메뉴 건너뛰기




Volumn 13, Issue 1, 2004, Pages 45-53

Structure of a Ternary Transcription Activation Complex

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DNA; PROTEIN DERIVATIVE; PROTEIN LAMBDA CL; RNA POLYMERASE; RNA POLYMERASE SIGMA SUBUNIT DOMAIN 4; UNCLASSIFIED DRUG;

EID: 1642441938     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(03)00483-0     Document Type: Article
Times cited : (74)

References (43)
  • 1
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement
    • Adams P.D., Pannu N.S., Read R.J., Brunger A.T. Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement. Proc. Natl. Acad. Sci. USA. 94:1997;5018-5023.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5018-5023
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brunger, A.T.4
  • 2
    • 44949289693 scopus 로고
    • Crystallization of DNA binding proteins with oligodeoxynucleotides
    • Aggarwal A.K. Crystallization of DNA binding proteins with oligodeoxynucleotides. Methods. 1:1990;83-90.
    • (1990) Methods , vol.1 , pp. 83-90
    • Aggarwal, A.K.1
  • 3
    • 0026657433 scopus 로고
    • Refined 1.8 Å crystal structure of the λ repressor-operator complex
    • Beamer L.J., Pabo C.O. Refined 1.8 Å crystal structure of the λ repressor-operator complex. J. Mol. Biol. 227:1992;177-196.
    • (1992) J. Mol. Biol. , vol.227 , pp. 177-196
    • Beamer, L.J.1    Pabo, C.O.2
  • 5
    • 0024462398 scopus 로고
    • A single glutamic acid residue plays a key role in the transcriptional activation function of lambda repressor
    • Bushman F.D., Shang C., Ptashne M. A single glutamic acid residue plays a key role in the transcriptional activation function of lambda repressor. Cell. 58:1989;1163-1171.
    • (1989) Cell , vol.58 , pp. 1163-1171
    • Bushman, F.D.1    Shang, C.2    Ptashne, M.3
  • 7
    • 0002583957 scopus 로고
    • Dm-density modification package
    • Cowtan K. Dm-density modification package. Joint CCP. 4(and ESF-EACBM Newsletter on Protein Crystallography 31):1994;34-38.
    • (1994) Joint CCP , vol.4 , Issue.AND ESF-EACBM NEWSLETTER ON PROTEIN CRYSTALLOGRAPHY 31 , pp. 34-38
    • Cowtan, K.1
  • 8
    • 0032491380 scopus 로고    scopus 로고
    • DNA footprints of the two kinetically significant intermediates in formation of an RNA polymerase-promoter open complex: Evidence that interactions with start site and downstream DNA induce sequential conformational changes in polymerase and DNA
    • Craig M.L., Tsodikov O.V., McQuade K.L., Schlax P.E.J., Capp M.W., Saecker R.M., Record M.T.J. DNA footprints of the two kinetically significant intermediates in formation of an RNA polymerase-promoter open complex. evidence that interactions with start site and downstream DNA induce sequential conformational changes in polymerase and DNA J. Mol. Biol. 283:1998;741-756.
    • (1998) J. Mol. Biol. , vol.283 , pp. 741-756
    • Craig, M.L.1    Tsodikov, O.V.2    McQuade, K.L.3    Schlax, P.E.J.4    Capp, M.W.5    Saecker, R.M.6    Record, M.T.J.7
  • 9
    • 0034700165 scopus 로고    scopus 로고
    • Mechanism for a transcriptional activator that works at the isomerization step
    • Dove S.L., Huang F.W., Hochschild A. Mechanism for a transcriptional activator that works at the isomerization step. Proc. Natl. Acad. Sci. USA. 97:2000;13215-13220.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13215-13220
    • Dove, S.L.1    Huang, F.W.2    Hochschild, A.3
  • 10
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276:1997;523-530.
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublie, S.1
  • 12
    • 0020490669 scopus 로고
    • Mechanism of activation of transcription initiation from the lambda PRM promoter
    • Hawley D.K., McClure W.R. Mechanism of activation of transcription initiation from the lambda PRM promoter. J. Mol. Biol. 157:1982;493-525.
    • (1982) J. Mol. Biol. , vol.157 , pp. 493-525
    • Hawley, D.K.1    McClure, W.R.2
  • 13
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson W.A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science. 254:1991;51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 14
    • 0032489504 scopus 로고    scopus 로고
    • Protein-protein contacts that activate and repress prokaryotic transcription
    • Hochschild A., Dove S.L. Protein-protein contacts that activate and repress prokaryotic transcription. Cell. 92:1998;597-600.
    • (1998) Cell , vol.92 , pp. 597-600
    • Hochschild, A.1    Dove, S.L.2
  • 15
    • 0020713848 scopus 로고
    • Repressor structure and the mechanism of positive control
    • Hochschild A., Irwin N., Ptashne M. Repressor structure and the mechanism of positive control. Cell. 32:1983;319-325.
    • (1983) Cell , vol.32 , pp. 319-325
    • Hochschild, A.1    Irwin, N.2    Ptashne, M.3
  • 17
    • 0018880549 scopus 로고
    • Bacteriophage lambda repressor and cro protein: Interactions with operator DNA
    • Johnson A.D., Pabo C.O., Sauer R.T. Bacteriophage lambda repressor and cro protein. interactions with operator DNA Methods Enzymol. 65:1980;839-856.
    • (1980) Methods Enzymol. , vol.65 , pp. 839-856
    • Johnson, A.D.1    Pabo, C.O.2    Sauer, R.T.3
  • 18
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron denstiy maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S., Kjeldgaard M. Improved methods for building protein models in electron denstiy maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 19
    • 0023645694 scopus 로고
    • The 0°C closed complexes between Escherichia coli RNA polymerase and two promoters, T7-A3 and lacUV5
    • Kovacic R.T. The 0°C closed complexes between Escherichia coli RNA polymerase and two promoters, T7-A3 and lacUV5. J. Biol. Chem. 262:1987;13654-13661.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13654-13661
    • Kovacic, R.T.1
  • 20
    • 0026354983 scopus 로고
    • DNase I-induced DNA conformation. 2 Å structure of a DNase I-octamer complex
    • Lahm A., Suck D. DNase I-induced DNA conformation. 2 Å structure of a DNase I-octamer complex. J. Mol. Biol. 222:1991;645-667.
    • (1991) J. Mol. Biol. , vol.222 , pp. 645-667
    • Lahm, A.1    Suck, D.2
  • 22
    • 0024058085 scopus 로고
    • The definition of generalized helicoidal parameters and of axis curvature for irregular nucleic acids
    • Lavery R., Sklenar H. The definition of generalized helicoidal parameters and of axis curvature for irregular nucleic acids. J. Biomol. Struct. Dyn. 6:1988;63-91.
    • (1988) J. Biomol. Struct. Dyn. , vol.6 , pp. 63-91
    • Lavery, R.1    Sklenar, H.2
  • 23
    • 0032483359 scopus 로고    scopus 로고
    • Characterization of the closed complex intermediate formed during transcription initiation by Escherichia coli RNA polymerase
    • Li X.-Y., McClure W.R. Characterization of the closed complex intermediate formed during transcription initiation by Escherichia coli RNA polymerase. J. Biol. Chem. 273:1998;23549-23557.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23549-23557
    • Li, X.-Y.1    McClure, W.R.2
  • 24
    • 0028197624 scopus 로고
    • Target of the transcriptional activation function of phage lambda cI protein
    • Li M., Moyle H., Susskind M.M. Target of the transcriptional activation function of phage lambda cI protein. Science. 263:1994;75-77.
    • (1994) Science , vol.263 , pp. 75-77
    • Li, M.1    Moyle, H.2    Susskind, M.M.3
  • 25
    • 0030890936 scopus 로고    scopus 로고
    • Changing the mechanism of transcriptional activation by phage λ repressor
    • Li M., McClure W.R., Susskind M.M. Changing the mechanism of transcriptional activation by phage λ repressor. Proc. Natl. Acad. Sci. USA. 94:1997;3691-3696.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3691-3696
    • Li, M.1    McClure, W.R.2    Susskind, M.M.3
  • 26
    • 0021591396 scopus 로고
    • Mechanism of CRP-cAMP activation of lac operon transcription initiation activation of the P1 promoter
    • Malan T.P., Kolb A., Buc H., McClure W.R. Mechanism of CRP-cAMP activation of lac operon transcription initiation activation of the P1 promoter. J. Mol. Biol. 180:1984;881-909.
    • (1984) J. Mol. Biol. , vol.180 , pp. 881-909
    • Malan, T.P.1    Kolb, A.2    Buc, H.3    McClure, W.R.4
  • 27
    • 0021891874 scopus 로고
    • Mechanism and control of transcription initiation in prokaryotes
    • McClure W.R. Mechanism and control of transcription initiation in prokaryotes. Annu. Rev. Biochem. 54:1985;171-204.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 171-204
    • McClure, W.R.1
  • 29
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme/DNA complex
    • Murakami K., Masuda S., Campbell E.A., Muzzin O., Darst S.A. Structural basis of transcription initiation. An RNA polymerase holoenzyme/DNA complex Science. 296:2002;1285-1290.
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.A.5
  • 30
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by maximum-likelihood method. Acta Crystallogr. D. 53:1997;240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 32
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy-atom parameters in isomorphous replacement and anomalous scattering
    • A.G.W. Leslie. Warrington, UK: SERC Daresbury Laboratory
    • Otwinowski Z. Maximum likelihood refinement of heavy-atom parameters in isomorphous replacement and anomalous scattering. Leslie A.G.W. Proceedings of the CCP4 Study Weekend. 1991;80-86 SERC Daresbury Laboratory, Warrington, UK.
    • (1991) Proceedings of the CCP4 Study Weekend , pp. 80-86
    • Otwinowski, Z.1
  • 33
    • 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. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0038522852 scopus 로고    scopus 로고
    • An intersubunit contact stimulating transcription initiation by E. coli RNA polymerase: Interaction of the α C-terminal domain and σ region 4
    • Ross W., Schneider D.A., Paul B.J., Mertens A., Gourse R.L. An intersubunit contact stimulating transcription initiation by E. coli RNA polymerase. Interaction of the α C-terminal domain and σ region 4 Genes Dev. 17:2003;1293-1307.
    • (2003) Genes Dev. , vol.17 , pp. 1293-1307
    • Ross, W.1    Schneider, D.A.2    Paul, B.J.3    Mertens, A.4    Gourse, R.L.5
  • 37
    • 0032486385 scopus 로고    scopus 로고
    • Activation and repression of transcription by differential contact: Two sides of a coin
    • Roy S., Garges S., Adhya S. Activation and repression of transcription by differential contact. two sides of a coin J. Biol. Chem. 273:1998;14059- 14062.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14059-14062
    • Roy, S.1    Garges, S.2    Adhya, S.3
  • 38
    • 0000058799 scopus 로고
    • Lambda repressor recognizes the approximately 2-fold symmetric half-operator sequences asymmetrically
    • Sarai A., Takeda Y. Lambda repressor recognizes the approximately 2-fold symmetric half-operator sequences asymmetrically. Proc. Natl. Acad. Sci. USA. 86:1989;6513-6517.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6513-6517
    • Sarai, A.1    Takeda, Y.2
  • 39
    • 0018386029 scopus 로고
    • Regulatory functions of the lambda repressor reside in the amino-terminal domain
    • Sauer R.T., Pabo C.O., Meyer B.J., Ptashne M., Backman K.C. Regulatory functions of the lambda repressor reside in the amino-terminal domain. Nature. 279:1979;396-400.
    • (1979) Nature , vol.279 , pp. 396-400
    • Sauer, R.T.1    Pabo, C.O.2    Meyer, B.J.3    Ptashne, M.4    Backman, K.C.5
  • 40
    • 0018867360 scopus 로고
    • E. coli RNA polymerase interacts homologously with two different promoters
    • Siebenlist U., Simpson R.B., Gilbert W. E. coli RNA polymerase interacts homologously with two different promoters. Cell. 20:1980;269-281.
    • (1980) Cell , vol.20 , pp. 269-281
    • Siebenlist, U.1    Simpson, R.B.2    Gilbert, W.3
  • 41
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • Weeks C.M., Miller R. The design and implementation of SnB v2.0. J. App. Crystallogr. 32:1999;120-124.
    • (1999) J. App. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 42
    • 0032529668 scopus 로고    scopus 로고
    • Genetic analysis of prokaryotic and eukaryotic DNA-binding proteins in Escherichia coli
    • Whipple F.W. Genetic analysis of prokaryotic and eukaryotic DNA-binding proteins in Escherichia coli. Nucleic Acids Res. 26:1998;3700-3706.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3700-3706
    • Whipple, F.W.1
  • 43
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D. 57:2001;122-123.
    • (2001) Acta Crystallogr. D , vol.57 , pp. 122-123
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.