akashi M, Ichise T, Mamine T, Takumi T. Molecular mechanism of cell-autonomous circadian gene expression of Pe-riod2, a crucial regulator of the mammalian circadian clock. Mol Biol Cell 2006; 17:555-565.
    • (2006) Mol Biol Cell , vol.17 , pp. 555-565
    • Akashi, M.1    Ichise, T.2    Mamine, T.3    Takumi, T.4
  • 45
    • 78649687209 scopus 로고    scopus 로고
    • Circadian integration of metabolism and energetics
    • Bass J, Takahashi JS. Circadian integration of metabolism and energetics. Science 2010; 330:1349-1354.
    • (2010) Science , vol.330 , pp. 1349-1354
    • Bass, J.1    Takahashi, J.S.2
  • 46
    • 0037016665 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase phosphorylates and negatively regulates basic helix-loop-helix-PAS transcription factor BMAL1
    • Sanada K, Okano T, Fukada Y. Mitogen-activated protein kinase phosphorylates and negatively regulates basic helix-loop-helix-PAS transcription factor BMAL1. J Biol Chem 2002; 277:267-271.
    • (2002) J Biol Chem , vol.277 , pp. 267-271
    • Sanada, K.1    Okano, T.2    Fukada, Y.3
  • 47
    • 33847779219 scopus 로고    scopus 로고
    • Post-translational modifications regulate the ticking of the circadian clock
    • Gallego M, Virshup DM. Post-translational modifications regulate the ticking of the circadian clock. Nat Rev Mol Cell Biol 2007; 8:139-148.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 139-148
    • Gallego, M.1    Virshup, D.M.2
  • 48
    • 33645010948 scopus 로고    scopus 로고
    • PER-dependent rhythms in CLK phosphorylation and E-box binding regulate circadian transcription
    • Yu W, Zheng H, Houl JH, Dauwalder B, Hardin PE. PER-dependent rhythms in CLK phosphorylation and E-box binding regulate circadian transcription. Genes Dev 2006; 20:723-733.
    • (2006) Genes Dev , vol.20 , pp. 723-733
    • Yu, W.1    Zheng, H.2    Houl, J.H.3    Dauwalder, B.4    Hardin, P.E.5
  • 49
  • 50
    • 33644617485 scopus 로고    scopus 로고
    • Rhythmic CLOCK-BMAL1 binding to multiple E-box motifs drives circadian Dbp transcription and chromatin transitions
    • Ripperger JA, Schibler U. Rhythmic CLOCK-BMAL1 binding to multiple E-box motifs drives circadian Dbp transcription and chromatin transitions. Nat Genet 2006; 38:369-374.
    • (2006) Nat Genet , vol.38 , pp. 369-374
    • Ripperger, J.A.1    Schibler, U.2
  • 51
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997; 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 52
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • Strong M, Sawaya MR, Wang S, Phillips M, Cascio D, Eisenberg D. Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc Natl Acad Sci USA 2006; 103:8060-8065.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8060-8065
    • Strong, M.1    Sawaya, M.R.2    Wang, S.3    Phillips, M.4    Cascio, D.5    Eisenberg, D.6
  • 53
  • 54
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams PD, Grosse-Kunstleve RW, Hung LW, et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 2002; 58:1948-1954.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1948-1954
    • Adams, P.D.1    Grosse-Kunstleve, R.W.2    Hung, L.W.3
  • 55
    • 34250666701 scopus 로고    scopus 로고
    • Production and purifcation of lentiviral vectors
    • Tiscornia G, Singer O, Verma IM. Production and purifcation of lentiviral vectors. Nat Protoc 2006; 1:241-245.
    • (2006) Nat Protoc , vol.1 , pp. 241-245
    • Tiscornia, G.1    Singer, O.2    Verma, I.M.3


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