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Volumn 40, Issue 6, 2006, Pages 875-884

Low-molecular-weight inhibitors of bacterial DNA-dependent RNA polymerase

Author keywords

CBR703; CBR9379; CBR9393; Daunomycin; Inhibitors of bacterial RNA polymerase; Lipiarmycin; Marcellomycin; Microcin J25; Rifabutin; Rifampicin; Rifamycins; Rifapentin; Sorangicin; Streptolydigin; Tagetitoxin

Indexed keywords

BACTERIA (MICROORGANISMS);

EID: 33845660314     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S0026893306060057     Document Type: Review
Times cited : (5)

References (52)
  • 1
    • 0014787953 scopus 로고
    • Escherichia coli RNA polymerase: Purification, subunit structure, and factor requirements
    • Burgess R.R., Travers A.A. 1970. Escherichia coli RNA polymerase: Purification, subunit structure, and factor requirements. Fed. Proc. 29, 1164-1169.
    • (1970) Fed. Proc. , vol.29 , pp. 1164-1169
    • Burgess, R.R.1    Travers, A.A.2
  • 2
    • 0021891874 scopus 로고
    • Mechanism and control of transcription initiation in prokaryotes
    • McClure W.R. 1985. Mechanism and control of transcription initiation in prokaryotes. Annu. Rev. Biochem. 54, 171-204.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 171-204
    • McClure, W.R.1
  • 3
    • 0037543997 scopus 로고    scopus 로고
    • Unified two-metal mechanism of RNA synthesis and degradation by RNA polymerase
    • Sosunov V., Sosunova E., Mustaev A., Bass I., Nikiforov V., Goldfarb A. 2003. Unified two-metal mechanism of RNA synthesis and degradation by RNA polymerase. EMBO J. 22, 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
  • 4
    • 0029157035 scopus 로고
    • A universally conserved region of the largest subunit participates in the active site of RNA polymerase III
    • Dieci G., Hermann-Le Denmat S., Lukhtanov E., Thuriaux P., Werner M., Sentenac A. 1995. A universally conserved region of the largest subunit participates in the active site of RNA polymerase III. EMBO J. 14, 3766-3776.
    • (1995) EMBO J. , vol.14 , pp. 3766-3776
    • Dieci, G.1    Hermann-Le Denmat, S.2    Lukhtanov, E.3    Thuriaux, P.4    Werner, M.5    Sentenac, A.6
  • 5
    • 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. 2001. Structural basis of transcription: RNA polymerase II at 2.8 Å resolution. Science. 292, 1863-1876.
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 7
    • 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. 1999. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution. Cell. 98, 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
  • 10
    • 0037073048 scopus 로고    scopus 로고
    • Promoting elongation with transcript cleavage stimulatory factors
    • Fish R.N., Kane C.M. 2002. Promoting elongation with transcript cleavage stimulatory factors. Biochim. Biophys. Acta. 1577, 287-307.
    • (2002) Biochim. Biophys. Acta. , vol.1577 , pp. 287-307
    • Fish, R.N.1    Kane, C.M.2
  • 13
    • 0014757028 scopus 로고
    • Transcription of the tryptophan operon in Escherichia coli: Rifampicin as an inhibitor of initiation
    • Mosteller R.D., Yanofsky C. 1970. Transcription of the tryptophan operon in Escherichia coli: Rifampicin as an inhibitor of initiation. J. Mol. Biol. 48, 525-531.
    • (1970) J. Mol. Biol. , vol.48 , pp. 525-531
    • Mosteller, R.D.1    Yanofsky, C.2
  • 14
    • 0015527442 scopus 로고
    • Studies of the binding of Escherichia coli RNA polymerase to DNA: 4. The effect of rifampicin on binding and on RNA chain initiation
    • Hinkle D.C., Mangel W.F., Chamberlin M.J. 1972. Studies of the binding of Escherichia coli RNA polymerase to DNA: 4. The effect of rifampicin on binding and on RNA chain initiation. J. Mol. Biol. 70, 209-220.
    • (1972) J. Mol. Biol. , vol.70 , pp. 209-220
    • Hinkle, D.C.1    Mangel, W.F.2    Chamberlin, M.J.3
  • 15
    • 0018239472 scopus 로고
    • On the mechanism of rifampicin inhibition of RNA synthesis
    • McClure W.R., Cech C.L. 1978. On the mechanism of rifampicin inhibition of RNA synthesis. J. Biol. Chem. 253, 8949-8956.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8949-8956
    • McClure, W.R.1    Cech, C.L.2
  • 16
    • 0023749808 scopus 로고
    • Mapping and sequencing of mutations in the Escherichia coli rpoB gene that lead to rifampicin resistance
    • Jin D.J., Gross C.A. 1988. Mapping and sequencing of mutations in the Escherichia coli rpoB gene that lead to rifampicin resistance. J. Mol. Biol. 202, 45-58.
    • (1988) J. Mol. Biol. , vol.202 , pp. 45-58
    • Jin, D.J.1    Gross, C.A.2
  • 17
    • 0027320544 scopus 로고
    • Rifampicin region revisited. New rifampicinresistant and streptolydigin-resistant mutants in the β subunit of Escherichia coli RNA polymerase
    • Severinov K., Soushko M., Goldfarb A., Nikiforov V. 1993. Rifampicin region revisited. New rifampicinresistant and streptolydigin-resistant mutants in the β subunit of Escherichia coli RNA polymerase. J. Biol. Chem. 268, 14,820-14,825.
    • (1993) J. Biol. Chem. , vol.268
    • Severinov, K.1    Soushko, M.2    Goldfarb, A.3    Nikiforov, V.4
  • 18
    • 0021149573 scopus 로고
    • Mutation to rifampicin resistance at the beginning of the RNA polymerase beta subunit gene in Escherichia coli
    • Lisitsyn N.A., Sverdlov E.D., Moiseyeva E.P., Danilevskaya O.N., Nikiforov V.G. 1984. Mutation to rifampicin resistance at the beginning of the RNA polymerase beta subunit gene in Escherichia coli. Mol. Gen. Genet. 196, 173-174.
    • (1984) Mol. Gen. Genet. , vol.196 , pp. 173-174
    • Lisitsyn, N.A.1    Sverdlov, E.D.2    Moiseyeva, E.P.3    Danilevskaya, O.N.4    Nikiforov, V.G.5
  • 19
    • 0028168928 scopus 로고
    • R ifR mutations in the beginning of the Escherichia coli rpoB gene
    • Severinov K., Soushko M., Goldfarb A., Nikiforov V. 1994 R ifR mutations in the beginning of the Escherichia coli rpoB gene. Mol. Gen. Genet. 244, 120-126.
    • (1994) Mol. Gen. Genet. , vol.244 , pp. 120-126
    • Severinov, K.1    Soushko, M.2    Goldfarb, A.3    Nikiforov, V.4
  • 20
    • 0035918272 scopus 로고    scopus 로고
    • The β′ subunit of Escherichia coli RNA polymerase is not required for interaction with initiating nucleotide but is necessary for interaction with rifampicin
    • Naryshkina T., Mustaev A., Darst S.A., Severinov K. 2001. The β′ subunit of Escherichia coli RNA polymerase is not required for interaction with initiating nucleotide but is necessary for interaction with rifampicin. J. Biol. Chem. 276, 13,308-13,368.
    • (2001) J. Biol. Chem. , vol.276
    • Naryshkina, T.1    Mustaev, A.2    Darst, S.A.3    Severinov, K.4
  • 21
    • 0035137371 scopus 로고    scopus 로고
    • Differential effect of rpoB mutations on antibacterial activities of rifampicin and KRM-1648 against Staphylococcus aureus
    • Wichelhaus T., Schafer V., Brade V., Boddinghaus B. 2001. Differential effect of rpoB mutations on antibacterial activities of rifampicin and KRM-1648 against Staphylococcus aureus. J. Antimicrob. Chemother. 47, 153-156.
    • (2001) J. Antimicrob. Chemother. , vol.47 , pp. 153-156
    • Wichelhaus, T.1    Schafer, V.2    Brade, V.3    Boddinghaus, B.4
  • 24
    • 0023104658 scopus 로고
    • The sorangicins, novel and powerful inhibitors of eubacterial RNA polymerase isolated from myxobacteria
    • Irschik H., Jansen R., Gerth K., Hofle G., Reichenbach H. 1985. The sorangicins, novel and powerful inhibitors of eubacterial RNA polymerase isolated from myxobacteria. J. Antibiotics. 40, 7-13.
    • (1985) J. Antibiotics , vol.40 , pp. 7-13
    • Irschik, H.1    Jansen, R.2    Gerth, K.3    Hofle, G.4    Reichenbach, H.5
  • 25
    • 0025134232 scopus 로고
    • Resistance of Escherichia coli to rifampicin and sorangicin A: A comparision
    • Rommele G., Wirz G., Solf R., Vosbeck K., Gruner J., Wehrli W. 1990. Resistance of Escherichia coli to rifampicin and sorangicin A: A comparision. J. Antibiot. 43, 88-91.
    • (1990) J. Antibiot. , vol.43 , pp. 88-91
    • Rommele, G.1    Wirz, G.2    Solf, R.3    Vosbeck, K.4    Gruner, J.5    Wehrli, W.6
  • 27
    • 0025096666 scopus 로고
    • Tagetitoxin inhibits RNA synthesis directed by RNA polymerases from chloroplasts and Escherichia coli
    • Mathews D.E., Durbin R.D. 1990. Tagetitoxin inhibits RNA synthesis directed by RNA polymerases from chloroplasts and Escherichia coli. J. Biol. Chem. 265, 493-498.
    • (1990) J. Biol. Chem. , vol.265 , pp. 493-498
    • Mathews, D.E.1    Durbin, R.D.2
  • 28
    • 0028037016 scopus 로고
    • Mechanistic aspects of tagetitoxin inhibition of RNA polymerase from Escherichia coli
    • Mathews D.E., Durbin R.D. 1994. Mechanistic aspects of tagetitoxin inhibition of RNA polymerase from Escherichia coli. Biochemistry. 33, 11,987-11,992.
    • (1994) Biochemistry , vol.33
    • Mathews, D.E.1    Durbin, R.D.2
  • 32
    • 0014665964 scopus 로고
    • Isolation and characterization of streptolydigin resistant RNA polymerase
    • Schleif R. 1969. Isolation and characterization of streptolydigin resistant RNA polymerase. Nature. 223, 1068-1069.
    • (1969) Nature , vol.223 , pp. 1068-1069
    • Schleif, R.1
  • 33
    • 0033750982 scopus 로고    scopus 로고
    • RNA polymerase inhibitors with activity against rifampin-resistant mutants of Staphylococcus aureus
    • O'Niell A., Oliva B., Storey C., Hoyle A., Fishwick C., Chopra I. 2000. RNA polymerase inhibitors with activity against rifampin-resistant mutants of Staphylococcus aureus. Antimicrob. Agents Chemotherapy. 44, 3163-3166.
    • (2000) Antimicrob. Agents Chemotherapy , vol.44 , pp. 3163-3166
    • O'Niell, A.1    Oliva, B.2    Storey, C.3    Hoyle, A.4    Fishwick, C.5    Chopra, I.6
  • 34
    • 0027486228 scopus 로고
    • Four contiguous aminoacids define the target for streptolydigin resistance in the beta subunit of Escherichia coli RNA polymerase
    • Heisler L.M., Suzuki H., Landick R., Gross C.A. 1993. Four contiguous aminoacids define the target for streptolydigin resistance in the beta subunit of Escherichia coli RNA polymerase. J. Biol. Chem. 268, 25,369-25,375.
    • (1993) J. Biol. Chem. , vol.268
    • Heisler, L.M.1    Suzuki, H.2    Landick, R.3    Gross, C.A.4
  • 35
    • 0022555872 scopus 로고
    • Transcription of cloned eukaryotic ribosomal RNA genes
    • Sollner-Webb B., Tower J. 1986. Transcription of cloned eukaryotic ribosomal RNA genes. Annu. Rev. Biochem. 55, 801-830.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 801-830
    • Sollner-Webb, B.1    Tower, J.2
  • 36
    • 0014959969 scopus 로고
    • Specific inhibition of nuclear RNA polymerase II by alpha-amanitin
    • Lindell T.J., Weinberg F., Morris P.W., Roeder R.G., Rutter W.J. 1970. Specific inhibition of nuclear RNA polymerase II by alpha-amanitin. Science. 170, 447-449.
    • (1970) Science , vol.170 , pp. 447-449
    • Lindell, T.J.1    Weinberg, F.2    Morris, P.W.3    Roeder, R.G.4    Rutter, W.J.5
  • 38
    • 0029786278 scopus 로고    scopus 로고
    • Biochemical analysis of catalytically crucial aspartate mutants of human immunodeficiency virus type 1 reverse transcriptase
    • Kaushik N., Rege N., Yadav P.N., Sarafianos S.G., Modak M.J., Pandey V.N. 1996. Biochemical analysis of catalytically crucial aspartate mutants of human immunodeficiency virus type 1 reverse transcriptase. Biochemistry. 35, 11,536-11,546.
    • (1996) Biochemistry , vol.35
    • Kaushik, N.1    Rege, N.2    Yadav, P.N.3    Sarafianos, S.G.4    Modak, M.J.5    Pandey, V.N.6
  • 39
    • 0026713678 scopus 로고
    • Side chains involved in catalysis of the polymerase reaction of DNA polymerase I from Escherichia coli
    • Polesky A.H., Dahlberg M.E., Benkovic S.J., Grindley N.D., Joyce C.M. 1992. Side chains involved in catalysis of the polymerase reaction of DNA polymerase I from Escherichia coli. J. Biol. Chem. 267, 8417-8428.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8417-8428
    • Polesky, A.H.1    Dahlberg, M.E.2    Benkovic, S.J.3    Grindley, N.D.4    Joyce, C.M.5
  • 40
    • 0017651941 scopus 로고
    • Lipiarmycin-resistant ribonucleic acid polymerase mutants of Bacillus subtilis
    • Sonenshein A., Alexander H., Rothstein D., Fisher S. 1977. Lipiarmycin-resistant ribonucleic acid polymerase mutants of Bacillus subtilis. J. Bacteriol. 132, 73-79.
    • (1977) J. Bacteriol. , vol.132 , pp. 73-79
    • Sonenshein, A.1    Alexander, H.2    Rothstein, D.3    Fisher, S.4
  • 41
    • 0018346209 scopus 로고
    • Initiation of transcription in vitro is inhibited by lipiarmycin
    • Sonenshein A.L., Alexander H.B. 1979. Initiation of transcription in vitro is inhibited by lipiarmycin. J. Mol. Biol. 127, 55-72.
    • (1979) J. Mol. Biol. , vol.127 , pp. 55-72
    • Sonenshein, A.L.1    Alexander, H.B.2
  • 42
    • 29944444405 scopus 로고    scopus 로고
    • Mutation in the Bacillus subtilis RNA polymerase β′ subunit confers resistance to lipiarmycin
    • Gualtieri M., Guillot P.V., Latouche J., Leonetti J.P. 2006. Mutation in the Bacillus subtilis RNA polymerase β′ subunit confers resistance to lipiarmycin. Antimicrob. Agents Chemotheapy. 50, 401-402.
    • (2006) Antimicrob. Agents Chemotheapy , vol.50 , pp. 401-402
    • Gualtieri, M.1    Guillot, P.V.2    Latouche, J.3    Leonetti, J.P.4
  • 43
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • Murakami K., Masuda S., Campbell E., Muzzin O., Darst S. 2002. Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex. Science. 296, 1285-1290.
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.1    Masuda, S.2    Campbell, E.3    Muzzin, O.4    Darst, S.5
  • 44
    • 0142147268 scopus 로고    scopus 로고
    • A new class of bacterial RNA polymerase inhibitor affects nucleotide addition
    • Artsimovitch I., Chu C., Lynch A.S., Landick R. 2003. A new class of bacterial RNA polymerase inhibitor affects nucleotide addition. Science. 302, 650-654.
    • (2003) Science , vol.302 , pp. 650-654
    • Artsimovitch, I.1    Chu, C.2    Lynch, A.S.3    Landick, R.4
  • 45
    • 0014021976 scopus 로고
    • Action of daunomycin on nucleic acid metabolism in HeLa cells
    • Rusconi A., Calendi E. 1966. Action of daunomycin on nucleic acid metabolism in HeLa cells. Biochim. Biophys. Acta. 119, 413-585.
    • (1966) Biochim. Biophys. Acta , vol.119 , pp. 413-585
    • Rusconi, A.1    Calendi, E.2
  • 46
    • 0023656179 scopus 로고
    • Inhibition of the RNA polymerase-catalyzed synthesis of RNA by daunomycin. Effect of the inhibitor on the late steps of RNA chain initiation
    • Kriebardis T., Meng D., Aktipis S. 1987. Inhibition of the RNA polymerase-catalyzed synthesis of RNA by daunomycin. Effect of the inhibitor on the late steps of RNA chain initiation. J. Biol. Chem. 262, 12,632-12,640.
    • (1987) J. Biol. Chem. , vol.262
    • Kriebardis, T.1    Meng, D.2    Aktipis, S.3
  • 47
    • 0023907960 scopus 로고
    • Inhibition of the RNA polymerase-catalyzed synthesis of RNA by marcellomycin. Preferential interference of the inhibitor with the stabilization of the ternary promoter-RNA polymerase-nascent RNA complex
    • Kriebardis T., Aktipis S. 1988. Inhibition of the RNA polymerase-catalyzed synthesis of RNA by marcellomycin. Preferential interference of the inhibitor with the stabilization of the ternary promoter-RNA polymerase-nascent RNA complex. J. Biol. Chem. 263, 6960-6963.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6960-6963
    • Kriebardis, T.1    Aktipis, S.2
  • 48
    • 0034932730 scopus 로고    scopus 로고
    • Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25
    • Delgado M.A., Rintoul M.R., Farias R.N., Salomon R.A. 2001. Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25. J. Bacteriol. 183, 4543-4550.
    • (2001) J. Bacteriol. , vol.183 , pp. 4543-4550
    • Delgado, M.A.1    Rintoul, M.R.2    Farias, R.N.3    Salomon, R.A.4


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