메뉴 건너뛰기




Volumn 17, Issue 14, 1998, Pages 4101-4113

Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme

Author keywords

Crystal form; Polymerase domain; T7 lysozyme; T7 RNA polymerase; Transcriptional inhibition

Indexed keywords

DNA POLYMERASE; LYSOZYME; RNA POLYMERASE;

EID: 0032527832     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.14.4101     Document Type: Article
Times cited : (155)

References (79)
  • 1
    • 0029692092 scopus 로고    scopus 로고
    • Preliminary characterization of crystals
    • Jones,C., Mulloy,B. and Sandersen,M.R (eds). Humana Press, Totowa, NJ
    • Abdel-Meguid,S.S., Jeruzalmi,D. and Sanderson,M.R. (1996) Preliminary characterization of crystals. In Jones,C., Mulloy,B. and Sandersen,M.R (eds), Crystallographic Methods and Protocols. Humana Press, Totowa, NJ, vol. 56, pp. 55-86.
    • (1996) Crystallographic Methods and Protocols , vol.56 , pp. 55-86
    • Abdel-Meguid, S.S.1    Jeruzalmi, D.2    Sanderson, M.R.3
  • 2
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement
    • Adams,P.D., Pannu,N.S., Read,R.J. and Brunger,A.T. (1997) Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement. Proc. Natl Acad. Sci. USA, 94, 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
  • 3
    • 0028932883 scopus 로고
    • Structures of DNA and RNA polymerases and their interactions with nucleic acid substrates
    • Arnold,E., Ding,J., Hughes,S. and Hostomsky,Z. (1995) Structures of DNA and RNA polymerases and their interactions with nucleic acid substrates. Curr. Opin. Struct. Biol., 5, 27-38.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 27-38
    • Arnold, E.1    Ding, J.2    Hughes, S.3    Hostomsky, Z.4
  • 4
    • 0027412196 scopus 로고
    • ALSCRIPT - A tool to format multiple sequence alignments
    • Barton,G.J. (1993) ALSCRIPT - A tool to format multiple sequence alignments. Protein Eng., 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 5
    • 0026733634 scopus 로고
    • Mutations in T7 RNA polymerase that support the proposal for a common polymerase active site structure
    • Bonner,G., Patra,D., Lafer,E. and Sousa,R. (1992) Mutations in T7 RNA polymerase that support the proposal for a common polymerase active site structure, EMBO J., 11, 3767-3775.
    • (1992) EMBO J. , vol.11 , pp. 3767-3775
    • Bonner, G.1    Patra, D.2    Lafer, E.3    Sousa, R.4
  • 6
    • 0028027513 scopus 로고
    • Characterization of a set of T7 RNA polymerase active site mutants
    • Bonner,G., Lafer,E.M. and Sousa,R. (1994a) Characterization of a set of T7 RNA polymerase active site mutants. J. Biol. Chem., 269, 25120-25128.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25120-25128
    • Bonner, G.1    Lafer, E.M.2    Sousa, R.3
  • 7
    • 0027959469 scopus 로고
    • The thumb subdomain of T7 RNA polymerase functions to stabilize the ternary complex during processive transcription
    • Bonner,G., Lafer,E.M. and Sousa,R. (1994b) The thumb subdomain of T7 RNA polymerase functions to stabilize the ternary complex during processive transcription. J. Biol. Chem., 269, 25129-25136.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25129-25136
    • Bonner, G.1    Lafer, E.M.2    Sousa, R.3
  • 8
    • 0032005866 scopus 로고    scopus 로고
    • Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes
    • Brautigam,CA. and Steitz,T.A. (1998) Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes. Curr. Opin. Struct. Biol. 8, 54-63.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 54-63
    • Brautigam, C.A.1    Steitz, T.A.2
  • 9
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quality for assessing the accuracy of crystal structures
    • Brunger,A.T. (1992) The free R value: A novel statistical quality for assessing the accuracy of crystal structures. Nature, 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brunger, A.T.1
  • 10
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system (CNS): A new software suite for macromolecular structure determination
    • in press
    • Brunger,A.T. et al. (1998) Crystallography and NMR system (CNS): A new software suite for macromolecular structure determination. Acta Crystallogr., D in press.
    • (1998) Acta Crystallogr., D
    • Brunger, A.T.1
  • 12
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • CCP4 (1994) The CCP4 Suite: Programs for protein crystallography. Acta Crystallogr., D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 13
    • 0028223308 scopus 로고
    • The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase
    • Cheng,X.D., Zhang,X., Pflugrath,J.W. and Studier,F.W. (1994) The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase, Proc. Natl Acad. Sci. USA, 91, 4034-4038.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4034-4038
    • Cheng, X.D.1    Zhang, X.2    Pflugrath, J.W.3    Studier, F.W.4
  • 14
    • 0028797896 scopus 로고
    • The direct rotation function: Global correlation search applied to molecular replacement
    • in press
    • Delano,W.L. and Brunger,A.T. (1995) The direct rotation function: Global correlation search applied to molecular replacement. Acta Crystallogr., D in press.
    • (1995) Acta Crystallogr., D
    • Delano, W.L.1    Brunger, A.T.2
  • 16
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage replication complex at 2.2 Å resolution
    • Doublie,S., Tabor,S., Long,A.M., Richardson,C.C. and Ellenberger,T. (1998) Crystal structure of a bacteriophage replication complex at 2.2 Å resolution. Nature, 391, 251-257.
    • (1998) Nature , vol.391 , pp. 251-257
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 17
    • 0030592095 scopus 로고    scopus 로고
    • Structure of Taq polymerase with DNA at the polymerase active site
    • Eom,S.H., Wang,J. and Steitz,T.A. (1996) Structure of Taq polymerase with DNA at the polymerase active site. Nature, 382, 278-281.
    • (1996) Nature , vol.382 , pp. 278-281
    • Eom, S.H.1    Wang, J.2    Steitz, T.A.3
  • 18
    • 0026728955 scopus 로고
    • The single-nucleotide addition cycle in transcription: A biophysical and biochemical perspective
    • Erie,D.A., Yager,T.D. and von-Hippel,P.H. (1992) The single-nucleotide addition cycle in transcription: A biophysical and biochemical perspective. Annu. Rev. Biophys. Biomol. Struct., 21, 379-415.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 379-415
    • Erie, D.A.1    Yager, T.D.2    Von-Hippel, P.H.3
  • 19
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf,R. (1997) An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph., 15, 133-138.
    • (1997) J. Mol. Graph. , vol.15 , pp. 133-138
    • Esnouf, R.1
  • 20
    • 0029653518 scopus 로고
    • Whole-genome random sequencing and assembly of Haemophilus influenzae
    • Fleischmann,R.D. et al. (1995) Whole-genome random sequencing and assembly of Haemophilus influenzae. Science, 269, 496-512.
    • (1995) Science , vol.269 , pp. 496-512
    • Fleischmann, R.D.1
  • 21
    • 0031028380 scopus 로고    scopus 로고
    • Conferring RNA polymerase activity to a DNA polymerase: A single residue in reverse transcriptase controls substrate selection
    • Gao,G., Orlova,M., Georgiadis,M.M. and Hendrickson,W.A. (1997) Conferring RNA polymerase activity to a DNA polymerase: A single residue in reverse transcriptase controls substrate selection. Proc. Natl Acad. Sci. USA, 94, 407-411.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 407-411
    • Gao, G.1    Orlova, M.2    Georgiadis, M.M.3    Hendrickson, W.A.4
  • 22
    • 0030995087 scopus 로고    scopus 로고
    • Initiation, elongation and processivity of carboxyl-terminal mutants of T7 RNA polymerase
    • Gardner,L.P., Mookhtiar,K.A. and Coleman,J.E. (1997) Initiation, elongation and processivity of carboxyl-terminal mutants of T7 RNA polymerase. Biochemistry, 36, 2908-2918.
    • (1997) Biochemistry , vol.36 , pp. 2908-2918
    • Gardner, L.P.1    Mookhtiar, K.A.2    Coleman, J.E.3
  • 23
    • 0026678170 scopus 로고
    • Characterization of bacteriophage T7 RNA polymerase by linker insertion mutagenesis
    • Gross,L., Chen,W.-J. and McAllister,W.T. (1992) Characterization of bacteriophage T7 RNA polymerase by linker insertion mutagenesis. J. Mol. Biol. 228, 488-505.
    • (1992) J. Mol. Biol. , vol.228 , pp. 488-505
    • Gross, L.1    Chen, W.-J.2    McAllister, W.T.3
  • 24
    • 0031046587 scopus 로고    scopus 로고
    • A mutant T7 RNA polymerase that is defective in RNA binding and blocked in the early stages of transcription
    • He,B., Rong,M., Durbin,R.K, and McAllister,W.T. (1997) A mutant T7 RNA polymerase that is defective in RNA binding and blocked in the early stages of transcription. J. Mol. Biol., 265, 275-288.
    • (1997) J. Mol. Biol. , vol.265 , pp. 275-288
    • He, B.1    Rong, M.2    Durbin, R.K.3    McAllister, W.T.4
  • 25
    • 1842411934 scopus 로고    scopus 로고
    • Mitochondrial and chloroplast phage-type RNA polymerases in Arabidopsis
    • Hedtke,B,. Borner,T. and Weihe,A. (1997) Mitochondrial and chloroplast phage-type RNA polymerases in Arabidopsis. Science, 277, 809-811.
    • (1997) Science , vol.277 , pp. 809-811
    • Hedtke, B.1    Borner, T.2    Weihe, A.3
  • 26
    • 0028232955 scopus 로고
    • Searching protein structure databases has come of age
    • Holm,L. and Sander,C. (1994) Searching protein structure databases has come of age. Proteins, 19, 165-173.
    • (1994) Proteins , vol.19 , pp. 165-173
    • Holm, L.1    Sander, C.2
  • 27
    • 0026739250 scopus 로고
    • Inhibition of T7 RNA polymerase by T7 lysozyme in vitro
    • Ikeda,R. and Bailey,P.A. (1992) Inhibition of T7 RNA polymerase by T7 lysozyme in vitro. J. Biol. Chem., 267, 20153-20158.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20153-20158
    • Ikeda, R.1    Bailey, P.A.2
  • 28
    • 0001210090 scopus 로고
    • Interactions of the RNA polymerase of bacteriophage T7 with its promoter during binding and initiation of transcription
    • Ikeda,R.A. and Richardson,C.C. (1986) Interactions of the RNA polymerase of bacteriophage T7 with its promoter during binding and initiation of transcription. Proc. Natl Acad. Sci. USA, 83, 3614-3618.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 3614-3618
    • Ikeda, R.A.1    Richardson, C.C.2
  • 29
    • 0023654282 scopus 로고
    • Enzymatic properties of a proteolytically nicked RNA polymerase of bacteriophage T7
    • Tkeda,R.A. and Richardson,C.C. (1987) Enzymatic properties of a proteolytically nicked RNA polymerase of bacteriophage T7. J. Biol. Chem., 262, 3790-3799.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3790-3799
    • Tkeda, R.A.1    Richardson, C.C.2
  • 30
    • 0015820033 scopus 로고
    • Bacteriophage T7 lysozyme is an N-acetylmuramyl-L-alanine amidase
    • Inouye,M., Arnheim,N. and Sternglanz,R. (1973) Bacteriophage T7 lysozyme is an N-acetylmuramyl-L-alanine amidase. J. Biol. Chem., 248, 7247-7252.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7247-7252
    • Inouye, M.1    Arnheim, N.2    Sternglanz, R.3
  • 31
    • 0027318776 scopus 로고
    • Crystal structure of Human Immunodeficiency Virus Type I reverse transcriptase complexed with double stranded DNA at 3.0 Å resolution shows bent DNA
    • Jacobo-Molina,A. et al. (1993) Crystal structure of Human Immunodeficiency Virus Type I reverse transcriptase complexed with double stranded DNA at 3.0 Å resolution shows bent DNA. Proc. Natl Acad. Sci. USA, 90, 6320-6324.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6320-6324
    • Jacobo-Molina, A.1
  • 32
    • 0031578707 scopus 로고    scopus 로고
    • Use of organic cosmotropic solutes to crystallize flexible proteins: Application to T7 RNA polymerase and its complex with the inhibitor T7 lysozyme
    • Jeruzalmi,D. and Steitz,T.A. (1997) Use of organic cosmotropic solutes to crystallize flexible proteins: application to T7 RNA polymerase and its complex with the inhibitor T7 lysozyme. J. Mol. Biol., 274, 748-756.
    • (1997) J. Mol. Biol. , vol.274 , pp. 748-756
    • Jeruzalmi, D.1    Steitz, T.A.2
  • 33
    • 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. and Kjeldgaard,M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr., 47, 110-119.
    • (1991) Acta Crystallogr. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 34
    • 0031042722 scopus 로고    scopus 로고
    • Choosing the right sugar: How polymerases select a nucleotide substrate
    • Joyce,C.M. (1997) Choosing the right sugar: How polymerases select a nucleotide substrate. Proc. Natl Acad. Sci. USA, 94, 1619-1622.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1619-1622
    • Joyce, C.M.1
  • 35
    • 0028206048 scopus 로고
    • Function and structure relationships in DNA polymerases
    • Joyce,C.M. and Steitz,T.A. (1994) Function and structure relationships in DNA polymerases. Annu. Rev. Biochem., 63, 777-822.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 777-822
    • Joyce, C.M.1    Steitz, T.A.2
  • 36
    • 0032518524 scopus 로고    scopus 로고
    • Visualizing DNA replication in a analytically active bacillus DNA polymerase crystal
    • Kiefer,J.R., Mao,C., Braman,J.C. and Beese,L.S. (1998) Visualizing DNA replication in a analytically active bacillus DNA polymerase crystal. Nature, 391, 304-307.
    • (1998) Nature , vol.391 , pp. 304-307
    • Kiefer, J.R.1    Mao, C.2    Braman, J.C.3    Beese, L.S.4
  • 37
    • 0028983795 scopus 로고
    • Crystal structure of Thermus aquaticus DNA polymerase
    • Kim,Y., Eom,S.H., Wang,J., Lee,D.-S., Suh,S.W. and Steitz,T.A. (1995) Crystal structure of Thermus aquaticus DNA polymerase. Nature, 376, 612-616.
    • (1995) Nature , vol.376 , pp. 612-616
    • Kim, Y.1    Eom, S.H.2    Wang, J.3    Lee, D.-S.4    Suh, S.W.5    Steitz, T.A.6
  • 38
    • 0030497978 scopus 로고    scopus 로고
    • Efficient rebuilding of protein structures
    • Kleywegt,G.J. and Jones,T.A. (1996) Efficient rebuilding of protein structures. Acta Crystallogr., D52, 829-832.
    • (1996) Acta Crystallogr. , vol.D52 , pp. 829-832
    • Kleywegt, G.J.1    Jones, T.A.2
  • 39
    • 0031574325 scopus 로고    scopus 로고
    • Not your average density
    • Kleywegt,G.J. and Read,R.J. (1998) Not your average density. Structure, 5, 1557-1569.
    • (1998) Structure , vol.5 , pp. 1557-1569
    • Kleywegt, G.J.1    Read, R.J.2
  • 40
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt,L.A., Wang,J., Friedman,J.M., Rice,P.A. and Steitz,T.A. (1992) Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science, 256, 1783-1790.
    • (1992) Science , vol.256 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 42
    • 0030666087 scopus 로고    scopus 로고
    • Inhibition of T7 RNA polymerase: Transcription initiation and transition from initiation to elongation are inhibited by T7 lysozyme via a ternary complex with RNA polymerase and promoter DNA
    • Kumar,A. and Patel,S.S. (1997) Inhibition of T7 RNA polymerase: Transcription initiation and transition from initiation to elongation are inhibited by T7 lysozyme via a ternary complex with RNA polymerase and promoter DNA. Biochemistry, 36, 13945-13962.
    • (1997) Biochemistry , vol.36 , pp. 13945-13962
    • Kumar, A.1    Patel, S.S.2
  • 43
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski,R.A., MacArthur,M.W., Moss,D.S. and Thornton,J.M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 44
    • 0024977953 scopus 로고
    • Abortive initiation by bacteriophage T3 and T7 RNA polymerases under conditions of limiting substrate
    • Ling,M.-I., Risman,S.S., Klement,J.F., McGraw,N. and McAllister,W.T. (1989) Abortive initiation by bacteriophage T3 and T7 RNA polymerases under conditions of limiting substrate. Nucleic Acids Res., 17, 1605-1619.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 1605-1619
    • Ling, M.-I.1    Risman, S.S.2    Klement, J.F.3    McGraw, N.4    McAllister, W.T.5
  • 45
    • 0027764344 scopus 로고
    • Protein sequence alignments; A strategy for the hierarchical analysis of residue conservation
    • Livingstone,C.D. and Barton,G.J. (1993) Protein sequence alignments; a strategy for the hierarchical analysis of residue conservation. Comput. Appl. Biosci. 9, 745-756.
    • (1993) Comput. Appl. Biosci. , vol.9 , pp. 745-756
    • Livingstone, C.D.1    Barton, G.J.2
  • 47
    • 0023924749 scopus 로고
    • Processivity in early stages of transcription by T7 RNA polymerase
    • Martin,C.T., Muller,D.K. and Coleman,J.E. (1988) Processivity in early stages of transcription by T7 RNA polymerase. Biochemistry. 27, 3966-3974.
    • (1988) Biochemistry , vol.27 , pp. 3966-3974
    • Martin, C.T.1    Muller, D.K.2    Coleman, J.E.3
  • 48
    • 0019778310 scopus 로고
    • Utilization of bacteriophage T7 late promoters in recombinant plasmids during infection
    • McAllister,W.T., Morris,C., Rosenberg,A.H. and Studier,F.W. (1981) Utilization of bacteriophage T7 late promoters in recombinant plasmids during infection. J. Mol. Biol., 153, 527-544.
    • (1981) J. Mol. Biol. , vol.153 , pp. 527-544
    • McAllister, W.T.1    Morris, C.2    Rosenberg, A.H.3    Studier, F.W.4
  • 49
    • 0017817821 scopus 로고
    • Regulation of transcription of the late genes of bacteriophage T7
    • McAllister,W.T. and Wu,H.-L. (1978) Regulation of transcription of the late genes of bacteriophage T7. Proc. Natl Acad. Sci. USA, 75, 804-808.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 804-808
    • McAllister, W.T.1    Wu, H.-L.2
  • 50
    • 0029784881 scopus 로고    scopus 로고
    • A thumb sub-domain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity and frameshift fidelity
    • Minnick,D.T., Astatke,M., Joyce,C.M. and Kunkel,T.A. (1996) A thumb sub-domain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity and frameshift fidelity. J. Biol. Chem., 271, 24954-24961.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24954-24961
    • Minnick, D.T.1    Astatke, M.2    Joyce, C.M.3    Kunkel, T.A.4
  • 51
    • 0023663369 scopus 로고
    • T7 Lysozyme inhibits transcription by T7 RNA polymerase
    • Moffat,B.A. and Studier,F.W. (1987) T7 Lysozyme inhibits transcription by T7 RNA polymerase. Cell, 49, 221-227.
    • (1987) Cell , vol.49 , pp. 221-227
    • Moffat, B.A.1    Studier, F.W.2
  • 53
    • 0023749703 scopus 로고
    • Processivity of proteolytically modified forms of T7 RNA polymerase
    • Muller,D.K., Martin,C.T. and Coleman,J.E. (1988) Processivity of proteolytically modified forms of T7 RNA polymerase. Biochemistry, 27, 5763-5771.
    • (1988) Biochemistry , vol.27 , pp. 5763-5771
    • Muller, D.K.1    Martin, C.T.2    Coleman, J.E.3
  • 54
    • 0000732609 scopus 로고
    • GRASP: Graphical representation and analysis of surface properties
    • Nicholls,A. Bharadwaj,R. and Honig,B. (1993) GRASP: Graphical representation and analysis of surface properties. Biophys. J., 64, A166.
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 55
    • 0021984004 scopus 로고
    • Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
    • Ollis,D.L., Brick,P., Hamlin,R., Xuong,N.G. and Steitz,T.A. (1985) Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Nature, 313, 762-766.
    • (1985) Nature , vol.313 , pp. 762-766
    • Ollis, D.L.1    Brick, P.2    Hamlin, R.3    Xuong, N.G.4    Steitz, T.A.5
  • 56
    • 0026763294 scopus 로고
    • Asp 357, Asp 812 are essential and Lys 631. His 811 are catalytically significant in bacteriophage T7 RNA polymerase activity
    • Osumi-Davis,P.A., Aguilera,M.C.D., Woody,R.W. and Woody,A.Y.M. (1992) Asp 357, Asp 812 are essential and Lys 631. His 811 are catalytically significant in bacteriophage T7 RNA polymerase activity. J. Mol. Biol., 226, 37-45.
    • (1992) J. Mol. Biol. , vol.226 , pp. 37-45
    • Osumi-Davis, P.A.1    Aguilera, M.C.D.2    Woody, R.W.3    Woody, A.Y.M.4
  • 57
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • Pannu,N.S. and Read,R.J. (1996) Improved structure refinement through maximum likelihood. Acta Crystallogr., A52, 659-668.
    • (1996) Acta Crystallogr. , vol.A52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 58
    • 0026533557 scopus 로고
    • Isolation and characterization of mutant bacteriophage T7 RNA polymerases
    • Patra,D., Lafer,E.M. and Sousa,R. (1992) Isolation and characterization of mutant bacteriophage T7 RNA polymerases. J. Mol. Biol., 224, 307-318.
    • (1992) J. Mol. Biol. , vol.224 , pp. 307-318
    • Patra, D.1    Lafer, E.M.2    Sousa, R.3
  • 59
    • 0028049441 scopus 로고
    • Structures of ternary complexes of rat DNA polymerase β, a DNA template-primer and ddCTP
    • Pelletier,H., Sawaya,M.R., Kumar,A., Wilson,S.H. and Kraut,J. (1994) Structures of ternary complexes of rat DNA polymerase β, a DNA template-primer and ddCTP. Science, 264, 1891-1903.
    • (1994) Science , vol.264 , pp. 1891-1903
    • Pelletier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 60
    • 0026619462 scopus 로고
    • Substitution of a single bacteriophage T3 residue in bacteriophage T7 RNA polymerase at position 748 results in a switch in promoter specificity
    • Raskin,C.A., Diaz,G., Joho,K. and McAllister,W.T. (1992) Substitution of a single bacteriophage T3 residue in bacteriophage T7 RNA polymerase at position 748 results in a switch in promoter specificity. J. Mol. Biol., 228, 506-515.
    • (1992) J. Mol. Biol. , vol.228 , pp. 506-515
    • Raskin, C.A.1    Diaz, G.2    Joho, K.3    McAllister, W.T.4
  • 65
    • 0026051447 scopus 로고
    • Studies on the interaction of T7 RNA polymerase with a DNA template containing a site specifically placed Psoralen cross-link I. characterization of elongation complexes
    • Sastry,S.S. and Hearst,J.E. (1991) Studies on the interaction of T7 RNA polymerase with a DNA template containing a site specifically placed Psoralen cross-link I. characterization of elongation complexes. J. Mol. Biol., 221, 1091-1110.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1091-1110
    • Sastry, S.S.1    Hearst, J.E.2
  • 66
    • 0026606938 scopus 로고
    • Model for the mechanism of bacteriophage T7 RNAP transcription initiation and termination
    • Sousa,R., Patra,D. and Lafer,E.M. (1992) Model for the mechanism of bacteriophage T7 RNAP transcription initiation and termination. J. Mol. Biol., 224, 319-334.
    • (1992) J. Mol. Biol. , vol.224 , pp. 319-334
    • Sousa, R.1    Patra, D.2    Lafer, E.M.3
  • 67
    • 0027163526 scopus 로고
    • Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution
    • Sousa,R., Chung,Y.J., Rose,J.P. and Wang,B.-C. (1993) Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution. Nature, 364, 593-599.
    • (1993) Nature , vol.364 , pp. 593-599
    • Sousa, R.1    Chung, Y.J.2    Rose, J.P.3    Wang, B.-C.4
  • 68
    • 0028035156 scopus 로고
    • The Thumb's Knuckle. Flexibility in the thumb subdomain of T7 RNA polymerase is revealed by the structure of a chimeric T7/T3 RNA polymerase
    • Sousa,R., Rose,J. and Wang,B.C. (1994) The Thumb's Knuckle. Flexibility in the thumb subdomain of T7 RNA polymerase is revealed by the structure of a chimeric T7/T3 RNA polymerase. J. Mol. Biol., 244, 6-12.
    • (1994) J. Mol. Biol. , vol.244 , pp. 6-12
    • Sousa, R.1    Rose, J.2    Wang, B.C.3
  • 69
    • 0027411261 scopus 로고
    • DNA- And RNA-dependent DNA polymerases
    • Steitz,J.A. (1993) DNA- and RNA-dependent DNA polymerases. Curr. Opin. Struct. Biol., 3, 31-38.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 31-38
    • Steitz, J.A.1
  • 70
    • 0028606031 scopus 로고
    • A unified polymerase mechanism for nonhomologous DNA and RNA polymerases
    • Steitz,J.A., Smerdon,S.J., Jaeger,J. and Joyce,C.M. (1994) A unified polymerase mechanism for nonhomologous DNA and RNA polymerases. Science, 266, 2022-2025.
    • (1994) Science , vol.266 , pp. 2022-2025
    • Steitz, J.A.1    Smerdon, S.J.2    Jaeger, J.3    Joyce, C.M.4
  • 71
    • 0015526899 scopus 로고
    • Bacteriophage T7
    • Studier,F.W. (1972) Bacteriophage T7. Science, 176, 367-376.
    • (1972) Science , vol.176 , pp. 367-376
    • Studier, F.W.1
  • 73
    • 0030605509 scopus 로고    scopus 로고
    • The biochemistry of transcription in eukaryotes: A paradigm for multisubunit regulatory complexes
    • Tjian,R. (1996) The biochemistry of transcription in eukaryotes: a paradigm for multisubunit regulatory complexes. Philos. Trans. R. Soc. Lond. B Biol. Sci., 351, 491-499.
    • (1996) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.351 , pp. 491-499
    • Tjian, R.1
  • 74
    • 0031558759 scopus 로고    scopus 로고
    • Identification of a minimal binding element within the T7 RNA polymerase promoter
    • Ujvari,A. and Martin,C.T. (1997) Identification of a minimal binding element within the T7 RNA polymerase promoter. J. Mol. Biol., 273, 775-781.
    • (1997) J. Mol. Biol. , vol.273 , pp. 775-781
    • Ujvari, A.1    Martin, C.T.2
  • 75
    • 0001280470 scopus 로고
    • DEMON/ ANGEL: A suite of programs to carry out density modification
    • Vellieux,F.M.D.A.P., Hunt,J.F. Roy,S. and Read,R.J. (1995) DEMON/ ANGEL: A suite of programs to carry out density modification. J. Appl. Crystallogr., 28, 347-351.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 347-351
    • Vellieux, F.M.D.A.P.1    Hunt, J.F.2    Roy, S.3    Read, R.J.4
  • 76
    • 0021154435 scopus 로고
    • Protein-nucleic acid interactions in transcription: A molecular analysis
    • von-Hippel,P.H., Bear,D.G., Morgan,W.D. and McSwiggen,J.A. (1984) Protein-nucleic acid interactions in transcription: A molecular analysis. Annu. Rev. Biochem., 53, 389-416.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 389-416
    • Von-Hippel, P.H.1    Bear, D.G.2    Morgan, W.D.3    McSwiggen, J.A.4
  • 77
    • 0031587827 scopus 로고    scopus 로고
    • Crystal structure of a pol α family replication DNA polymerase from bacteriophage RB69
    • Wang,J., Sattar,A.K.M., Wang,C.C. and Steitz,T.A. (1997) Crystal structure of a pol α family replication DNA polymerase from bacteriophage RB69. Cell, 89, 1087-1099.
    • (1997) Cell , vol.89 , pp. 1087-1099
    • Wang, J.1    Sattar, A.K.M.2    Wang, C.C.3    Steitz, T.A.4
  • 79
    • 0031591384 scopus 로고    scopus 로고
    • Mechanism of inhibition of bacteriophage T7 RNA polymerase by T7 lysozyme
    • Zhang,X. and Studier,F.W. (1997) Mechanism of inhibition of bacteriophage T7 RNA polymerase by T7 lysozyme. J. Mol. Biol., 269, 10-27.
    • (1997) J. Mol. Biol. , vol.269 , pp. 10-27
    • Zhang, X.1    Studier, F.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.