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Volumn 17, Issue 9, 1997, Pages 5369-5376

Conformational changes induced in Hoxb-8/Pbx-1 heterodimers in solution and upon interaction with specific DNA

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; HOMEODOMAIN PROTEIN; PLASMID DNA;

EID: 1842414314     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.9.5369     Document Type: Article
Times cited : (22)

References (36)
  • 1
    • 0027966927 scopus 로고
    • The DNA binding specificity of ultrabithorax is modulated by cooperative interactions with extradenticle, another homeodomain protein
    • Chan, S.-K., L. Jaffe, M. Capovilla, J. Botas, and R. S. Mann. 1994. The DNA binding specificity of ultrabithorax is modulated by cooperative interactions with extradenticle, another homeodomain protein. Cell 78:603-615.
    • (1994) Cell , vol.78 , pp. 603-615
    • Chan, S.-K.1    Jaffe, L.2    Capovilla, M.3    Botas, J.4    Mann, R.S.5
  • 2
    • 0029925624 scopus 로고    scopus 로고
    • An extradenticle-induced conformational change in a HOX protein overcomes an inhibitory function of the conserved hexapeptide motif
    • Chan, S.-K., H. Pöpperl, R. Krumlauf, and R. S. Mann. 1996. An extradenticle-induced conformational change in a HOX protein overcomes an inhibitory function of the conserved hexapeptide motif. EMBO J. 15:2476-2487.
    • (1996) EMBO J. , vol.15 , pp. 2476-2487
    • Chan, S.-K.1    Pöpperl, H.2    Krumlauf, R.3    Mann, R.S.4
  • 3
    • 0028947525 scopus 로고
    • Pbx proteins display hexapeptide-dependent cooperative DNA binding with a subset of Hox proteins
    • Chang, C.-P., W.-F. Shen, S. Rozenfeld, H. J. Lawrence, C. Largman, and M. L. Cleary. 1995. Pbx proteins display hexapeptide-dependent cooperative DNA binding with a subset of Hox proteins. Genes Dev. 9:663-674.
    • (1995) Genes Dev. , vol.9 , pp. 663-674
    • Chang, C.-P.1    Shen, W.-F.2    Rozenfeld, S.3    Lawrence, H.J.4    Largman, C.5    Cleary, M.L.6
  • 4
    • 0029939199 scopus 로고    scopus 로고
    • Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus
    • Chang, C.-P., L. Brocchieri, W.-F. Shen, C. Largman, and M. L. Cleary. 1996. Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus. Mol. Cell. Biol. 16:1734-1745.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1734-1745
    • Chang, C.-P.1    Brocchieri, L.2    Shen, W.-F.3    Largman, C.4    Cleary, M.L.5
  • 5
    • 0027197205 scopus 로고
    • Dpbx, a new homeobox gene closely related to the human proto-oncogene pbx1: Molecular structure and developmental expression
    • Flegel, W. A., A. W. Singson, J. S. Margolis, A. G. Bang, J. W. Posakony, and C. Murre. 1993. Dpbx, a new homeobox gene closely related to the human proto-oncogene pbx1: molecular structure and developmental expression. Mech. Dev. 41:155-161.
    • (1993) Mech. Dev. , vol.41 , pp. 155-161
    • Flegel, W.A.1    Singson, A.W.2    Margolis, J.S.3    Bang, A.G.4    Posakony, J.W.5    Murre, C.6
  • 6
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S., and P. von Hippel. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.1    Von Hippel, P.2
  • 7
    • 0027527069 scopus 로고
    • Yeast a1 and α2 homeodomain proteins form a DNA-binding activity with properties distinct from those of either protein
    • Goutte, C., and A. D. Johnson. 1993. Yeast a1 and α2 homeodomain proteins form a DNA-binding activity with properties distinct from those of either protein. J. Mol. Biol. 233:359-371.
    • (1993) J. Mol. Biol. , vol.233 , pp. 359-371
    • Goutte, C.1    Johnson, A.D.2
  • 8
    • 0025254308 scopus 로고
    • Sequence-specific DNA binding of the proto-oncoprotein ets-1 defines a transcriptional activator sequence within the long terminal repeat of the Moloney murine sarcoma virus
    • Gunther, C., J. Nye, R. Bryner, and B. Graves. 1990. Sequence-specific DNA binding of the proto-oncoprotein ets-1 defines a transcriptional activator sequence within the long terminal repeat of the Moloney murine sarcoma virus. Genes Dev. 4:667-679.
    • (1990) Genes Dev. , vol.4 , pp. 667-679
    • Gunther, C.1    Nye, J.2    Bryner, R.3    Graves, B.4
  • 9
    • 0001294043 scopus 로고
    • A combinatorial regulatory circuit in budding yeast
    • S. L. McKnight and K. R. Yamamoto (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Johnson, A. 1992. A combinatorial regulatory circuit in budding yeast, p. 975-1006. In S. L. McKnight and K. R. Yamamoto (ed.), Transcriptional regulation. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1992) Transcriptional Regulation , pp. 975-1006
    • Johnson, A.1
  • 10
    • 0028809109 scopus 로고
    • Extradenticle protein is a selective cofactor for the Drosophila homeotics: Role of the homeodomain and YPWM amino acid motif in the interaction
    • Johnson, F. B., E. Parker, and M. A. Krasnow. 1995. extradenticle protein is a selective cofactor for the Drosophila homeotics: role of the homeodomain and YPWM amino acid motif in the interaction. Proc. Natl. Acad. Sci. USA 92:739-743.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 739-743
    • Johnson, F.B.1    Parker, E.2    Krasnow, M.A.3
  • 11
    • 0029118224 scopus 로고
    • The pentapeptide motif of Hox proteins is required for cooperative DNA binding with Pbx1, physically contacts Pbx1, and enhances DNA binding by Pbx1
    • Knoepfler, P. S., and M. P. Kamps. 1995. The pentapeptide motif of Hox proteins is required for cooperative DNA binding with Pbx1, physically contacts Pbx1, and enhances DNA binding by Pbx1. Mol. Cell. Biol. 15:5811-5819.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5811-5819
    • Knoepfler, P.S.1    Kamps, M.P.2
  • 12
    • 0027953771 scopus 로고
    • Hox genes in vertebrate development
    • Krumlauf, R. 1994. Hox genes in vertebrate development. Cell 78:191-201.
    • (1994) Cell , vol.78 , pp. 191-201
    • Krumlauf, R.1
  • 14
    • 0028828745 scopus 로고
    • Crystal structure of the MATa1/MATα2 homeodomain heterodimer bound to DNA
    • Li, T., M. R. Stark, A. D. Johnson, and C. Wolberger. 1995. Crystal structure of the MATa1/MATα2 homeodomain heterodimer bound to DNA. Science 270:262-269.
    • (1995) Science , vol.270 , pp. 262-269
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4
  • 15
    • 0029054140 scopus 로고
    • Both Pbx1 and E2A-Pbx1 bind the DNA motif ATCAATCAA cooperatively with the products of multiple murine Hox genes, some of which are oncogenes themselves
    • Lu, Q., P. S. Knoepfler, J. Scheele, D. D. Wright, and M. P. Kamps. 1995. Both Pbx1 and E2A-Pbx1 bind the DNA motif ATCAATCAA cooperatively with the products of multiple murine Hox genes, some of which are oncogenes themselves. Mol. Cell. Biol. 15:3786-3795.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3786-3795
    • Lu, Q.1    Knoepfler, P.S.2    Scheele, J.3    Wright, D.D.4    Kamps, M.P.5
  • 16
    • 0029966661 scopus 로고    scopus 로고
    • Structural determinants within Pbx1 that mediate cooperative DNA binding with pentapeptide-containing Hox proteins: Proposal for a model of a Pbx1-Hox-DNA complex
    • Lu, Q., and M. P. Kamps. 1996. Structural determinants within Pbx1 that mediate cooperative DNA binding with pentapeptide-containing Hox proteins: proposal for a model of a Pbx1-Hox-DNA complex. Mol. Cell. Biol. 16:1632-1640.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1632-1640
    • Lu, Q.1    Kamps, M.P.2
  • 17
    • 0027496093 scopus 로고
    • The carboxy-terminal tail of the homeo domain protein alpha 1 is required for function with a second homeo domain protein
    • Mak, A., and A. Johnson. 1993. The carboxy-terminal tail of the homeo domain protein alpha 1 is required for function with a second homeo domain protein. Genes Dev. 7:1862-1870.
    • (1993) Genes Dev. , vol.7 , pp. 1862-1870
    • Mak, A.1    Johnson, A.2
  • 18
    • 0026066608 scopus 로고
    • PBX2 and PBX3, new homeohox genes with extensive homology to the human proto-oncogene PBX1
    • Monica, K., N. Galili, J. Nourse, D. Saltman, and M. L. Cleary. 1991. PBX2 and PBX3, new homeohox genes with extensive homology to the human proto-oncogene PBX1. Mol. Cell. Biol. 11:6149-6157.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 6149-6157
    • Monica, K.1    Galili, N.2    Nourse, J.3    Saltman, D.4    Cleary, M.L.5
  • 19
    • 0029079663 scopus 로고
    • The hexapeptide LFPWMR in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins
    • Neuteboom, S. T. C., L. T. C. Peltenburg, M. A. van Dijk, and C. Murre. 1945. The hexapeptide LFPWMR in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins. Proc. Natl. Acad. Sci. USA 92:9166-9170.
    • (1945) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9166-9170
    • Neuteboom, S.T.C.1    Peltenburg, L.T.C.2    Van Dijk, M.A.3    Murre, C.4
  • 20
    • 0029048413 scopus 로고
    • Structure of BamHI endonuclease bound to DNA: Partial folding and unfolding on DNA binding
    • Newman, M., T. Strzelecka, L. F. Dorner, I. Schildkraut, and A. K. Aggarwal. 1995. Structure of BamHI endonuclease bound to DNA: partial folding and unfolding on DNA binding. Science 269:656-663.
    • (1995) Science , vol.269 , pp. 656-663
    • Newman, M.1    Strzelecka, T.2    Dorner, L.F.3    Schildkraut, I.4    Aggarwal, A.K.5
  • 21
    • 0030001665 scopus 로고    scopus 로고
    • Characterization of the interaction between RhoGDI and Cdc42Hs using fluorescence spectroscopy
    • Nomanbhoy, T. K., and R. A. Cerione. 1996. Characterization of the interaction between RhoGDI and Cdc42Hs using fluorescence spectroscopy. J. Biol. Chem. 271:10004-10009.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10004-10009
    • Nomanbhoy, T.K.1    Cerione, R.A.2
  • 22
    • 0025182484 scopus 로고
    • Design of DNA-binding peptides based on the leucine zipper motif
    • O'Neil, K., R. Hoess, and W. Degrado. 1990. Design of DNA-binding peptides based on the leucine zipper motif. Science 249:774-778.
    • (1990) Science , vol.249 , pp. 774-778
    • O'Neil, K.1    Hoess, R.2    Degrado, W.3
  • 23
    • 0028868441 scopus 로고
    • The pancreatic islet factor STF-1 binds cooperatively with Pbx to a regulatory element in the somatostatin promoter: Importance of the FPWMK motif and of the homeodomain
    • Peers, B., S. Sharma, T. Johnson, M. P. Kamps, and M. Montminy. 1995. The pancreatic islet factor STF-1 binds cooperatively with Pbx to a regulatory element in the somatostatin promoter: importance of the FPWMK motif and of the homeodomain. Mol. Cell. Biol. 15:7091-7097.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7091-7097
    • Peers, B.1    Sharma, S.2    Johnson, T.3    Kamps, M.P.4    Montminy, M.5
  • 24
    • 0030035691 scopus 로고    scopus 로고
    • Engrailed and Hox homeodomain proteins contain a related Pbx interaction motif that recognizes a common structure present in Pbx
    • Peltenburg, L. T. C., and C. Murre. 1996. Engrailed and Hox homeodomain proteins contain a related Pbx interaction motif that recognizes a common structure present in Pbx. EMBO J. 15:3385-3393.
    • (1996) EMBO J. , vol.15 , pp. 3385-3393
    • Peltenburg, L.T.C.1    Murre, C.2
  • 25
    • 0030894303 scopus 로고    scopus 로고
    • Specific residues in the Pbx homeodomain differentially modulate the DNA-binding activity of Hox and Engrailed proteins
    • Peltenburg, L. T. C., and C. Murre. 1997. Specific residues in the Pbx homeodomain differentially modulate the DNA-binding activity of Hox and Engrailed proteins. Development 124:1089-1098.
    • (1997) Development , vol.124 , pp. 1089-1098
    • Peltenburg, L.T.C.1    Murre, C.2
  • 26
    • 0028874393 scopus 로고
    • Modulation of transcription factor Ets-1 DNA binding: DNA-induced unfolding of an α helix
    • Petersen, J. M., J. J. Skalicky, L. W. Donaldson, L. P. McIntosh, T. Alber, and B. J. Graves. 1995. Modulation of transcription factor Ets-1 DNA binding: DNA-induced unfolding of an α helix. Science 269:1866-1869.
    • (1995) Science , vol.269 , pp. 1866-1869
    • Petersen, J.M.1    Skalicky, J.J.2    Donaldson, L.W.3    McIntosh, L.P.4    Alber, T.5    Graves, B.J.6
  • 27
    • 0029008293 scopus 로고
    • Cooperative interactions between Hox and Pbx proteins mediated by a conserved peptide motif
    • Phelan, M. L., I. Rambaldi, and M. S. Featherstone. 1995. Cooperative interactions between Hox and Pbx proteins mediated by a conserved peptide motif. Mol. Cell. Biol. 15:3989-3997.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3989-3997
    • Phelan, M.L.1    Rambaldi, I.2    Featherstone, M.S.3
  • 28
    • 0029055810 scopus 로고
    • Segmental expression of Hoxb-1 iscontrolled by a highly conserved autoregulatory loop dependent upon exd/phx
    • Pöpperl, H., M. Bienz, M. Studer, S.-K. Chan, S. Aparicio, S. Brenner, R. S. Mann, and R. Krumlauf. 1995. Segmental expression of Hoxb-1 iscontrolled by a highly conserved autoregulatory loop dependent upon exd/phx. Cell 81:1031-1042.
    • (1995) Cell , vol.81 , pp. 1031-1042
    • Pöpperl, H.1    Bienz, M.2    Studer, M.3    Chan, S.-K.4    Aparicio, S.5    Brenner, S.6    Mann, R.S.7    Krumlauf, R.8
  • 29
    • 0027519720 scopus 로고
    • Extradenticle, a regulator of homeotic gene activity, is a homolog of the homeobox-containing human proto-oncogene pbex1
    • Rauskolb, C., M. Peifer, and E. Wieschaus. 1993. Extradenticle, a regulator of homeotic gene activity, is a homolog of the homeobox-containing human proto-oncogene pbex1. Cell 74:1101-1112.
    • (1993) Cell , vol.74 , pp. 1101-1112
    • Rauskolb, C.1    Peifer, M.2    Wieschaus, E.3
  • 30
    • 0029863755 scopus 로고    scopus 로고
    • GroEL binds to and unfolds Rhodanese posttranslationally
    • Reid, B. G., and G. C. Flynn. 1996. GroEL binds to and unfolds Rhodanese posttranslationally. J. Biol. Chem. 271:7212-7217.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7212-7217
    • Reid, B.G.1    Flynn, G.C.2
  • 33
    • 0029865110 scopus 로고    scopus 로고
    • Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors
    • Shen, F., S. J. Triezenberg, P. Hensley, D. Porter, and J. R. Knutson. 1996. Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors. J. Biol. Chem. 271:4827-4837.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4827-4837
    • Shen, F.1    Triezenberg, S.J.2    Hensley, P.3    Porter, D.4    Knutson, J.R.5
  • 34
    • 0028169993 scopus 로고
    • Extradenticle raises the DNA binding specificity of homeotic selector gene products
    • van Dijk, M. A., and C. Murre. 1994. extradenticle raises the DNA binding specificity of homeotic selector gene products. Cell 78:617-624.
    • (1994) Cell , vol.78 , pp. 617-624
    • Van Dijk, M.A.1    Murre, C.2
  • 35
    • 0029160039 scopus 로고
    • Hox gene products modulate the DNA binding activity of Pbx1 and Pbx2
    • van Dijk, M. A., L. T. C. Peltenburg, and C. Murre. 1995. Hox gene products modulate the DNA binding activity of Pbx1 and Pbx2. Mech. Dev. 52:99-108.
    • (1995) Mech. Dev. , vol.52 , pp. 99-108
    • Van Dijk, M.A.1    Peltenburg, L.T.C.2    Murre, C.3
  • 36
    • 0025045635 scopus 로고
    • Thermal unfolding studies of a leucine zipper domain and its specific DNA complex. Implications for scissors grip recognition
    • Weiss, M. A. 1990. Thermal unfolding studies of a leucine zipper domain and its specific DNA complex. Implications for scissors grip recognition. Biochemistry 29:8020-8024.
    • (1990) Biochemistry , vol.29 , pp. 8020-8024
    • Weiss, M.A.1


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