메뉴 건너뛰기




Volumn 122, Issue 4, 2005, Pages 541-552

Inhibition of bacterial RNA polymerase by streptolydigin: Stabilization of a straight-bridge-helix active-center conformation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; RNA POLYMERASE; STREPTOLYDIGIN;

EID: 23944521364     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2005.07.017     Document Type: Article
Times cited : (174)

References (61)
  • 2
    • 0037495037 scopus 로고    scopus 로고
    • Architecture of initiation-competent 12-subunit RNA polymerase II
    • K. Armache, H. Kettenberger, and P. Cramer Architecture of initiation-competent 12-subunit RNA polymerase II Proc. Natl. Acad. Sci. USA 100 2003 6964 6968
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6964-6968
    • Armache, K.1    Kettenberger, H.2    Cramer, P.3
  • 3
    • 0142147268 scopus 로고    scopus 로고
    • A new class of bacterial RNA polymerase inhibitor affects nucleotide addition
    • I. Artsimovitch, C. Chu, A. Lynch, and R. Landick A new class of bacterial RNA polymerase inhibitor affects nucleotide addition Science 302 2003 650 654
    • (2003) Science , vol.302 , pp. 650-654
    • Artsimovitch, I.1    Chu, C.2    Lynch, A.3    Landick, R.4
  • 7
    • 0037022279 scopus 로고    scopus 로고
    • Structural basis of transcription: Alpha-amanitin-RNA polymerase II cocrystal at 2.8 Å resolution
    • D. Bushnell, P. Cramer, and R. Kornberg Structural basis of transcription: alpha-amanitin-RNA polymerase II cocrystal at 2.8 Å resolution Proc. Natl. Acad. Sci. USA 99 2002 1218 1222
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1218-1222
    • Bushnell, D.1    Cramer, P.2    Kornberg, R.3
  • 8
    • 0037832543 scopus 로고    scopus 로고
    • Complete, 12-subunit RNA polymerase II at 4.1-Å resolution: Implications for the initiation of transcription
    • D. Bushnell, and R. Kornberg Complete, 12-subunit RNA polymerase II at 4.1-Å resolution: implications for the initiation of transcription Proc. Natl. Acad. Sci. USA 100 2003 6969 6973
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6969-6973
    • Bushnell, D.1    Kornberg, R.2
  • 9
    • 1142274214 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II-TFIIB cocrystal at 4.5 angstroms
    • D. Bushnell, K. Westover, R. Davis, and R. Kornberg Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 angstroms Science 303 2004 983 988
    • (2004) Science , vol.303 , pp. 983-988
    • Bushnell, D.1    Westover, K.2    Davis, R.3    Kornberg, R.4
  • 11
    • 15444374664 scopus 로고    scopus 로고
    • Structural, functional, and genetic analysis of sorangicin inhibition of bacterial RNA polymerase
    • E. Campbell, O. Pavlova, N. Zenkin, F. Leon, H. Irschik, R. Jansen, K. Severinov, and S. Darst Structural, functional, and genetic analysis of sorangicin inhibition of bacterial RNA polymerase EMBO J. 24 2005 674 682
    • (2005) EMBO J. , vol.24 , pp. 674-682
    • Campbell, E.1    Pavlova, O.2    Zenkin, N.3    Leon, F.4    Irschik, H.5    Jansen, R.6    Severinov, K.7    Darst, S.8
  • 13
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • P. Chou, and G. Fasman Prediction of protein conformation Biochemistry 13 1974 222 245
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.1    Fasman, G.2
  • 14
    • 0029830434 scopus 로고    scopus 로고
    • Escherichia coli rpoC397 encodes a temperature-sensitive C-terminal frameshift in the β′ subunit of RNA polymerase that blocks growth of bacteriophage P2
    • G. Christie, S. Cale, L. Iraksson, D. Jin, M. Xu, B. Sauer, and R. Calendar Escherichia coli rpoC397 encodes a temperature-sensitive C-terminal frameshift in the β′ subunit of RNA polymerase that blocks growth of bacteriophage P2 J. Bacteriol. 178 1996 6991 6993
    • (1996) J. Bacteriol. , vol.178 , pp. 6991-6993
    • Christie, G.1    Cale, S.2    Iraksson, L.3    Jin, D.4    Xu, M.5    Sauer, B.6    Calendar, R.7
  • 15
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D. Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D. Biol. Crystallogr. , vol.50 , pp. 760-763
  • 16
    • 0036468364 scopus 로고    scopus 로고
    • Multisubunit RNA polymerases
    • P. Cramer Multisubunit RNA polymerases Curr. Opin. Struct. Biol. 12 2002 89 97
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 89-97
    • Cramer, P.1
  • 17
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • P. Cramer, D. Bushnell, and R. Kornberg Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution Science 292 2001 1863 1876
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.2    Kornberg, R.3
  • 18
    • 0035312415 scopus 로고    scopus 로고
    • Bacterial RNA polymerase
    • S. Darst Bacterial RNA polymerase Curr. Opin. Struct. Biol. 11 2001 155 162
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 155-162
    • Darst, S.1
  • 19
    • 0034671288 scopus 로고    scopus 로고
    • RNA polymerase: Structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II
    • R. Ebright RNA polymerase: structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II J. Mol. Biol. 304 2000 687 698
    • (2000) J. Mol. Biol. , vol.304 , pp. 687-698
    • Ebright, R.1
  • 21
    • 0028051714 scopus 로고
    • Additive effect of tolC and rfa mutations on the hydrophobic barrier of the outer membrane of Escherichia coli K-12
    • J. Fralick, and L. Burns-Keliher Additive effect of tolC and rfa mutations on the hydrophobic barrier of the outer membrane of Escherichia coli K-12 J. Bacteriol. 176 1994 6404 6406
    • (1994) J. Bacteriol. , vol.176 , pp. 6404-6406
    • Fralick, J.1    Burns-Keliher, L.2
  • 22
    • 0029315603 scopus 로고
    • MAB, a generally applicable molecular force field for structure modelling in medicinal chemistry
    • P.R. Gerber, and K. Muller MAB, a generally applicable molecular force field for structure modelling in medicinal chemistry J. Comput. Aided Mol. Des. 9 1995 251 268
    • (1995) J. Comput. Aided Mol. Des. , vol.9 , pp. 251-268
    • Gerber, P.R.1    Muller, K.2
  • 23
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 Å resolution
    • A. Gnatt, P. Cramer, J. Fu, D. Bushnell, and R. Kornberg 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.1    Cramer, P.2    Fu, J.3    Bushnell, D.4    Kornberg, R.5
  • 24
    • 0032483305 scopus 로고    scopus 로고
    • NTP concentration effects on initial transcription by T7 RNAP indicate that translocation occurs through passive sliding and reveal that divergent promoters have distinct NTP concentration requirements for productive initiation
    • R. Guajardo, P. Lopez, M. Dreyfus, and R. Sousa NTP concentration effects on initial transcription by T7 RNAP indicate that translocation occurs through passive sliding and reveal that divergent promoters have distinct NTP concentration requirements for productive initiation J. Mol. Biol. 281 1998 777 792
    • (1998) J. Mol. Biol. , vol.281 , pp. 777-792
    • Guajardo, R.1    Lopez, P.2    Dreyfus, M.3    Sousa, R.4
  • 25
    • 0027486228 scopus 로고
    • Four contiguous amino acids define the target for streptolydigin resistance in the beta subunit of Escherichia coli RNA polymerase
    • L. Heisler, H. Suzuki, R. Landick, and C. Gross Four contiguous amino acids define the target for streptolydigin resistance in the beta subunit of Escherichia coli RNA polymerase J. Biol. Chem. 268 1993 25369 25375
    • (1993) J. Biol. Chem. , vol.268 , pp. 25369-25375
    • Heisler, L.1    Suzuki, H.2    Landick, R.3    Gross, C.4
  • 26
    • 0024834564 scopus 로고
    • A reliable method for random mutagenesis: The generation of mutant libraries using spiked oligodeoxyribonucleotide primers
    • J. Hermes, S. Parekh, S. Blacklow, H. Koster, and J. Knowles A reliable method for random mutagenesis: the generation of mutant libraries using spiked oligodeoxyribonucleotide primers Gene 84 1989 143 151
    • (1989) Gene , vol.84 , pp. 143-151
    • Hermes, J.1    Parekh, S.2    Blacklow, S.3    Koster, H.4    Knowles, J.5
  • 27
    • 0025186676 scopus 로고
    • Searching sequence space by definably random mutagenesis: Improving the catalytic potency of an enzyme
    • J. Hermes, S. Blacklow, and J. Knowles Searching sequence space by definably random mutagenesis: improving the catalytic potency of an enzyme Proc. Natl. Acad. Sci. USA 87 1990 696 700
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 696-700
    • Hermes, J.1    Blacklow, S.2    Knowles, J.3
  • 28
    • 0041315524 scopus 로고    scopus 로고
    • Downstream DNA sequence effects on transcription elongation: Allosteric binding of nucleoside triphosphates facilitates translocation via a ratchet motion
    • S. Holmes, and D. Erie Downstream DNA sequence effects on transcription elongation: allosteric binding of nucleoside triphosphates facilitates translocation via a ratchet motion J. Biol. Chem. 278 2003 35597 35608
    • (2003) J. Biol. Chem. , vol.278 , pp. 35597-35608
    • Holmes, S.1    Erie, D.2
  • 29
    • 16244401160 scopus 로고    scopus 로고
    • Tetramic acid antibiotics: Stereoselective synthesis of streptolic acid and tirandalydigin
    • Y. Iwata, N. Maekawara, K. Tanino, and M. Miyashita Tetramic acid antibiotics: stereoselective synthesis of streptolic acid and tirandalydigin Angew. Chem. Int. Ed. Engl. 44 2005 1532 1536
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 1532-1536
    • Iwata, Y.1    Maekawara, N.2    Tanino, K.3    Miyashita, M.4
  • 30
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T. Jones, J. Zou, and S. Cowan Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A A47 1991 110 119
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.1    Zou, J.2    Cowan, S.3
  • 31
    • 0043244876 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage
    • H. Kettenberger, K. Armache, and P. Cramer Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage Cell 114 2003 347 357
    • (2003) Cell , vol.114 , pp. 347-357
    • Kettenberger, H.1    Armache, K.2    Cramer, P.3
  • 32
    • 10944232674 scopus 로고    scopus 로고
    • Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
    • H. Kettenberger, K. Armache, and P. Cramer Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS Mol. Cell 16 2004 955 965
    • (2004) Mol. Cell , vol.16 , pp. 955-965
    • Kettenberger, H.1    Armache, K.2    Cramer, P.3
  • 34
    • 0025062984 scopus 로고
    • Amino acid changes in conserved regions of the beta-subunit of Escherichia coli RNA polymerase alter transcription pausing and termination
    • R. Landick, J. Stewart, and D.N. Lee Amino acid changes in conserved regions of the beta-subunit of Escherichia coli RNA polymerase alter transcription pausing and termination Genes Dev. 4 1990 1623 1636
    • (1990) Genes Dev. , vol.4 , pp. 1623-1636
    • Landick, R.1    Stewart, J.2    Lee, D.N.3
  • 35
    • 0348166026 scopus 로고    scopus 로고
    • Biochemical assays of Gre factors of Thermus thermophilus
    • O. Laptenko, and S. Borukhov Biochemical assays of Gre factors of Thermus thermophilus Methods Enzymol. 371 2003 219 232
    • (2003) Methods Enzymol. , vol.371 , pp. 219-232
    • Laptenko, O.1    Borukhov, S.2
  • 36
    • 0019121079 scopus 로고
    • 13C NMR spectra of streptolydigin, tirandmycin, and related degradation products
    • 13C NMR spectra of streptolydigin, tirandmycin, and related degradation products J. Antibiot. (Tokyo) 33 1980 408 415
    • (1980) J. Antibiot. (Tokyo) , vol.33 , pp. 408-415
    • Lee, V.1    Rinehart, K.2
  • 37
    • 0018846636 scopus 로고
    • Sequencing end-labeled DNA with base-specific chemical cleavages
    • A. Maxam, and W. Gilbert Sequencing end-labeled DNA with base-specific chemical cleavages Methods Enzymol. 65 1980 499 560
    • (1980) Methods Enzymol. , vol.65 , pp. 499-560
    • Maxam, A.1    Gilbert, W.2
  • 38
    • 0018861875 scopus 로고
    • On the mechanism of streptolydigin inhibition of Escherichia coli RNA polymerase
    • W. McClure On the mechanism of streptolydigin inhibition of Escherichia coli RNA polymerase J. Biol. Chem. 255 1980 1610 1616
    • (1980) J. Biol. Chem. , vol.255 , pp. 1610-1616
    • McClure, W.1
  • 39
    • 0024463634 scopus 로고
    • A cinematographic view of Escherichia coli RNA polymerase translocation
    • W. Metzger, P. Schickor, and H. Heumann 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
  • 40
    • 2942696237 scopus 로고    scopus 로고
    • Antibacterial peptide microcin J25 inhibits transcription by binding within, and obstructing, the RNA polymerase secondary channel
    • J. Mukhopadhyay, E. Sineva, J. Knight, R. Levy, and R. Ebright Antibacterial peptide microcin J25 inhibits transcription by binding within, and obstructing, the RNA polymerase secondary channel Mol. Cell 14 2004 739 751
    • (2004) Mol. Cell , vol.14 , pp. 739-751
    • Mukhopadhyay, J.1    Sineva, E.2    Knight, J.3    Levy, R.4    Ebright, R.5
  • 41
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution
    • K. Murakami, S. Masuda, and S. Darst Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution Science 296 2002 1280 1284
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.1    Masuda, S.2    Darst, S.3
  • 42
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • K. Murakami, S. Masuda, E. Campbell, O. Muzzin, and S. Darst 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.3    Muzzin, O.4    Darst, S.5
  • 43
    • 0034625251 scopus 로고    scopus 로고
    • Structural organization of the RNA polymerase-promoter open complex
    • N. Naryshkin, A. Revyakin, Y. Kim, V. Mekler, and R. Ebright 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.5
  • 44
    • 0030582675 scopus 로고    scopus 로고
    • Transcription activation at Class II CAP-dependent promoters: Two interactions between CAP and RNA polymerase
    • W. Niu, Y. Kim, G. Tau, T. Heyduk, and R. Ebright Transcription activation at Class II CAP-dependent promoters: two interactions between CAP and RNA polymerase Cell 87 1996 1123 1134
    • (1996) Cell , vol.87 , pp. 1123-1134
    • Niu, W.1    Kim, Y.2    Tau, G.3    Heyduk, T.4    Ebright, R.5
  • 45
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor 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
  • 48
    • 0028841199 scopus 로고
    • Streptolydigin-resistant mutants in an evolutionarily conserved region of the beta′ subunit of Escherichia coli RNA polymerase
    • K. Severinov, D. Markov, E. Severinova, V. Nikiforov, R. Landick, S. Darst, and A. Goldfarb Streptolydigin-resistant mutants in an evolutionarily conserved region of the beta′ subunit of Escherichia coli RNA polymerase J. Biol. Chem. 270 1995 23926 23929
    • (1995) J. Biol. Chem. , vol.270 , pp. 23926-23929
    • Severinov, K.1    Markov, D.2    Severinova, E.3    Nikiforov, V.4    Landick, R.5    Darst, S.6    Goldfarb, A.7
  • 49
    • 0030808646 scopus 로고    scopus 로고
    • Tethering of the large subunits of Escherichia coli RNA polymerase
    • K. Severinov, R. Mooney, S.A. Darst, and R. Landick Tethering of the large subunits of Escherichia coli RNA polymerase J. Biol. Chem. 272 1997 24137 24140
    • (1997) J. Biol. Chem. , vol.272 , pp. 24137-24140
    • Severinov, K.1    Mooney, R.2    Darst, S.A.3    Landick, R.4
  • 51
    • 0037543997 scopus 로고    scopus 로고
    • Unified two-metal mechanism of RNA synthesis and degradation by RNA polymerase
    • V. Sosunov, E. Sosunova, A. Mustaev, I. Bass, V. Nikiforov, and A. Goldfarb Unified two-metal mechanism of RNA synthesis and degradation by RNA polymerase EMBO J. 22 2003 2234 2244
    • (2003) EMBO J. , vol.22 , pp. 2234-2244
    • Sosunov, V.1    Sosunova, E.2    Mustaev, A.3    Bass, I.4    Nikiforov, V.5    Goldfarb, A.6
  • 52
    • 0028598437 scopus 로고
    • Location, structure, and function of the target of a transcription activator protein
    • H. Tang, K. Severinov, A. Goldfarb, D. Fenyo, B. Chait, and R. Ebright Location, structure, and function of the target of a transcription activator protein Genes Dev. 8 1994 3058 3067
    • (1994) Genes Dev. , vol.8 , pp. 3058-3067
    • Tang, H.1    Severinov, K.2    Goldfarb, A.3    Fenyo, D.4    Chait, B.5    Ebright, R.6
  • 55
    • 0029029468 scopus 로고
    • Discontinuous movements of DNA and RNA in RNA polymerase accompany formation of a paused transcription complex
    • D. Wang, T. Meier, C. Chan, G. Feng, D. Lee, and R. Landick Discontinuous movements of DNA and RNA in RNA polymerase accompany formation of a paused transcription complex Cell 81 1995 341 350
    • (1995) Cell , vol.81 , pp. 341-350
    • Wang, D.1    Meier, T.2    Chan, C.3    Feng, G.4    Lee, D.5    Landick, R.6
  • 56
    • 8344234112 scopus 로고    scopus 로고
    • Structural basis of transcription: Nucleotide selection by rotation in the RNA polymerase II active center
    • K. Westover, D. Bushnell, and R. Kornberg Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center Cell 119 2004 481 489
    • (2004) Cell , vol.119 , pp. 481-489
    • Westover, K.1    Bushnell, D.2    Kornberg, R.3
  • 57
    • 1142310578 scopus 로고    scopus 로고
    • Structural basis of transcription: Separation of RNA from DNA by RNA polymerase II
    • K. Westover, D. Bushnell, and R. Kornberg Structural basis of transcription: separation of RNA from DNA by RNA polymerase II Science 303 2004 1014 1016
    • (2004) Science , vol.303 , pp. 1014-1016
    • Westover, K.1    Bushnell, D.2    Kornberg, R.3
  • 58
    • 0028884222 scopus 로고
    • Streptolydigin resistance can be conferred by alterations to either the beta or beta′ subunits of Bacillus subtilis RNA polymerase
    • X. Yang, and C. Price Streptolydigin resistance can be conferred by alterations to either the beta or beta′ subunits of Bacillus subtilis RNA polymerase J. Biol. Chem. 270 1995 23930 23933
    • (1995) J. Biol. Chem. , vol.270 , pp. 23930-23933
    • Yang, X.1    Price, C.2
  • 59
    • 0031059039 scopus 로고    scopus 로고
    • Detecting and overcoming crystal twinning
    • T. Yeates Detecting and overcoming crystal twinning Methods Enzymol. 276 1997 344 358
    • (1997) Methods Enzymol. , vol.276 , pp. 344-358
    • Yeates, T.1
  • 61
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
    • G. Zhang, E. Campbell, L. Minakhin, C. Richter, K. Severinov, and S. Darst 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.2    Minakhin, L.3    Richter, C.4    Severinov, K.5    Darst, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.