메뉴 건너뛰기




Volumn 391, Issue 6668, 1998, Pages 660-666

Crystal structure of the yeast MATα2/MCM1/DNA ternary complex

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HOMEODOMAIN PROTEIN; TRANSCRIPTION FACTOR;

EID: 0032509980     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35563     Document Type: Article
Times cited : (198)

References (42)
  • 1
    • 0028103855 scopus 로고
    • Homeodomain-DNA recognition
    • Gehring, W. J. et al. Homeodomain-DNA recognition. Cell 78, 211-223 (1994).
    • (1994) Cell , vol.78 , pp. 211-223
    • Gehring, W.J.1
  • 2
    • 0029109864 scopus 로고
    • Homeodomain proteins. Cooperating to be different
    • Wilson, D. S. & Desplan, C. Homeodomain proteins. Cooperating to be different. Curr. Biol. 5, 32-34 (1995).
    • (1995) Curr. Biol. , vol.5 , pp. 32-34
    • Wilson, D.S.1    Desplan, C.2
  • 4
    • 0030220608 scopus 로고    scopus 로고
    • Protein interactions of homeodomain proteins
    • Vershon, A. K. Protein interactions of homeodomain proteins. Curr. Opin. Biotechnol. 7, 392-396 (1996).
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 392-396
    • Vershon, A.K.1
  • 5
    • 0029154633 scopus 로고
    • Molecular mechanisms of cell-type determination in budding yeast
    • Johnson, A. D. Molecular mechanisms of cell-type determination in budding yeast. Curr. Opin. Genet. Dev. 5, 552-558 (1995).
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 552-558
    • Johnson, A.D.1
  • 6
    • 0024052649 scopus 로고
    • Flexibility of the yeast alpha 2 repressor enables it to occupy the ends of its operator, leaving the center free
    • Sauer, R. T., Smith, D. L. & Johnson, A. D. Flexibility of the yeast alpha 2 repressor enables it to occupy the ends of its operator, leaving the center free. Genes Dev. 2, 807-816 (1988).
    • (1988) Genes Dev. , vol.2 , pp. 807-816
    • Sauer, R.T.1    Smith, D.L.2    Johnson, A.D.3
  • 7
    • 0023272433 scopus 로고
    • Homeodomain of the yeast repressor alpha 2 is a sequence-specific DNA-binding domain but is not sufficient for repression
    • Hall, M. N. & Johnson, A. D. Homeodomain of the yeast repressor alpha 2 is a sequence-specific DNA-binding domain but is not sufficient for repression. Science 237, 1007-1012 (1987).
    • (1987) Science , vol.237 , pp. 1007-1012
    • Hall, M.N.1    Johnson, A.D.2
  • 8
    • 0028034201 scopus 로고
    • The WD repeats of Tup1 interact with the homeodomain protein alpha 2
    • Komachi, K., Redd, M. J. & Johnson, A. D. The WD repeats of Tup1 interact with the homeodomain protein alpha 2. Genes Dev. 8, 2857-2867 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 2857-2867
    • Komachi, K.1    Redd, M.J.2    Johnson, A.D.3
  • 9
    • 0026002757 scopus 로고
    • Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions
    • Wolberger, C. Vershon, A. K., Liu, B., Johnson, A. D. & Pabo, C. O. Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions. Cell 67, 517-528 (1991).
    • (1991) Cell , vol.67 , pp. 517-528
    • Wolberger, C.1    Vershon, A.K.2    Liu, B.3    Johnson, A.D.4    Pabo, C.O.5
  • 10
    • 0025754413 scopus 로고
    • Secondary structure of the homeodomain of yeast alpha 2 repressor determined by NMR spectroscopy
    • Phillips, C. L., Vershon, A. K., Johnson, A. D. & Dahlquist, F. W. Secondary structure of the homeodomain of yeast alpha 2 repressor determined by NMR spectroscopy. Genes. Dev. 5, 764-772 (1991).
    • (1991) Genes. Dev. , vol.5 , pp. 764-772
    • Phillips, C.L.1    Vershon, A.K.2    Johnson, A.D.3    Dahlquist, F.W.4
  • 11
    • 0027496093 scopus 로고
    • The carboxy-terminal tail of the homeodomain protein alpha 2 is required for function with a second homeodomain protein
    • Mak, A. & Johnson, A. D. The carboxy-terminal tail of the homeodomain protein alpha 2 is required for function with a second homeodomain protein. Genes Dev. 7, 1862-1870 (1993).
    • (1993) Genes Dev. , vol.7 , pp. 1862-1870
    • Mak, A.1    Johnson, A.D.2
  • 12
    • 0028828745 scopus 로고
    • Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA
    • Li, T., Stark, M. R., Johnson, A. D. & Wolberger, C. Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA. Science 270, 262-269 (1995).
    • (1995) Science , vol.270 , pp. 262-269
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4
  • 13
    • 0026267950 scopus 로고
    • A new role for MCM1 in yeast cell cycle regulation of SW15 transcription
    • Lydall, D., Ammerer, G. & Nasmyth, K. A new role for MCM1 in yeast cell cycle regulation of SW15 transcription. Genes Dev. 5, 2405-2519 (1991).
    • (1991) Genes Dev. , vol.5 , pp. 2405-2519
    • Lydall, D.1    Ammerer, G.2    Nasmyth, K.3
  • 14
    • 0024165602 scopus 로고
    • Saccharomyces cerevisiae protein involved in plasmid maintenance is necessary for mating of MAT alpha cells
    • Passmore, S., Maine, G. T., Elble, R., Christ, C. & Tye, B. K. Saccharomyces cerevisiae protein involved in plasmid maintenance is necessary for mating of MAT alpha cells. J. Mol. Biol. 204, 593-606 (1988).
    • (1988) J. Mol. Biol. , vol.204 , pp. 593-606
    • Passmore, S.1    Maine, G.T.2    Elble, R.3    Christ, C.4    Tye, B.K.5
  • 15
    • 0031053706 scopus 로고    scopus 로고
    • Multiple phosphorylated forms of the Saccharomyces cerevisiae Mcm1 protein include an isoform induced in response to high salt concentrations
    • Kuo, M. H., Nadeau, E. T. & Grayhack, E. J. Multiple phosphorylated forms of the Saccharomyces cerevisiae Mcm1 protein include an isoform induced in response to high salt concentrations. Mol. Cell. Biol. 17, 819-832 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 819-832
    • Kuo, M.H.1    Nadeau, E.T.2    Grayhack, E.J.3
  • 16
    • 0028799428 scopus 로고
    • Mcm1 is required to coordinate G2-specific transcription in Saccharomyces cerevisiae
    • Althoefer, H., Schleiffer, A., Wassmann, K., Nordheim, A. & Ammerer, G. Mcm1 is required to coordinate G2-specific transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 15, 5917-5928 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5917-5928
    • Althoefer, H.1    Schleiffer, A.2    Wassmann, K.3    Nordheim, A.4    Ammerer, G.5
  • 17
    • 0029038733 scopus 로고
    • Cell cycle-regulated transcription of the CLB2 gene is dependent on Mcm1 and a ternary complex factor
    • Maher, M., Cong, F., Kindelberger, D., Nasmyth, K. & Dalton, S. Cell cycle-regulated transcription of the CLB2 gene is dependent on Mcm1 and a ternary complex factor. Mol. Cell. Biol. 15, 3129-3137 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3129-3137
    • Maher, M.1    Cong, F.2    Kindelberger, D.3    Nasmyth, K.4    Dalton, S.5
  • 18
    • 0025804652 scopus 로고
    • Functional domains of the yeast transcription/replication factor MCM1
    • Christ, C. & Tye, B. K. Functional domains of the yeast transcription/replication factor MCM1. Genes Dev. 5, 751-763 (1991).
    • (1991) Genes Dev. , vol.5 , pp. 751-763
    • Christ, C.1    Tye, B.K.2
  • 19
    • 0025930897 scopus 로고
    • The DNA binding and oligomerization domain of MCM1 is sufficient for its interaction with other regulatory proteins
    • Primig, M., Winkler, H. & Ammerer, G. The DNA binding and oligomerization domain of MCM1 is sufficient for its interaction with other regulatory proteins. EMBO J. 10, 4209-4218 (1991).
    • (1991) EMBO J. , vol.10 , pp. 4209-4218
    • Primig, M.1    Winkler, H.2    Ammerer, G.3
  • 20
    • 0028934434 scopus 로고
    • The MADS-box family of transcription factors
    • Shore, P. & Sharrocks, A. D. The MADS-box family of transcription factors. Eur. J. Biochem. 229, 1-13 (1995).
    • (1995) Eur. J. Biochem. , vol.229 , pp. 1-13
    • Shore, P.1    Sharrocks, A.D.2
  • 21
    • 0029102041 scopus 로고
    • Structure of serum response factor core bound to DNA
    • Pellegrini, L., Tan, S. & Richmond, T. J. Structure of serum response factor core bound to DNA. Nature 376, 490-498 (1995).
    • (1995) Nature , vol.376 , pp. 490-498
    • Pellegrini, L.1    Tan, S.2    Richmond, T.J.3
  • 22
    • 0026571502 scopus 로고
    • A molecular mechanism for combinatorial control in yeast: MCM1 protein sets the spacing and orientation of the homeodomains of an alpha 2 dimer
    • Smith, D. L. & Johnson, A. D. A molecular mechanism for combinatorial control in yeast: MCM1 protein sets the spacing and orientation of the homeodomains of an alpha 2 dimer. Cell 68, 133-142 (1992).
    • (1992) Cell , vol.68 , pp. 133-142
    • Smith, D.L.1    Johnson, A.D.2
  • 23
    • 0027509952 scopus 로고
    • A short, disordered protein region mediates interactions between the homeodomain of the yeast alpha 2 protein and the MCM1 protein
    • Vershon, A. K. & Johnson, A. D. A short, disordered protein region mediates interactions between the homeodomain of the yeast alpha 2 protein and the MCM1 protein. Cell 72, 105-112 (1993).
    • (1993) Cell , vol.72 , pp. 105-112
    • Vershon, A.K.1    Johnson, A.D.2
  • 24
    • 0024290441 scopus 로고
    • The yeast cell-type specific repressor alpha 2 acts cooperatively with a non-cell-type-specific protein
    • Keleher, C. A., Goutte, C. & Johnson, A. D. The yeast cell-type specific repressor alpha 2 acts cooperatively with a non-cell-type-specific protein. Cell 53, 927-936 (1988).
    • (1988) Cell , vol.53 , pp. 927-936
    • Keleher, C.A.1    Goutte, C.2    Johnson, A.D.3
  • 25
    • 0024396954 scopus 로고
    • Yeast repressor alpha 2 binds to its operator cooperatively with yeast protein Mcm1
    • Keleher, C. A., Passmore, S. & Johnson, A. D. Yeast repressor alpha 2 binds to its operator cooperatively with yeast protein Mcm1. Mol. Cell Biol. 9, 5228-5230 (1989).
    • (1989) Mol. Cell Biol. , vol.9 , pp. 5228-5230
    • Keleher, C.A.1    Passmore, S.2    Johnson, A.D.3
  • 26
    • 0029664658 scopus 로고    scopus 로고
    • The yeast alpha2 and Mcm1 proteins interact through a region similar to a motif found in homeodomain proteins of higher eukaryotes
    • Mead, J., Zhong, H., Acton, T. B. & Vershon, A. K. The yeast alpha2 and Mcm1 proteins interact through a region similar to a motif found in homeodomain proteins of higher eukaryotes. Mol. Cell. Biol. 16, 2135-2143 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2135-2143
    • Mead, J.1    Zhong, H.2    Acton, T.B.3    Vershon, A.K.4
  • 27
    • 0029865623 scopus 로고    scopus 로고
    • Context-dependent secondary structure formation of a designed protein sequence
    • Minor, D. L. Jr & Kim, P. S. Context-dependent secondary structure formation of a designed protein sequence. Nature 380, 730-734 (1996).
    • (1996) Nature , vol.380 , pp. 730-734
    • Minor Jr., D.L.1    Kim, P.S.2
  • 28
    • 0026723896 scopus 로고
    • SRF and MCM1 have related but distinct DNA binding specificities
    • Wynne, J. & Treisman, R. SRF and MCM1 have related but distinct DNA binding specificities. Nucleic Acids Res. 20, 3297-3303 (1992).
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3297-3303
    • Wynne, J.1    Treisman, R.2
  • 29
    • 0030950532 scopus 로고    scopus 로고
    • DNA-binding specificity of Mcm1: Operator mutations that alter DNA-bending and transcriptional activities by a MADS box protein
    • Acton, T. B., Zhong, H. & Vershon, A. K. DNA-binding specificity of Mcm1: operator mutations that alter DNA-bending and transcriptional activities by a MADS box protein. Mol. Cell. Biol. 17, 1881-1889 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1881-1889
    • Acton, T.B.1    Zhong, H.2    Vershon, A.K.3
  • 30
    • 0030889410 scopus 로고    scopus 로고
    • The yeast homeodomain protein Mat alpha 2 shows extended DNA binding specificity in complex with Mcml
    • Zhong, H. L. & Vershon, A. K. The yeast homeodomain protein Mat alpha 2 shows extended DNA binding specificity in complex with Mcml. J. Biol. Chem. 272, 8402-8409 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 8402-8409
    • Zhong, H.L.1    Vershon, A.K.2
  • 31
    • 0031591393 scopus 로고    scopus 로고
    • Electrostatics and hydration at the homeodomain DNA interface: Chemical probes of an interfacial water cavity
    • Labeots, L. A. & Weiss, M. A. Electrostatics and hydration at the homeodomain DNA interface: chemical probes of an interfacial water cavity. J. Mol. Biol. 269, 113-128 (1997).
    • (1997) J. Mol. Biol. , vol.269 , pp. 113-128
    • Labeots, L.A.1    Weiss, M.A.2
  • 32
    • 0028329225 scopus 로고
    • MCM1 point mutants deficient in expression of alpha-specific genes residues important for interaction with alpha 1
    • Bruhn, L. & Sprague, G. F. Jr MCM1 point mutants deficient in expression of alpha-specific genes residues important for interaction with alpha 1. Mol. Cell. Biol. 14, 2534-2544 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2534-2544
    • Bruhn, L.1    Sprague Jr., G.F.2
  • 33
    • 0030587932 scopus 로고    scopus 로고
    • An alpha to beta conformational switch in EF-Tu
    • Abel, K., Yoder, M. D., Hilgenfeld, R. & Jurnak, F. An alpha to beta conformational switch in EF-Tu. Structure 4, 1153-1159 (1996).
    • (1996) Structure , vol.4 , pp. 1153-1159
    • Abel, K.1    Yoder, M.D.2    Hilgenfeld, R.3    Jurnak, F.4
  • 34
    • 0030587857 scopus 로고    scopus 로고
    • Helix unwinding in the effector region of elongation factor EF-Tu-GDP
    • Polekhina, G. et al. Helix unwinding in the effector region of elongation factor EF-Tu-GDP. Structure 4, 1141-1151 (1996).
    • (1996) Structure , vol.4 , pp. 1141-1151
    • Polekhina, G.1
  • 35
    • 0030159797 scopus 로고    scopus 로고
    • The structural puzzle of how serpin serine proteinase inhibitors work
    • Wright, H. T. The structural puzzle of how serpin serine proteinase inhibitors work. BioEssays 18, 453-464 (1996).
    • (1996) BioEssays , vol.18 , pp. 453-464
    • Wright, H.T.1
  • 36
    • 0031055820 scopus 로고    scopus 로고
    • Amyloid fibrils. Mutations make enzyme polymerize
    • Perutz, M. F. Amyloid fibrils. Mutations make enzyme polymerize. Nature 385, 773-775 (1997).
    • (1997) Nature , vol.385 , pp. 773-775
    • Perutz, M.F.1
  • 37
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 38
  • 39
    • 84945074880 scopus 로고
    • Conjugate-direction minimization: An improved method for the refinement of macromolecules
    • Tronrud, D. E. Conjugate-direction minimization: an improved method for the refinement of macromolecules. Acta Crystallogr. A 48, 912-916 (1992).
    • (1992) Acta Crystallogr. A , vol.48 , pp. 912-916
    • Tronrud, D.E.1
  • 41
    • 0024058085 scopus 로고
    • The definition of generalised helicoidal parameters and of axis curvature for irregular nucleic acids
    • Lavery, R. & Sklenar, H. The definition of generalised helicoidal parameters and of axis curvature for irregular nucleic acids. J. Biomol. Struct. Dynam. 6, 63-91 (1988).
    • (1988) J. Biomol. Struct. Dynam. , vol.6 , pp. 63-91
    • Lavery, R.1    Sklenar, H.2
  • 42
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.