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Volumn 13, Issue 1, 2003, Pages 31-39

Bacterial RNA polymerases: The wholo story

Author keywords

[No Author keywords available]

Indexed keywords

HOLOENZYME; RNA POLYMERASE;

EID: 0037308665     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(02)00005-2     Document Type: Review
Times cited : (398)

References (57)
  • 1
    • 0027306799 scopus 로고
    • Genetics of RNA polymerases I, II, and III
    • Archambault J., Friesen J.D. Genetics of RNA polymerases I, II, and III. Microbiol. Rev. 57:1993;703-724.
    • (1993) Microbiol. Rev. , vol.57 , pp. 703-724
    • Archambault, J.1    Friesen, J.D.2
  • 2
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 Å resolution
    • Cramer P., Bushnell D.A., Kornberg R.D. Structural basis of transcription: RNA polymerase II at 2.8 Å resolution. Science. 292:2001;1863-1876.
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 3
    • 0000138962 scopus 로고    scopus 로고
    • RNA polymerase: Structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II
    • Ebright R.H. RNA polymerase: structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II. J. Mol. Biol. 293:2000;199-213.
    • (2000) J. Mol. Biol. , vol.293 , pp. 199-213
    • Ebright, R.H.1
  • 4
    • 0035970037 scopus 로고    scopus 로고
    • Bacterial RNA polymerase subunit ω and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly
    • Minakhin L., Bhagat S., Brunning A., Campbell E.A., Darst S.A., Ebright R.H., Severinov K. Bacterial RNA polymerase subunit ω and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly. Proc. Natl. Acad. Sci. U.S.A. 98:2001;892-897.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 892-897
    • Minakhin, L.1    Bhagat, S.2    Brunning, A.3    Campbell, E.A.4    Darst, S.A.5    Ebright, R.H.6    Severinov, K.7
  • 5
    • 0032504132 scopus 로고    scopus 로고
    • Structure of the Escherichia coli RNA polymerase α subunit amino-terminal domain
    • Zhang G., Darst S.A. Structure of the Escherichia coli RNA polymerase α subunit amino-terminal domain. Science. 281:1998;262-266.
    • (1998) Science , vol.281 , pp. 262-266
    • Zhang, G.1    Darst, S.A.2
  • 6
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
    • Zhang G., Campbell E.A., Minakhin L., Richter C., Severinov K., Darst S.A. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution. Cell. 98:1999;811-824.
    • (1999) Cell , vol.98 , pp. 811-824
    • Zhang, G.1    Campbell, E.A.2    Minakhin, L.3    Richter, C.4    Severinov, K.5    Darst, S.A.6
  • 8
    • 0036468364 scopus 로고    scopus 로고
    • Multisubunit RNA polymerases
    • Cramer P. Multisubunit RNA polymerases. Curr. Opin. Struct. Biol. 12:2002;89-97.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 89-97
    • Cramer, P.1
  • 11
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 Å resolution
    • Gnatt A.L., Cramer P., Fu J., Bushnell D.A., Kornberg R.D. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 Å resolution. Science. 292:2001;1876-1882.
    • (2001) Science , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 13
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution
    • 3.2 loop in abortive initiation.
    • 3.2 loop in abortive initiation.
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.S.1    Masuda, S.2    Darst, S.A.3
  • 15
    • 0037071844 scopus 로고    scopus 로고
    • Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 Å resolution
    • High-resolution (2.6 Å) structure of Tth RNAP holoenzyme, providing a wealth of detailed information.
    • Vassylyev D.G., Sekine S., Laptenko O., Lee J., Vassylyeva M.N., Borukhov S., Yokoyama S. Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 Å resolution. Nature. 417:2002;712-719 High-resolution (2.6 Å) structure of Tth RNAP holoenzyme, providing a wealth of detailed information.
    • (2002) Nature , vol.417 , pp. 712-719
    • Vassylyev, D.G.1    Sekine, S.2    Laptenko, O.3    Lee, J.4    Vassylyeva, M.N.5    Borukhov, S.6    Yokoyama, S.7
  • 17
    • 0031050795 scopus 로고    scopus 로고
    • 70-type sigma factors of group 1 and group 2
    • 70-type sigma factors of group 1 and group 2. J. Bacteriol. 179:1997;1734-1747.
    • (1997) J. Bacteriol. , vol.179 , pp. 1734-1747
    • Gruber, T.M.1    Bryant, D.A.2
  • 18
    • 0026612797 scopus 로고
    • 70 family: Sequence conservation and evolutionary relationships
    • 70 family: sequence conservation and evolutionary relationships. J. Bacteriol. 174:1992;3843-3849.
    • (1992) J. Bacteriol. , vol.174 , pp. 3843-3849
    • Lonetto, M.1    Gribskov, M.2    Gross, C.A.3
  • 19
    • 0025744584 scopus 로고
    • 70 and NusA proteins. I. Binding interactions with core RNA polymerase in solution and within the transcription complex
    • 70 and NusA proteins. I. Binding interactions with core RNA polymerase in solution and within the transcription complex. J. Mol. Biol. 220:1991;307-324.
    • (1991) J. Mol. Biol. , vol.220 , pp. 307-324
    • Gill, S.C.1    Weitzel, S.E.2    Von Hippel, P.H.3
  • 20
    • 0032578471 scopus 로고    scopus 로고
    • Promoter opening via a DNA fork junction binding activity
    • Guo Y., Gralla J.D. Promoter opening via a DNA fork junction binding activity. Proc. Natl. Acad. Sci. U.S.A. 95:1998;11655-11660.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 11655-11660
    • Guo, Y.1    Gralla, J.D.2
  • 21
    • 0037133615 scopus 로고    scopus 로고
    • Interaction of RNA polymerase with forked DNA: Evidence for two kinetically significant intermediates on the pathway to the final complex
    • Tsujikawa L., Tsodikov O., de Haseth P. Interaction of RNA polymerase with forked DNA: Evidence for two kinetically significant intermediates on the pathway to the final complex. Proc. Natl. Acad. Sci. U.S.A. 99:2002;3493-3498.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 3493-3498
    • Tsujikawa, L.1    Tsodikov, O.2    De Haseth, P.3
  • 27
    • 0030915128 scopus 로고    scopus 로고
    • Promoter recognition as measured by binding of polymerase to nontemplate strand oligonucleotide
    • Marr M.T., Roberts J.W. Promoter recognition as measured by binding of polymerase to nontemplate strand oligonucleotide. Science. 276:1997;1258-1260.
    • (1997) Science , vol.276 , pp. 1258-1260
    • Marr, M.T.1    Roberts, J.W.2
  • 28
    • 0028130508 scopus 로고
    • Mutations in sigma factor that affect the temperature dependence of transcription from a promoter, but not from a mismatch bubble in double-stranded DNA
    • Aiyar S.E., Juang Y.L., Helmann J.D., deHaseth P.L. Mutations in sigma factor that affect the temperature dependence of transcription from a promoter, but not from a mismatch bubble in double-stranded DNA. Biochemistry. 33:1994;11501-11506.
    • (1994) Biochemistry , vol.33 , pp. 11501-11506
    • Aiyar, S.E.1    Juang, Y.L.2    Helmann, J.D.3    DeHaseth, P.L.4
  • 29
    • 0028333908 scopus 로고
    • A promoter melting region in the primary σ factor of Bacillus subtilis: Identification of functionally important aromatic amino acids
    • Juang Y.-L., Helmann J.D. A promoter melting region in the primary σ factor of Bacillus subtilis: identification of functionally important aromatic amino acids. J. Mol. Biol. 235:1994;1470-1488.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1470-1488
    • Juang, Y.-L.1    Helmann, J.D.2
  • 30
    • 0028106101 scopus 로고
    • A mutants defective in promoter melting
    • A mutants defective in promoter melting. J. Bacteriol. 176:1994;5218-5224.
    • (1994) J. Bacteriol. , vol.176 , pp. 5218-5224
    • Rong, J.C.1    Helmann, J.D.2
  • 31
    • 0030965301 scopus 로고    scopus 로고
    • 70 subunit is responsible for the recognition of the 'extended -10' motif at promoters
    • 70 subunit is responsible for the recognition of the 'extended -10' motif at promoters. EMBO J. 16:1997;4034-4040.
    • (1997) EMBO J. , vol.16 , pp. 4034-4040
    • Barne, K.A.1    Bown, J.A.2    Busby, S.J.W.3    Minchin, S.D.4
  • 33
    • 0036384435 scopus 로고    scopus 로고
    • The TRTGn motif stabilizes the transcription initiation open complex
    • Voskuil M., Chambliss G. The TRTGn motif stabilizes the transcription initiation open complex. J. Mol. Biol. 322:2002;521-532.
    • (2002) J. Mol. Biol. , vol.322 , pp. 521-532
    • Voskuil, M.1    Chambliss, G.2
  • 35
    • 0027761839 scopus 로고
    • A third recognition element in bacterial promoters: DNA binding by the α subunit of RNA polymerase
    • Ross W., Gosink K., Salomon J., Igarashi K., Zou C., Ishihama A., Severinov K., Gourse R.L. A third recognition element in bacterial promoters: DNA binding by the α subunit of RNA polymerase. Science. 262:1993;1407-1413.
    • (1993) Science , vol.262 , pp. 1407-1413
    • Ross, W.1    Gosink, K.2    Salomon, J.3    Igarashi, K.4    Zou, C.5    Ishihama, A.6    Severinov, K.7    Gourse, R.L.8
  • 37
    • 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
  • 38
    • 0025785249 scopus 로고
    • Development of RNA polymerase-promoter contacts during open complex formation
    • Mecsas J., Cowing D.W., Gross C.A. Development of RNA polymerase-promoter contacts during open complex formation. J. Mol. Biol. 220:1991;585-597.
    • (1991) J. Mol. Biol. , vol.220 , pp. 585-597
    • Mecsas, J.1    Cowing, D.W.2    Gross, C.A.3
  • 39
    • 0025369026 scopus 로고
    • Topography of intermediates in transcription initiation of E. coli
    • Schickor P., Metzger W., Wladyslaw W., Lederer H., Heumann H. Topography of intermediates in transcription initiation of E. coli. EMBO J. 9:1990;2215-2220.
    • (1990) EMBO J. , vol.9 , pp. 2215-2220
    • Schickor, P.1    Metzger, W.2    Wladyslaw, W.3    Lederer, H.4    Heumann, H.5
  • 40
    • 0024022451 scopus 로고
    • Correlation between the conformation of Escherichia coli -10 hexamer sequences and promoter strength: Use of orthophenanthroline cuprous complex as a structural index
    • Spassky A., Rimsky S., Buc H., Busby S. Correlation between the conformation of Escherichia coli -10 hexamer sequences and promoter strength: use of orthophenanthroline cuprous complex as a structural index. EMBO J. 7:1988;1871-1879.
    • (1988) EMBO J. , vol.7 , pp. 1871-1879
    • Spassky, A.1    Rimsky, S.2    Buc, H.3    Busby, S.4
  • 42
    • 0028789430 scopus 로고
    • 2+ binding and its structural consequences at the transcription start site
    • 2+ binding and its structural consequences at the transcription start site. Biochemistry. 34:1995;15624-15632.
    • (1995) Biochemistry , vol.34 , pp. 15624-15632
    • Craig, M.L.1    Suh, W.-C.2    Record, M.T.J.3
  • 43
    • 0024463634 scopus 로고
    • A cinematographic view of Escherichia coli RNA polymerase translocation
    • Metzger W., Schickor P., Heumann H. A cinematographic view of Escherichia coli RNA polymerase translocation. EMBO J. 8:1989;2745-2754.
    • (1989) EMBO J. , vol.8 , pp. 2745-2754
    • Metzger, W.1    Schickor, P.2    Heumann, H.3
  • 44
    • 0029818631 scopus 로고    scopus 로고
    • Transcription processivity: Protein-DNA interactions holding together the elongation complex
    • Nudler E., Avetissova E., Markovtsov V., Goldfarb A. Transcription processivity: protein-DNA interactions holding together the elongation complex. Science. 273:1996;211-217.
    • (1996) Science , vol.273 , pp. 211-217
    • Nudler, E.1    Avetissova, E.2    Markovtsov, V.3    Goldfarb, A.4
  • 45
    • 0035943341 scopus 로고    scopus 로고
    • 70-retaining transcription elongation complexes from Escherichia coli
    • 70-retaining transcription elongation complexes from Escherichia coli. Cell. 106:2001;443-451.
    • (2001) Cell , vol.106 , pp. 443-451
    • Bar-Nahum, G.1    Nudler, E.2
  • 48
    • 0023029081 scopus 로고
    • Release of the sigma subunit of Escherichia coli DNA-dependent RNA polymerase depends mainly on time elapsed after the start of initiation, not on length of product RNA
    • Shimamoto N., Kamigochi T., Utiyama H. Release of the sigma subunit of Escherichia coli DNA-dependent RNA polymerase depends mainly on time elapsed after the start of initiation, not on length of product RNA. J. Biol. Chem. 261:1986;11859-11865.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11859-11865
    • Shimamoto, N.1    Kamigochi, T.2    Utiyama, H.3
  • 49
    • 0033823109 scopus 로고    scopus 로고
    • The orientation of DNA in an archaeal transcription initiation complex
    • Bartlett M.S., Thomm M., Geiduschek E.P. The orientation of DNA in an archaeal transcription initiation complex. Nat. Struct. Biol. 7:2000;782-785.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 782-785
    • Bartlett, M.S.1    Thomm, M.2    Geiduschek, E.P.3
  • 51
    • 0034625251 scopus 로고    scopus 로고
    • Structural organization of the RNA polymerase-promoter open complex
    • Naryshkin N., Revyakin A., Kim Y., Mekler V., Ebright R.H. Structural organization of the RNA polymerase-promoter open complex. Cell. 101:2000;601-611.
    • (2000) Cell , vol.101 , pp. 601-611
    • Naryshkin, N.1    Revyakin, A.2    Kim, Y.3    Mekler, V.4    Ebright, R.H.5
  • 52
    • 0035826258 scopus 로고    scopus 로고
    • A mechanism for initiating RNA-dependent RNA polymerization
    • The authors present the X-ray crystal structures of φ6 RNA-dependent RNAP and various complexes, delineating the mechanism of primer-independent initiation.
    • Butcher S.J., Grimes J.M., Makeyev E.V., Bamford D.H., Stuart D.I. A mechanism for initiating RNA-dependent RNA polymerization. Nature. 410:2001;235-240 The authors present the X-ray crystal structures of φ6 RNA-dependent RNAP and various complexes, delineating the mechanism of primer-independent initiation.
    • (2001) Nature , vol.410 , pp. 235-240
    • Butcher, S.J.1    Grimes, J.M.2    Makeyev, E.V.3    Bamford, D.H.4    Stuart, D.I.5
  • 53
    • 0037053339 scopus 로고    scopus 로고
    • Bacteriophage φ6 RNA-dependent RNA polymerase. Molecular details of initiating nucleic acid synthesis without primer
    • Laurila M.R.L., Makeyev E.V., Bamford D.H. Bacteriophage φ6 RNA-dependent RNA polymerase. Molecular details of initiating nucleic acid synthesis without primer. J. Biol. Chem. 277:2002;17117-17124.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17117-17124
    • Laurila, M.R.L.1    Makeyev, E.V.2    Bamford, D.H.3
  • 54
    • 0033579380 scopus 로고    scopus 로고
    • Structure of a transcribing T7 RNA polymerase initiation complex
    • Cheetham G.M., Steitz T.A. Structure of a transcribing T7 RNA polymerase initiation complex. Science. 286:1999;2305-2309.
    • (1999) Science , vol.286 , pp. 2305-2309
    • Cheetham, G.M.1    Steitz, T.A.2
  • 55
    • 0037112082 scopus 로고    scopus 로고
    • Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase
    • ••].
    • ••].
    • (2002) Science , vol.298 , pp. 1387-1395
    • Yin, Y.W.1    Steitz, T.A.2
  • 56
    • 0037038361 scopus 로고    scopus 로고
    • Structure of a T7 RNA polymerase elongation complex at 2.9 Å resolution
    • The X-ray structures of elongation complex of T7 RNAP. Delineates massive conformational changes between the initiation and elongation forms of the enzyme.
    • Tahirov T.H., Temiakov D., Anikin M., Patlan V., MacAllister W.T., Vassylyev D.G., Yokoyama S. Structure of a T7 RNA polymerase elongation complex at 2.9 Å resolution. Nature. 420:2002;43-50 The X-ray structures of elongation complex of T7 RNAP. Delineates massive conformational changes between the initiation and elongation forms of the enzyme.
    • (2002) Nature , vol.420 , pp. 43-50
    • Tahirov, T.H.1    Temiakov, D.2    Anikin, M.3    Patlan, V.4    MacAllister, W.T.5    Vassylyev, D.G.6    Yokoyama, S.7
  • 57
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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