메뉴 건너뛰기




Volumn 371, Issue 4, 2007, Pages 855-872

Transcription Termination Defective Mutants of Rho: Role of Different Functions of Rho in Releasing RNA from the Elongation Complex

Author keywords

mutagenesis; NusG; Rho; RNA polymerase; transcription termination

Indexed keywords

ADENOSINE TRIPHOSPHATE; BETA GALACTOSIDASE; ELONGATION FACTOR; MUTANT PROTEIN; RHO FACTOR; RNA BINDING PROTEIN; RNA POLYMERASE; TRANSCRIPTION TERMINATION FACTOR RHO;

EID: 34548667500     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.06.013     Document Type: Article
Times cited : (55)

References (56)
  • 1
    • 0028091898 scopus 로고
    • Stability of Escherichia coli transcription complexes near an intrinsic terminator
    • Wilson K.S., and von Hippel P.H. Stability of Escherichia coli transcription complexes near an intrinsic terminator. J. Mol. Biol. 244 (1994) 36-51
    • (1994) J. Mol. Biol. , vol.244 , pp. 36-51
    • Wilson, K.S.1    von Hippel, P.H.2
  • 2
    • 0031801743 scopus 로고    scopus 로고
    • Information processing by RNA polymerase: recognition of regulatory signals during RNA chain elongation
    • Mooney R.A., Artsimovitch I., and Landick R. Information processing by RNA polymerase: recognition of regulatory signals during RNA chain elongation. J. Bacteriol. 180 (1998) 3265-3275
    • (1998) J. Bacteriol. , vol.180 , pp. 3265-3275
    • Mooney, R.A.1    Artsimovitch, I.2    Landick, R.3
  • 3
    • 0033597435 scopus 로고    scopus 로고
    • Mechanism of intrinsic transcription termination and antitermination
    • Yarnell W.S., and Roberts J.W. Mechanism of intrinsic transcription termination and antitermination. Science 284 (1999) 611-615
    • (1999) Science , vol.284 , pp. 611-615
    • Yarnell, W.S.1    Roberts, J.W.2
  • 5
    • 0031008221 scopus 로고    scopus 로고
    • Basic mechanisms of transcript elongation and its regulation
    • Uptain S.M., Kane C.M., and Chamberlin M.J. Basic mechanisms of transcript elongation and its regulation. Annu. Rev. Biochem. 66 (1997) 117-172
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 117-172
    • Uptain, S.M.1    Kane, C.M.2    Chamberlin, M.J.3
  • 6
    • 0041696782 scopus 로고    scopus 로고
    • Loading Rho to terminate transcription
    • Richardson J.P. Loading Rho to terminate transcription. Cell 114 (2003) 157-159
    • (2003) Cell , vol.114 , pp. 157-159
    • Richardson, J.P.1
  • 7
    • 0037073063 scopus 로고    scopus 로고
    • Rho-dependent termination and ATPases in transcript termination
    • Richardson J.P. Rho-dependent termination and ATPases in transcript termination. Biochim. Biophys. Acta 1577 (2002) 251-260
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 251-260
    • Richardson, J.P.1
  • 8
    • 33646849728 scopus 로고    scopus 로고
    • Rho-dependent transcription termination: more questions than answers
    • Banerjee S., Chalissery J., Bandey I., and Sen R. Rho-dependent transcription termination: more questions than answers. J. Microbiol. 44 (2006) 11-22
    • (2006) J. Microbiol. , vol.44 , pp. 11-22
    • Banerjee, S.1    Chalissery, J.2    Bandey, I.3    Sen, R.4
  • 9
    • 0028068117 scopus 로고
    • The RNA-binding domain of transcription termination factor rho: isolation, characterization, and determination of sequence limits
    • Modrak D., and Richardson J.P. The RNA-binding domain of transcription termination factor rho: isolation, characterization, and determination of sequence limits. Biochemistry 33 (1994) 8292-8299
    • (1994) Biochemistry , vol.33 , pp. 8292-8299
    • Modrak, D.1    Richardson, J.P.2
  • 10
    • 0035958964 scopus 로고    scopus 로고
    • Identification of an RNA-binding Site in the ATP binding domain of Escherichia coli Rho by H2O2/Fe-EDTA cleavage protection studies
    • Wei R.R., and Richardson J.P. Identification of an RNA-binding Site in the ATP binding domain of Escherichia coli Rho by H2O2/Fe-EDTA cleavage protection studies. J. Biol. Chem. 276 (2001) 28380-28387
    • (2001) J. Biol. Chem. , vol.276 , pp. 28380-28387
    • Wei, R.R.1    Richardson, J.P.2
  • 11
    • 0035830896 scopus 로고    scopus 로고
    • RNA passes through the hole of the protein hexamer in the complex with the Escherichia coli Rho factor
    • Burgess B.R., and Richardson J.P. RNA passes through the hole of the protein hexamer in the complex with the Escherichia coli Rho factor. J. Biol. Chem. 276 (2001) 4182-4189
    • (2001) J. Biol. Chem. , vol.276 , pp. 4182-4189
    • Burgess, B.R.1    Richardson, J.P.2
  • 12
    • 0035861978 scopus 로고    scopus 로고
    • Mutational changes of conserved residues in the Q-loop region of transcription factor Rho greatly reduce secondary site RNA-binding
    • Wei R.R., and Richardson J.P. Mutational changes of conserved residues in the Q-loop region of transcription factor Rho greatly reduce secondary site RNA-binding. J. Mol. Biol. 314 (2001) 1007-1015
    • (2001) J. Mol. Biol. , vol.314 , pp. 1007-1015
    • Wei, R.R.1    Richardson, J.P.2
  • 13
    • 0037119488 scopus 로고    scopus 로고
    • Mutations in the rho transcription termination factor that affect RNA tracking
    • Xu Y., Kohn H., and Widger W.R. Mutations in the rho transcription termination factor that affect RNA tracking. J. Biol. Chem. 277 (2002) 30023-30030
    • (2002) J. Biol. Chem. , vol.277 , pp. 30023-30030
    • Xu, Y.1    Kohn, H.2    Widger, W.R.3
  • 14
    • 0029565119 scopus 로고
    • Structural and functional dissections of transcription termination factor rho by random mutagenesis
    • Miwa Y., Horiguchi T., and Shigesada K. Structural and functional dissections of transcription termination factor rho by random mutagenesis. J. Mol. Biol. 254 (1995) 815-837
    • (1995) J. Mol. Biol. , vol.254 , pp. 815-837
    • Miwa, Y.1    Horiguchi, T.2    Shigesada, K.3
  • 15
    • 0037559627 scopus 로고    scopus 로고
    • Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading
    • Skordalakes E., and Berger J.M. Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading. Cell 114 (2003) 135-146
    • (2003) Cell , vol.114 , pp. 135-146
    • Skordalakes, E.1    Berger, J.M.2
  • 16
    • 0026027218 scopus 로고
    • A consensus motif common to all Rho-dependent prokaryotic transcription terminators
    • Alifano P., Rivellini F., Limauro D., Bruni C.B., and Carlomagno M.S. A consensus motif common to all Rho-dependent prokaryotic transcription terminators. Cell 64 (1991) 553-563
    • (1991) Cell , vol.64 , pp. 553-563
    • Alifano, P.1    Rivellini, F.2    Limauro, D.3    Bruni, C.B.4    Carlomagno, M.S.5
  • 17
    • 0022431528 scopus 로고
    • RNA sequence and secondary structure requirements for rho-dependent transcription termination
    • Morgan W.D., Bear D.G., Litchman B.L., and von Hippel P.H. RNA sequence and secondary structure requirements for rho-dependent transcription termination. Nucl. Acids Res. 13 (1985) 3739-3754
    • (1985) Nucl. Acids Res. , vol.13 , pp. 3739-3754
    • Morgan, W.D.1    Bear, D.G.2    Litchman, B.L.3    von Hippel, P.H.4
  • 18
    • 0023898207 scopus 로고
    • Interactions of Escherichia coli transcription termination factor rho with RNA. II. Electron microscopy and nuclease protection experiments
    • Bear D.G., Hicks P.S., Escudero K.W., Andrews C.L., McSwiggen J.A., and von Hippel P.H. Interactions of Escherichia coli transcription termination factor rho with RNA. II. Electron microscopy and nuclease protection experiments. J. Mol. Biol. 199 (1988) 623-635
    • (1988) J. Mol. Biol. , vol.199 , pp. 623-635
    • Bear, D.G.1    Hicks, P.S.2    Escudero, K.W.3    Andrews, C.L.4    McSwiggen, J.A.5    von Hippel, P.H.6
  • 19
    • 33750477997 scopus 로고    scopus 로고
    • Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor
    • Skordalakes E., and Berger J.M. Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor. Cell 127 (2006) 553-564
    • (2006) Cell , vol.127 , pp. 553-564
    • Skordalakes, E.1    Berger, J.M.2
  • 20
    • 0029869425 scopus 로고    scopus 로고
    • Mutational analysis and secondary structure model of the RNP1-like sequence motif of transcription termination factor Rho
    • Martinez A., Opperman T., and Richardson J.P. Mutational analysis and secondary structure model of the RNP1-like sequence motif of transcription termination factor Rho. J. Mol. Biol. 257 (1996) 895-908
    • (1996) J. Mol. Biol. , vol.257 , pp. 895-908
    • Martinez, A.1    Opperman, T.2    Richardson, J.P.3
  • 21
    • 0029081051 scopus 로고
    • Analysis of E. coli rho factor: mutations affecting secondary-site interactions
    • Pereira S., and Platt T. Analysis of E. coli rho factor: mutations affecting secondary-site interactions. J. Mol. Biol. 251 (1995) 30-40
    • (1995) J. Mol. Biol. , vol.251 , pp. 30-40
    • Pereira, S.1    Platt, T.2
  • 22
    • 0031746606 scopus 로고    scopus 로고
    • Functional and genetic analysis of regulatory regions of coliphage H-19B: location of shiga-like toxin and lysis genes suggest a role for phage functions in toxin release
    • Neely M.N., and Friedman D.I. Functional and genetic analysis of regulatory regions of coliphage H-19B: location of shiga-like toxin and lysis genes suggest a role for phage functions in toxin release. Mol. Microbiol. 28 (1998) 1255-1267
    • (1998) Mol. Microbiol. , vol.28 , pp. 1255-1267
    • Neely, M.N.1    Friedman, D.I.2
  • 23
    • 0025088052 scopus 로고
    • Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability
    • Lerner C.G., and Inouye M. Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability. Nucl. Acids Res. 18 (1990) 4631
    • (1990) Nucl. Acids Res. , vol.18 , pp. 4631
    • Lerner, C.G.1    Inouye, M.2
  • 24
    • 0026527507 scopus 로고
    • Termination efficiency at rho-dependent terminators depends on kinetic coupling between RNA polymerase and rho
    • Jin D.J., Burgess R.R., Richardson J.P., and Gross C.A. Termination efficiency at rho-dependent terminators depends on kinetic coupling between RNA polymerase and rho. Proc. Natl Acad. Sci. USA 89 (1992) 1453-1457
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 1453-1457
    • Jin, D.J.1    Burgess, R.R.2    Richardson, J.P.3    Gross, C.A.4
  • 25
    • 0023749808 scopus 로고
    • Mapping and sequencing of mutations in the Escherichia coli rpoB gene that lead to rifampicin resistance
    • Jin D.J., and Gross C.A. Mapping and sequencing of mutations in the Escherichia coli rpoB gene that lead to rifampicin resistance. J. Mol. Biol. 202 (1988) 45-58
    • (1988) J. Mol. Biol. , vol.202 , pp. 45-58
    • Jin, D.J.1    Gross, C.A.2
  • 26
    • 0017800538 scopus 로고
    • Mutant RNA polymerase of Escherichia coli terminates transcription in strains making defective rho factor
    • Guarente L.P., and Beckwith J. Mutant RNA polymerase of Escherichia coli terminates transcription in strains making defective rho factor. Proc. Natl Acad. Sci. USA 75 (1978) 294-297
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 294-297
    • Guarente, L.P.1    Beckwith, J.2
  • 27
    • 0033548445 scopus 로고    scopus 로고
    • Identifying the bicyclomycin binding domain through biochemical analysis of antibiotic-resistant rho proteins
    • Magyar A., Zhang X., Abdi F., Kohn H., and Widger W.R. Identifying the bicyclomycin binding domain through biochemical analysis of antibiotic-resistant rho proteins. J. Biol. Chem. 274 (1999) 7316-7324
    • (1999) J. Biol. Chem. , vol.274 , pp. 7316-7324
    • Magyar, A.1    Zhang, X.2    Abdi, F.3    Kohn, H.4    Widger, W.R.5
  • 28
    • 0029588669 scopus 로고
    • A mutation in the ATP binding domain of rho alters its RNA binding properties and uncouples ATP hydrolysis from helicase activity
    • Pereira S., and Platt T. A mutation in the ATP binding domain of rho alters its RNA binding properties and uncouples ATP hydrolysis from helicase activity. J. Biol. Chem. 270 (1995) 30401-30407
    • (1995) J. Biol. Chem. , vol.270 , pp. 30401-30407
    • Pereira, S.1    Platt, T.2
  • 29
    • 0033120903 scopus 로고    scopus 로고
    • The structural basis for terminator recognition by the Rho transcription termination factor
    • Bogden C.E., Fass D., Bergman N., Nichols M.D., and Berger J.M. The structural basis for terminator recognition by the Rho transcription termination factor. Mol. Cell 3 (1999) 487-493
    • (1999) Mol. Cell , vol.3 , pp. 487-493
    • Bogden, C.E.1    Fass, D.2    Bergman, N.3    Nichols, M.D.4    Berger, J.M.5
  • 30
    • 0027085888 scopus 로고
    • Functional interactions of ligand cofactors with Escherichia coli transcription termination factor rho. II. Binding of RNA
    • Geiselmann J., Yager T.D., and von Hippel P.H. Functional interactions of ligand cofactors with Escherichia coli transcription termination factor rho. II. Binding of RNA. Protein Sci. 1 (1992) 861-873
    • (1992) Protein Sci. , vol.1 , pp. 861-873
    • Geiselmann, J.1    Yager, T.D.2    von Hippel, P.H.3
  • 31
    • 33845940368 scopus 로고    scopus 로고
    • Sequence-specific interactions in the RNA-binding domain of Escherichia coli transcription termination factor Rho
    • Hitchens T.K., Zhan Y., Richardson L.V., Richardson J.P., and Rule G.S. Sequence-specific interactions in the RNA-binding domain of Escherichia coli transcription termination factor Rho. J. Biol. Chem. 281 (2006) 33697-33703
    • (2006) J. Biol. Chem. , vol.281 , pp. 33697-33703
    • Hitchens, T.K.1    Zhan, Y.2    Richardson, L.V.3    Richardson, J.P.4    Rule, G.S.5
  • 32
    • 0020490675 scopus 로고
    • Activation of rho protein ATPase requires simultaneous interaction at two kinds of nucleic acid-binding sites
    • Richardson J.P. Activation of rho protein ATPase requires simultaneous interaction at two kinds of nucleic acid-binding sites. J. Biol. Chem. 257 (1982) 5760-5766
    • (1982) J. Biol. Chem. , vol.257 , pp. 5760-5766
    • Richardson, J.P.1
  • 33
    • 0030009284 scopus 로고    scopus 로고
    • Residues in the RNP1-like sequence motif of Rho protein are involved in RNA-binding affinity and discrimination
    • Martinez A., Burns C.M., and Richardson J.P. Residues in the RNP1-like sequence motif of Rho protein are involved in RNA-binding affinity and discrimination. J. Mol. Biol. 257 (1996) 909-918
    • (1996) J. Mol. Biol. , vol.257 , pp. 909-918
    • Martinez, A.1    Burns, C.M.2    Richardson, J.P.3
  • 34
    • 0025255851 scopus 로고
    • Transcription termination factor rho has three distinct structural domains
    • Dolan J.W., Marshall N.F., and Richardson J.P. Transcription termination factor rho has three distinct structural domains. J. Biol. Chem. 265 (1990) 5747-5754
    • (1990) J. Biol. Chem. , vol.265 , pp. 5747-5754
    • Dolan, J.W.1    Marshall, N.F.2    Richardson, J.P.3
  • 35
    • 0023925795 scopus 로고
    • Interactions of Escherichia coli transcription termination factor rho with RNA. I. Binding stoichiometries and free energies
    • McSwiggen J.A., Bear D.G., and von Hippel P.H. Interactions of Escherichia coli transcription termination factor rho with RNA. I. Binding stoichiometries and free energies. J. Mol. Biol. 199 (1988) 609-622
    • (1988) J. Mol. Biol. , vol.199 , pp. 609-622
    • McSwiggen, J.A.1    Bear, D.G.2    von Hippel, P.H.3
  • 36
    • 0019960564 scopus 로고
    • 3rd rho Factors from polarity suppressor mutants with defects in their RNA interactions
    • Richardson J.P., and Carey J.L. 3rd rho Factors from polarity suppressor mutants with defects in their RNA interactions. J. Biol. Chem. 257 (1982) 5767-5771
    • (1982) J. Biol. Chem. , vol.257 , pp. 5767-5771
    • Richardson, J.P.1    Carey, J.L.2
  • 37
    • 1942437475 scopus 로고    scopus 로고
    • The binding of C10 oligomers to Escherichia coli transcription termination factor Rho
    • Chen X., and Stitt B.L. The binding of C10 oligomers to Escherichia coli transcription termination factor Rho. J. Biol. Chem. 279 (2004) 16301-16310
    • (2004) J. Biol. Chem. , vol.279 , pp. 16301-16310
    • Chen, X.1    Stitt, B.L.2
  • 39
    • 0025117624 scopus 로고
    • Resonance energy transfer study on the proximity relationship between the GTP binding site and the rifampicin binding site of Escherichia coli RNA polymerase
    • Kumar K.P., and Chatterji D. Resonance energy transfer study on the proximity relationship between the GTP binding site and the rifampicin binding site of Escherichia coli RNA polymerase. Biochemistry 29 (1990) 317-322
    • (1990) Biochemistry , vol.29 , pp. 317-322
    • Kumar, K.P.1    Chatterji, D.2
  • 40
    • 0346120324 scopus 로고    scopus 로고
    • Simple fluorescence assays probing conformational changes of Escherichia coli RNA polymerase during transcription initiation
    • Sen R., and Dasgupta D. Simple fluorescence assays probing conformational changes of Escherichia coli RNA polymerase during transcription initiation. Methods Enzymol. 370 (2003) 598-605
    • (2003) Methods Enzymol. , vol.370 , pp. 598-605
    • Sen, R.1    Dasgupta, D.2
  • 41
    • 0017582694 scopus 로고
    • Characterization of the nucleoside triphosphate phosphohydrolase (ATPase) activity of RNA synthesis termination factor p. I. Enzymatic properties and effects of inhibitors
    • Lowery C., and Richardson J.P. Characterization of the nucleoside triphosphate phosphohydrolase (ATPase) activity of RNA synthesis termination factor p. I. Enzymatic properties and effects of inhibitors. J. Biol. Chem. 252 (1977) 1375-1380
    • (1977) J. Biol. Chem. , vol.252 , pp. 1375-1380
    • Lowery, C.1    Richardson, J.P.2
  • 42
    • 0030026271 scopus 로고    scopus 로고
    • Characterization of an unusual Rho factor from the high G+ C Gram-positive bacterium Micrococcus luteus
    • Nowatzke W.L., and Richardson J.P. Characterization of an unusual Rho factor from the high G+ C Gram-positive bacterium Micrococcus luteus. J. Biol. Chem. 271 (1996) 742-747
    • (1996) J. Biol. Chem. , vol.271 , pp. 742-747
    • Nowatzke, W.L.1    Richardson, J.P.2
  • 43
    • 0346275199 scopus 로고    scopus 로고
    • Using a lac repressor roadblock to analyze the E. coli transcription elongation complex
    • King R.A., Sen R., and Weisberg R.A. Using a lac repressor roadblock to analyze the E. coli transcription elongation complex. Methods Enzymol. 371 (2003) 207-218
    • (2003) Methods Enzymol. , vol.371 , pp. 207-218
    • King, R.A.1    Sen, R.2    Weisberg, R.A.3
  • 44
    • 33748754299 scopus 로고    scopus 로고
    • Mechanism of inhibition of RHO-dependent transcription termination by bacteriophage P4 protein PSU
    • Pani B., Banerjee S., Chalissery J., Abhishek M., Malarini L.R., Suganthan R., and Sen R. Mechanism of inhibition of RHO-dependent transcription termination by bacteriophage P4 protein PSU. J. Biol. Chem. 281 (2006) 26491-26500
    • (2006) J. Biol. Chem. , vol.281 , pp. 26491-26500
    • Pani, B.1    Banerjee, S.2    Chalissery, J.3    Abhishek, M.4    Malarini, L.R.5    Suganthan, R.6    Sen, R.7
  • 45
    • 0018958616 scopus 로고
    • Studies of RNA release reaction catalyzed by E. coli transcription termination factor rho using isolated ternary transcription complexes
    • Shigesada K., and Wu C.W. Studies of RNA release reaction catalyzed by E. coli transcription termination factor rho using isolated ternary transcription complexes. Nucl. Acids Res. 8 (1980) 3355-3369
    • (1980) Nucl. Acids Res. , vol.8 , pp. 3355-3369
    • Shigesada, K.1    Wu, C.W.2
  • 46
    • 0017294366 scopus 로고
    • ATPase activity required for termination of transcription by the Escherichia coli protein factor rho
    • Howard B.H., and de Crombrugghe B. ATPase activity required for termination of transcription by the Escherichia coli protein factor rho. J. Biol. Chem. 251 (1976) 2520-2524
    • (1976) J. Biol. Chem. , vol.251 , pp. 2520-2524
    • Howard, B.H.1    de Crombrugghe, B.2
  • 47
    • 0023666140 scopus 로고
    • Transcription termination factor rho is an RNA-DNA helicase
    • Brennan C.A., Dombroski A.J., and Platt T. Transcription termination factor rho is an RNA-DNA helicase. Cell 48 (1987) 945-952
    • (1987) Cell , vol.48 , pp. 945-952
    • Brennan, C.A.1    Dombroski, A.J.2    Platt, T.3
  • 49
    • 0033582469 scopus 로고    scopus 로고
    • Activation of Rho-dependent transcription termination by NusG. Dependence on terminator location and acceleration of RNA release
    • Burns C.M., Nowatzke W.L., and Richardson J.P. Activation of Rho-dependent transcription termination by NusG. Dependence on terminator location and acceleration of RNA release. J. Biol. Chem. 274 (1999) 5245-5251
    • (1999) J. Biol. Chem. , vol.274 , pp. 5245-5251
    • Burns, C.M.1    Nowatzke, W.L.2    Richardson, J.P.3
  • 50
    • 0015505443 scopus 로고
    • Amber suA mutations which relieve polarity
    • Morse D.E., and Guertin M. Amber suA mutations which relieve polarity. J. Mol. Biol. 63 (1972) 605-608
    • (1972) J. Mol. Biol. , vol.63 , pp. 605-608
    • Morse, D.E.1    Guertin, M.2
  • 51
    • 0018085977 scopus 로고
    • Interaction of RNA polymerase and rho in transcription termination: coupled ATPase
    • Das A., Merril C., and Adhya S. Interaction of RNA polymerase and rho in transcription termination: coupled ATPase. Proc. Natl Acad. Sci. USA 75 (1978) 4828-4832
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 4828-4832
    • Das, A.1    Merril, C.2    Adhya, S.3
  • 52
    • 0024314683 scopus 로고
    • A microtiter plate-based system for the semiautomated growth and assay of bacterial cells for beta-galactosidase activity
    • Menzel R. A microtiter plate-based system for the semiautomated growth and assay of bacterial cells for beta-galactosidase activity. Anal. Biochem. 181 (1989) 40-50
    • (1989) Anal. Biochem. , vol.181 , pp. 40-50
    • Menzel, R.1
  • 53
    • 23944518352 scopus 로고    scopus 로고
    • Escherichia coli RNA polymerase mutations located near the upstream edge of an RNA:DNA hybrid and the beginning of the RNA-exit channel are defective for transcription antitermination by the N protein from lambdoid phage H-19B
    • Cheeran A., Babu Suganthan R., Swapna G., Bandey I., Achary M.S., Nagarajaram H.A., and Sen R. Escherichia coli RNA polymerase mutations located near the upstream edge of an RNA:DNA hybrid and the beginning of the RNA-exit channel are defective for transcription antitermination by the N protein from lambdoid phage H-19B. J. Mol. Biol. 352 (2005) 28-43
    • (2005) J. Mol. Biol. , vol.352 , pp. 28-43
    • Cheeran, A.1    Babu Suganthan, R.2    Swapna, G.3    Bandey, I.4    Achary, M.S.5    Nagarajaram, H.A.6    Sen, R.7
  • 55
    • 0026597267 scopus 로고
    • Physical properties of the Escherichia coli transcription termination factor rho. 2. Quaternary structure of the rho hexamer
    • Geiselmann J., Seifried S.E., Yager T.D., Liang C., and von Hippel P.H. Physical properties of the Escherichia coli transcription termination factor rho. 2. Quaternary structure of the rho hexamer. Biochemistry 31 (1992) 121-132
    • (1992) Biochemistry , vol.31 , pp. 121-132
    • Geiselmann, J.1    Seifried, S.E.2    Yager, T.D.3    Liang, C.4    von Hippel, P.H.5
  • 56
    • 0043237757 scopus 로고    scopus 로고
    • Host factor titration by chromosomal R-loops as a mechanism for runaway plasmid replication in transcription termination-defective mutants of Escherichia coli
    • Harinarayanan R., and Gowrishankar J. Host factor titration by chromosomal R-loops as a mechanism for runaway plasmid replication in transcription termination-defective mutants of Escherichia coli. J. Mol. Biol. 332 (2003) 31-46
    • (2003) J. Mol. Biol. , vol.332 , pp. 31-46
    • Harinarayanan, R.1    Gowrishankar, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.