메뉴 건너뛰기




Volumn 5, Issue 4, 1997, Pages 509-520

The crystal structure of an intact human Max-DNA complex: New insights into mechanisms of transcriptional control

Author keywords

DNA binding; helix loop helix; leucine zipper; Max; transcription factor; X ray crystallography

Indexed keywords

ESCHERICHIA COLI;

EID: 0031569798     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00207-4     Document Type: Article
Times cited : (144)

References (48)
  • 1
    • 0025763419 scopus 로고
    • Max: A helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc
    • Blackwood, E.M. & Eisenman, R.N. (1991). Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science 251, 1211-1217.
    • (1991) Science , vol.251 , pp. 1211-1217
    • Blackwood, E.M.1    Eisenman, R.N.2
  • 2
    • 0028084338 scopus 로고
    • Myc-Max-Mad: A transcription factor network controlling cell cycle progression, differentiation and death
    • Amati, B. & Land, H. (1994). Myc-Max-Mad: a transcription factor network controlling cell cycle progression, differentiation and death. Curr. Opin. Cell Biol. 4, 102-108.
    • (1994) Curr. Opin. Cell Biol. , vol.4 , pp. 102-108
    • Amati, B.1    Land, H.2
  • 3
    • 0026665523 scopus 로고
    • Transcriptional activation by the human c-Myc protein in yeast requires interaction with Max
    • Amati, B., Dalton, S., Brooks, M.W., Littlewood, T.D., Evan, G.I. & Land, H. (1992). Transcriptional activation by the human c-Myc protein in yeast requires interaction with Max. Nature 359, 423-426.
    • (1992) Nature , vol.359 , pp. 423-426
    • Amati, B.1    Dalton, S.2    Brooks, M.W.3    Littlewood, T.D.4    Evan, G.I.5    Land, H.6
  • 4
    • 0027408096 scopus 로고
    • Mad: A heterodimeric partner for Max that antagonizes Myc transcriptional activity
    • Ayer, D.E., Kretzner, L. & Eisenman, R.N. (1993). Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell 72, 211-222.
    • (1993) Cell , vol.72 , pp. 211-222
    • Ayer, D.E.1    Kretzner, L.2    Eisenman, R.N.3
  • 5
    • 0027511606 scopus 로고
    • Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites
    • Zervos, A.S., Gyuris, J. & Brent, R. (1993). Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites. Cell 72, 223-232.
    • (1993) Cell , vol.72 , pp. 223-232
    • Zervos, A.S.1    Gyuris, J.2    Brent, R.3
  • 7
    • 0028299321 scopus 로고
    • Expression of mad, mxi1, max, and c-myc during induced differentiation of hematopoietic cells: Opposite regulation of mad and c-myc
    • Larsson, L.G., Pettersson, M., Oeberg, F., Nilsson, K. & Luescher, B. (1994). Expression of mad, mxi1, max, and c-myc during induced differentiation of hematopoietic cells: opposite regulation of mad and c-myc. Oncogene 9, 1247-1252.
    • (1994) Oncogene , vol.9 , pp. 1247-1252
    • Larsson, L.G.1    Pettersson, M.2    Oeberg, F.3    Nilsson, K.4    Luescher, B.5
  • 8
    • 0028905563 scopus 로고
    • Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of the yeast repressor Sin3
    • Ayer, D.E., Lawrence, Q.A. & Eisenman, R.N. (1995). Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of the yeast repressor Sin3. Cell 80, 767-776.
    • (1995) Cell , vol.80 , pp. 767-776
    • Ayer, D.E.1    Lawrence, Q.A.2    Eisenman, R.N.3
  • 10
    • 0027910469 scopus 로고
    • Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
    • Ferre-D'Amare, A.R., Prendergast, G.C., Ziff, E.B. & Burley, S.K. (1993). Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature 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
  • 12
    • 0028329080 scopus 로고
    • Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer
    • Ellenberger, T., Fass, D., Arnaud, M. & Harrison, S.C. (1994). Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer. Genes Dev. 8, 970-980.
    • (1994) Genes Dev. , vol.8 , pp. 970-980
    • Ellenberger, T.1    Fass, D.2    Arnaud, M.3    Harrison, S.C.4
  • 13
    • 0028215362 scopus 로고
    • Crystal structure of MyoD bHLH domain-DNA complex: Perspectives on DNA recognition and implications for transcriptional activation
    • Ma, P.C.M., Rould, M.A., Weintraub, H. & Pabo, C.O. (1994). Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation. Cell 77, 451-459.
    • (1994) Cell , vol.77 , pp. 451-459
    • Ma, P.C.M.1    Rould, M.A.2    Weintraub, H.3    Pabo, C.O.4
  • 14
    • 0027441937 scopus 로고
    • Transcription activation by Myc and Max: Flanking sequences target activation to a subset of CACGTG motifs in vivo
    • Fisher, F., Crouch, D.H., Jayaraman, P.S., Clark, W., Gillespie, D.A.F. & Coding, C.R. (1993). Transcription activation by Myc and Max: flanking sequences target activation to a subset of CACGTG motifs in vivo. EMBO J. 12, 5075-5082.
    • (1993) EMBO J. , vol.12 , pp. 5075-5082
    • Fisher, F.1    Crouch, D.H.2    Jayaraman, P.S.3    Clark, W.4    Gillespie, D.A.F.5    Coding, C.R.6
  • 15
    • 0026554939 scopus 로고
    • Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers
    • Berberich, S.J. & Cole, D.M. (1992). Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers. Genes Dev. 6, 166-176.
    • (1992) Genes Dev. , vol.6 , pp. 166-176
    • Berberich, S.J.1    Cole, D.M.2
  • 16
    • 0027385033 scopus 로고
    • Identification of casein kinase II phosphorylation sites in Max: Effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers
    • Bousset, K., Henriksson, M., Luescher-Firzlaff, J.M., Litchfield, D.W. & Luescher, B. (1993). Identification of casein kinase II phosphorylation sites in Max: effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers. Oncogene 8, 3211-3220.
    • (1993) Oncogene , vol.8 , pp. 3211-3220
    • Bousset, K.1    Henriksson, M.2    Luescher-Firzlaff, J.M.3    Litchfield, D.W.4    Luescher, B.5
  • 18
    • 0026601537 scopus 로고
    • Alternative forms of Max as enhancers or repressors of Myc-Ras cotransformation
    • Maekelae, T.P., Koskinen, P.J., Vaestrik, I. & Alitalo, K. (1992). Alternative forms of Max as enhancers or repressors of Myc-Ras cotransformation. Science 256, 373-377.
    • (1992) Science , vol.256 , pp. 373-377
    • Maekelae, T.P.1    Koskinen, P.J.2    Vaestrik, I.3    Alitalo, K.4
  • 19
    • 0026516472 scopus 로고
    • Max: Functional domains and interaction with c-Myc
    • Kato, G.J., Lee, M.F.W., Chen, L. & Dand, C.V. (1992). Max: functional domains and interaction with c-Myc. Genes Dev. 6, 81-92.
    • (1992) Genes Dev. , vol.6 , pp. 81-92
    • Kato, G.J.1    Lee, M.F.W.2    Chen, L.3    Dand, C.V.4
  • 20
    • 0024511105 scopus 로고
    • Involvement of the 'leucine zipper' region in the oligomerization and transforming activity of human c-Myc protein
    • Dang, C.V., McGuire, M., Buckmire, M. & Lee, W.M. (1989). Involvement of the 'leucine zipper' region in the oligomerization and transforming activity of human c-Myc protein. Nature 337, 664-666.
    • (1989) Nature , vol.337 , pp. 664-666
    • Dang, C.V.1    McGuire, M.2    Buckmire, M.3    Lee, W.M.4
  • 21
    • 0025719216 scopus 로고
    • TFEB has DNA-binding and oligomerization properties of a unique helix-loop-helix/leucine zipper family
    • Fisher, D.E., Carr, C.S., Parent, L.A. & Sharp, P.A. (1991). TFEB has DNA-binding and oligomerization properties of a unique helix-loop-helix/leucine zipper family. Genes Dev. 5, 2342-2352.
    • (1991) Genes Dev. , vol.5 , pp. 2342-2352
    • Fisher, D.E.1    Carr, C.S.2    Parent, L.A.3    Sharp, P.A.4
  • 22
    • 0029095998 scopus 로고
    • Anti-cooperative biphasic equilibrium binding of transcription factor upstream stimulatory factor to its cognate DNA monitored by protein fluorescence changes
    • Sha, M., Ferre-D'Amare, A.R., Burley, K.S. & Goss, D.J. (1995). Anti-cooperative biphasic equilibrium binding of transcription factor upstream stimulatory factor to its cognate DNA monitored by protein fluorescence changes. J. Biol. Chem. 270, 19325-19329.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19325-19329
    • Sha, M.1    Ferre-D'Amare, A.R.2    Burley, K.S.3    Goss, D.J.4
  • 23
    • 0027490354 scopus 로고
    • Multiple oligomeric states regulate the DNA binding of helix-loop-helix peptides
    • Fairman, R., et al., & Brenner, S.L. (1993). Multiple oligomeric states regulate the DNA binding of helix-loop-helix peptides. Proc. Natl. Acad. Sci. USA 190, 10429-10433.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.190 , pp. 10429-10433
    • Fairman, R.1    Brenner, S.L.2
  • 24
    • 0028773466 scopus 로고
    • Use of dynamic light scattering to assess crystallizability of macromolecules and macromolecular assemblies
    • Ferre-D'Amare, A.R. & Burley, S.K. (1994). Use of dynamic light scattering to assess crystallizability of macromolecules and macromolecular assemblies. Structure 2, 357-359.
    • (1994) Structure , vol.2 , pp. 357-359
    • Ferre-D'Amare, A.R.1    Burley, S.K.2
  • 25
    • 0343063933 scopus 로고
    • Structure of proteins: Packing of α helices and pleated sheets
    • Chothia, C., Levitt, M. & Richardson, D. (1977). Structure of proteins: packing of α helices and pleated sheets. Proc. Natl. Acad. Sci. USA 74, 4130-4134.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 4130-4134
    • Chothia, C.1    Levitt, M.2    Richardson, D.3
  • 26
    • 0017876485 scopus 로고
    • Packing of helices: Geometrical constraints and contact areas
    • Richmond, T.J. & Richards, F.M. (1978). Packing of helices: geometrical constraints and contact areas. J. Mol. Biol. 119, 536-555.
    • (1978) J. Mol. Biol. , vol.119 , pp. 536-555
    • Richmond, T.J.1    Richards, F.M.2
  • 27
    • 0028792332 scopus 로고
    • c-Myc and Maxtransregulate the mouse ornithine decarboxylase promoter through interaction with two downstream CACGTG motifs
    • Tobias, K.E., Shor, J. & Kahana, C. (1995). c-Myc and Maxtransregulate the mouse ornithine decarboxylase promoter through interaction with two downstream CACGTG motifs. Oncogene 11, 1721-1727.
    • (1995) Oncogene , vol.11 , pp. 1721-1727
    • Tobias, K.E.1    Shor, J.2    Kahana, C.3
  • 28
    • 0029864934 scopus 로고    scopus 로고
    • Discrimination between different E-box-binding proteins at an endogenous target gene of c-myc
    • Desbarats, L., Gaubatz, S. & Eilers, M. (1996). Discrimination between different E-box-binding proteins at an endogenous target gene of c-myc. Genes Dev. 10, 447-460.
    • (1996) Genes Dev. , vol.10 , pp. 447-460
    • Desbarats, L.1    Gaubatz, S.2    Eilers, M.3
  • 29
    • 0029772318 scopus 로고    scopus 로고
    • An essential E-box in the promoter of the gene encoding the mRNA cap-binding protein (eukaryotic initiation factor 4E) is a target for activation by c-myc
    • Jones, R.M., et al., & Schmidt, E.V. (1996). An essential E-box in the promoter of the gene encoding the mRNA cap-binding protein (eukaryotic initiation factor 4E) is a target for activation by c-myc. Mol. Cell. Biol. 16, 4754-4764.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4754-4764
    • Jones, R.M.1    Schmidt, E.V.2
  • 30
    • 0028839440 scopus 로고
    • The leucine-zippers of the HLH-LZ proteins Max and c-Myc preferentially form heterodimers
    • Muhle-Goll, C., Nilges, M. & Pastore, A. (1995). The leucine-zippers of the HLH-LZ proteins Max and c-Myc preferentially form heterodimers. Biochemistry 43, 13554-13564.
    • (1995) Biochemistry , vol.43 , pp. 13554-13564
    • Muhle-Goll, C.1    Nilges, M.2    Pastore, A.3
  • 32
    • 0027050007 scopus 로고
    • Myc/Max and other helix-loop-helix/leucine zipper proteins bend DNA toward the minor groove
    • Fisher, D.A., Parent, L.A. & Sharp, P.A. (1992). Myc/Max and other helix-loop-helix/leucine zipper proteins bend DNA toward the minor groove. Proc. Natl. Acad. Sci. USA 89, 11779-11783.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11779-11783
    • Fisher, D.A.1    Parent, L.A.2    Sharp, P.A.3
  • 33
    • 0029790141 scopus 로고    scopus 로고
    • Do basic region-leucine zipper proteins bend their DNA targets...does it matter?
    • Hagerman, P.J. (1996). Do basic region-leucine zipper proteins bend their DNA targets...does it matter? Proc. Natl. Acad. Sci. USA 93, 9993-9996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9993-9996
    • Hagerman, P.J.1
  • 34
    • 0028050025 scopus 로고
    • 2 on specificity and comparison with binding of Myc family members
    • 2 on specificity and comparison with binding of Myc family members. Nucl. Acids Res. 22, 2801-2810.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 2801-2810
    • Bendall, A.J.1    Molloy, P.L.2
  • 35
    • 0027399193 scopus 로고
    • High affinity DNA-binding Myc analogs: Recognition by an α helix
    • Fisher, D.E., Parent, L.A. & Sharp, P.A. (1993). High affinity DNA-binding Myc analogs: recognition by an α helix. Cell 72, 467-476.
    • (1993) Cell , vol.72 , pp. 467-476
    • Fisher, D.E.1    Parent, L.A.2    Sharp, P.A.3
  • 36
    • 0026538243 scopus 로고
    • Molecular characterization of helix-loop-helix peptides
    • Anthony-Cahill, S.J., et al., & DeGrado, W.F. (1992). Molecular characterization of helix-loop-helix peptides. Science 255, 979-983.
    • (1992) Science , vol.255 , pp. 979-983
    • Anthony-Cahill, S.J.1    DeGrado, W.F.2
  • 38
    • 0028286549 scopus 로고
    • Isolation of phosphorylated calmodulin from rat liver and identification of the in vivo phosphorylation sites
    • Quadroni, M., James, P. & Carafoli, E. (1994). Isolation of phosphorylated calmodulin from rat liver and identification of the in vivo phosphorylation sites. J. Biol. Chem. 269, 16116-16122.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16116-16122
    • Quadroni, M.1    James, P.2    Carafoli, E.3
  • 39
    • 11944256565 scopus 로고
    • Mutational analysis of Max: Role of basic, helix-loop-helix/leucine zipper domains in DNA binding, dimerization and regulation of Myc-mediated transcriptional activation
    • Reddy, C.D., Dasgupta, P., Saikumar, P., Dudek, H., Rauscher, F.J. & Reddy, E.P. (1992). Mutational analysis of Max: role of basic, helix-loop-helix/leucine zipper domains in DNA binding, dimerization and regulation of Myc-mediated transcriptional activation. Oncogene 7, 2085-2092.
    • (1992) Oncogene , vol.7 , pp. 2085-2092
    • Reddy, C.D.1    Dasgupta, P.2    Saikumar, P.3    Dudek, H.4    Rauscher, F.J.5    Reddy, E.P.6
  • 40
    • 0028168627 scopus 로고
    • The dimerization stability of the HLH-LZ transcription protein family is modulated by the leucine zippers. A CD and NMR study of TEFB and c-Myc
    • Muhle-Goll, C., et al., & Pastore, A. (1994). The dimerization stability of the HLH-LZ transcription protein family is modulated by the leucine zippers. A CD and NMR study of TEFB and c-Myc. Biochemistry 33, 11296-11306.
    • (1994) Biochemistry , vol.33 , pp. 11296-11306
    • Muhle-Goll, C.1    Pastore, A.2
  • 41
    • 0025084602 scopus 로고
    • The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer
    • Gregor, P.D., Sawadodgo, M. & Roeder, R.G. (1990). The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer. Genes Dev. 4, 1730-1740.
    • (1990) Genes Dev. , vol.4 , pp. 1730-1740
    • Gregor, P.D.1    Sawadodgo, M.2    Roeder, R.G.3
  • 42
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B. & Sander, C. (1993). Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 43
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown cell constants
    • Kabsch, W.J. (1993). Automatic processing of rotation diffraction data from crystals of initially unknown cell constants. J. Appl. Cryst. 26, 795-800.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 44
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No.4
    • Collaborative Computational Project No.4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 45
    • 0003769049 scopus 로고
    • Yale University Press, New Haven, CT, USA
    • Brünger, A.T. (1992). X-PLOR, Version 3.1. Yale University Press, New Haven, CT, USA.
    • (1992) X-PLOR, Version 3.1
    • Brünger, A.1
  • 46
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A 42, 140-149.
    • (1986) Acta Cryst. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 47
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 48
    • 0001280470 scopus 로고
    • DEMON/ANGEL: A suite of programs to carry out density modifications
    • Vellieux, F.M.D.A., Hunt, J.F., Roy, S. & Read, R.J. (1995). DEMON/ANGEL: a suite of programs to carry out density modifications. J. Appl. Cryst. 28, 347-351.
    • (1995) J. Appl. Cryst. , vol.28 , pp. 347-351
    • Vellieux, F.M.D.A.1    Hunt, J.F.2    Roy, S.3    Read, R.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.