메뉴 건너뛰기




Volumn 289, Issue 2, 2014, Pages 1151-1163

Antisense oligonucleotide-stimulated transcriptional pausing reveals RNA exit channel specificity of RNA polymerase and mechanistic contributions of NusA and RfaH

Author keywords

[No Author keywords available]

Indexed keywords

ANTISENSE; ANTISENSE RNA; BACTERIAL TRANSCRIPTION; DNA OLIGONUCLEOTIDES; RNA POLYMERASE; RNA STRUCTURES;

EID: 84891910083     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.521393     Document Type: Article
Times cited : (41)

References (58)
  • 1
    • 33846914726 scopus 로고    scopus 로고
    • The regulatory roles and mechanism of transcriptional pausing
    • Landick, R. (2006) The regulatory roles and mechanism of transcriptional pausing. Biochem. Soc. Trans. 34, 1062-1066
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 1062-1066
    • Landick, R.1
  • 2
    • 0033578330 scopus 로고    scopus 로고
    • Folding of a large ribozyme during transcription and the effect of the elongation factor NusA
    • Pan, T., Artsimovitch, I., Fang, X. W., Landick, R., and Sosnick, T. R. (1999) Folding of a large ribozyme during transcription and the effect of the elongation factor NusA. Proc. Natl. Acad. Sci. U.S.A. 96, 9545-9550
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 9545-9550
    • Pan, T.1    Artsimovitch, I.2    Fang, X.W.3    Landick, R.4    Sosnick, T.R.5
  • 4
    • 0022392670 scopus 로고
    • Translation activates the paused transcription complex and restores transcription of the trp operon leader region
    • Landick, R., Carey, J., and Yanofsky, C. (1985) Translation activates the paused transcription complex and restores transcription of the trp operon leader region. Proc. Natl. Acad. Sci. U.S.A. 82, 4663-4667
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 4663-4667
    • Landick, R.1    Carey, J.2    Yanofsky, C.3
  • 5
    • 0037133970 scopus 로고    scopus 로고
    • The transcriptional regulator RfaH stimulates RNA chain synthesis after recruitment to elongation complexes by the exposed nontemplate DNA strand
    • Artsimovitch, I., and Landick, R. (2002) The transcriptional regulator RfaH stimulates RNA chain synthesis after recruitment to elongation complexes by the exposed nontemplate DNA strand. Cell 109, 193-203
    • (2002) Cell , vol.109 , pp. 193-203
    • Artsimovitch, I.1    Landick, R.2
  • 6
    • 0033120034 scopus 로고    scopus 로고
    • The mechanism of intrinsic transcription termination
    • Gusarov, I., and Nudler, E. (1999) The mechanism of intrinsic transcription termination. Mol. Cell 3, 495-504
    • (1999) Mol. Cell , vol.3 , pp. 495-504
    • Gusarov, I.1    Nudler, E.2
  • 7
    • 79960395328 scopus 로고    scopus 로고
    • Bacterial transcription terminators. The RNA 3-end chronicles
    • Peters, J. M., Vangeloff, A. D., and Landick, R. (2011) Bacterial transcription terminators. The RNA 3-end chronicles. J. Mol. Biol. 412, 793-813
    • (2011) J. Mol. Biol. , vol.412 , pp. 793-813
    • Peters, J.M.1    Vangeloff, A.D.2    Landick, R.3
  • 8
    • 15944382675 scopus 로고    scopus 로고
    • The speed of RNA transcription and metabolite binding kinetics operate an FMN riboswitch
    • Wickiser, J. K., Winkler, W. C., Breaker, R. R., and Crothers, D. M. (2005) The speed of RNA transcription and metabolite binding kinetics operate an FMN riboswitch. Mol. Cell 18, 49-60
    • (2005) Mol. Cell , vol.18 , pp. 49-60
    • Wickiser, J.K.1    Winkler, W.C.2    Breaker, R.R.3    Crothers, D.M.4
  • 9
    • 77951589688 scopus 로고    scopus 로고
    • Cooperation between translating ribosomes and RNA polymerase in transcription elongation
    • Proshkin, S., Rahmouni, A. R., Mironov, A., and Nudler, E. (2010) Cooperation between translating ribosomes and RNA polymerase in transcription elongation. Science 328, 504-508
    • (2010) Science , vol.328 , pp. 504-508
    • Proshkin, S.1    Rahmouni, A.R.2    Mironov, A.3    Nudler, E.4
  • 10
    • 0019412155 scopus 로고
    • Pausing and termination of transcription within the early region of bacteriophage T7 DNA in vitro
    • Kassavetis, G. A., and Chamberlin, M. J. (1981) Pausing and termination of transcription within the early region of bacteriophage T7 DNA in vitro. J. Biol. Chem. 256, 2777-2786
    • (1981) J. Biol. Chem. , vol.256 , pp. 2777-2786
    • Kassavetis, G.A.1    Chamberlin, M.J.2
  • 11
    • 0345047725 scopus 로고    scopus 로고
    • Ubiquitous transcriptional pausing is independent of RNA polymerase backtracking
    • Neuman, K. C., Abbondanzieri, E. A., Landick, R., Gelles, J., and Block, S. M. (2003) Ubiquitous transcriptional pausing is independent of RNA polymerase backtracking. Cell 115, 437-447
    • (2003) Cell , vol.115 , pp. 437-447
    • Neuman, K.C.1    Abbondanzieri, E.A.2    Landick, R.3    Gelles, J.4    Block, S.M.5
  • 12
    • 0034691146 scopus 로고    scopus 로고
    • Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals
    • Artsimovitch, I., and Landick, R. (2000) Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals. Proc. Natl. Acad. Sci. U.S.A. 97, 7090-7095
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 7090-7095
    • Artsimovitch, I.1    Landick, R.2
  • 13
    • 34547204502 scopus 로고    scopus 로고
    • A central role of the RNA polymerase trigger loop in active-site rearrangement during transcriptional pausing
    • Toulokhonov, I., Zhang, J., Palangat, M., and Landick, R. (2007) A central role of the RNA polymerase trigger loop in active-site rearrangement during transcriptional pausing. Mol. Cell 27, 406-419
    • (2007) Mol. Cell , vol.27 , pp. 406-419
    • Toulokhonov, I.1    Zhang, J.2    Palangat, M.3    Landick, R.4
  • 14
    • 80051517051 scopus 로고    scopus 로고
    • Substrate loading, nucleotide addition, and translocation by RNA polymerase
    • (Buc, H., and Strick, T., eds) Royal Society of Chemistry, London
    • Zhang, J., and Landick, R. (2009) Substrate loading, nucleotide addition, and translocation by RNA polymerase. in RNA Polymerase as Molecular Motors (Buc, H., and Strick, T., eds) pp. 206-235, Royal Society of Chemistry, London
    • (2009) RNA Polymerase As Molecular Motors , pp. 206-235
    • Zhang, J.1    Landick, R.2
  • 16
    • 77953711880 scopus 로고    scopus 로고
    • Translocation by multisubunit RNA polymerases
    • Kireeva, M., Kashlev, M., and Burton, Z. F. (2010) Translocation by multisubunit RNA polymerases. Biochim. Biophys. Acta 1799, 389-401
    • (2010) Biochim. Biophys. Acta , vol.1799 , pp. 389-401
    • Kireeva, M.1    Kashlev, M.2    Burton, Z.F.3
  • 17
    • 84873323216 scopus 로고    scopus 로고
    • Structural basis of transcriptional pausing in bacteria
    • Weixlbaumer, A., Leon, K., Landick, R., and Darst, S. A. (2013) Structural basis of transcriptional pausing in bacteria. Cell 152, 431-441
    • (2013) Cell , vol.152 , pp. 431-441
    • Weixlbaumer, A.1    Leon, K.2    Landick, R.3    Darst, S.A.4
  • 18
    • 77449093660 scopus 로고    scopus 로고
    • Role of the RNA polymerase trigger loop in catalysis and pausing
    • Zhang, J., Palangat, M., and Landick, R. (2010) Role of the RNA polymerase trigger loop in catalysis and pausing. Nat. Struct. Mol. Biol. 17, 99-104
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 99-104
    • Zhang, J.1    Palangat, M.2    Landick, R.3
  • 19
    • 84880839662 scopus 로고    scopus 로고
    • Cys-pair reporters detect a constrained trigger loop in a paused RNA polymerase
    • Nayak, D., Voss, M., Windgassen, T., Mooney, R. A., and Landick, R. (2013) Cys-pair reporters detect a constrained trigger loop in a paused RNA polymerase. Mol. Cell 50, 882-893
    • (2013) Mol. Cell , vol.50 , pp. 882-893
    • Nayak, D.1    Voss, M.2    Windgassen, T.3    Mooney, R.A.4    Landick, R.5
  • 22
    • 0344413496 scopus 로고    scopus 로고
    • The flap domain is required for pause RNA hairpin inhibition of catalysis by RNA polymerase and can modulate intrinsic termination
    • Toulokhonov, I., and Landick, R. (2003) The flap domain is required for pause RNA hairpin inhibition of catalysis by RNA polymerase and can modulate intrinsic termination. Mol. Cell 12, 1125-1136
    • (2003) Mol. Cell , vol.12 , pp. 1125-1136
    • Toulokhonov, I.1    Landick, R.2
  • 23
    • 77955550450 scopus 로고    scopus 로고
    • The NusA N-terminal domain is necessary and sufficient for enhancement of transcriptional pausing via interaction with the RNA exit channel of RNA polymerase
    • Ha, K. S., Toulokhonov, I., Vassylyev, D. G., and Landick, R. (2010) The NusA N-terminal domain is necessary and sufficient for enhancement of transcriptional pausing via interaction with the RNA exit channel of RNA polymerase. J. Mol. Biol. 401, 708-725
    • (2010) J. Mol. Biol. , vol.401 , pp. 708-725
    • Ha, K.S.1    Toulokhonov, I.2    Vassylyev, D.G.3    Landick, R.4
  • 25
    • 0030738525 scopus 로고    scopus 로고
    • Preferential interaction of the his pause RNA hairpin with RNA polymerase-subunit residues 904-950 correlates with strong transcriptional pausing
    • Wang, D., Severinov, K., and Landick, R. (1997) Preferential interaction of the his pause RNA hairpin with RNA polymerase-subunit residues 904-950 correlates with strong transcriptional pausing. Proc. Natl. Acad. Sci. U.S.A. 94, 8433-8438
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8433-8438
    • Wang, D.1    Severinov, K.2    Landick, R.3
  • 26
    • 0027374650 scopus 로고
    • Dissection of the his leader pause site by base substitution reveals a multipartite signal that includes a pause RNA hairpin
    • Chan, C. L., and Landick, R. (1993) Dissection of the his leader pause site by base substitution reveals a multipartite signal that includes a pause RNA hairpin. J. Mol. Biol. 233, 25-42
    • (1993) J. Mol. Biol. , vol.233 , pp. 25-42
    • Chan, C.L.1    Landick, R.2
  • 27
    • 0035957687 scopus 로고    scopus 로고
    • Allosteric control of RNA polymerase by a site that contacts nascent RNA hairpins
    • Toulokhonov, I., Artsimovitch, I., and Landick, R. (2001) Allosteric control of RNA polymerase by a site that contacts nascent RNA hairpins. Science 292, 730-733
    • (2001) Science , vol.292 , pp. 730-733
    • Toulokhonov, I.1    Artsimovitch, I.2    Landick, R.3
  • 28
    • 34547097808 scopus 로고    scopus 로고
    • Direct versus limited-step reconstitution reveals key features of an RNA hairpin-stabilized paused transcription complex
    • Kyzer, S., Ha, K. S., Landick, R., and Palangat, M. (2007) Direct versus limited-step reconstitution reveals key features of an RNA hairpin-stabilized paused transcription complex. J. Biol. Chem. 282, 19020-19028
    • (2007) J. Biol. Chem. , vol.282 , pp. 19020-19028
    • Kyzer, S.1    Ha, K.S.2    Landick, R.3    Palangat, M.4
  • 29
    • 0035900642 scopus 로고    scopus 로고
    • Control of intrinsic transcription termination by N and NusA. The basic mechanisms
    • Gusarov, I., and Nudler, E. (2001) Control of intrinsic transcription termination by N and NusA. The basic mechanisms. Cell 107, 437-449
    • (2001) Cell , vol.107 , pp. 437-449
    • Gusarov, I.1    Nudler, E.2
  • 30
    • 79960449643 scopus 로고    scopus 로고
    • The-subunit gate loop is required for RNA polymerase modification by RfaH and NusG
    • Sevostyanova, A., Belogurov, G. A., Mooney, R. A., Landick, R., and Artsimovitch, I. (2011) The-subunit gate loop is required for RNA polymerase modification by RfaH and NusG. Mol. Cell 43, 253-262
    • (2011) Mol. Cell , vol.43 , pp. 253-262
    • Sevostyanova, A.1    Belogurov, G.A.2    Mooney, R.A.3    Landick, R.4    Artsimovitch, I.5
  • 34
    • 80051538984 scopus 로고    scopus 로고
    • RNA transcript 3-proximal sequence affects translocation bias of RNA polymerase
    • Hein, P. P., Palangat, M., and Landick, R. (2011) RNA transcript 3-proximal sequence affects translocation bias of RNA polymerase. Biochemistry 50, 7002-7014
    • (2011) Biochemistry , vol.50 , pp. 7002-7014
    • Hein, P.P.1    Palangat, M.2    Landick, R.3
  • 35
    • 0029834733 scopus 로고    scopus 로고
    • Quantitative analysis of transcriptional pausing by RNA polymerase: The his leader pause site as a paradigm
    • Landick, R., Wang, D., and Chan, C. (1996) Quantitative analysis of transcriptional pausing by RNA polymerase: the his leader pause site as a paradigm. Methods Enzymol. 274, 334-353
    • (1996) Methods Enzymol. , vol.274 , pp. 334-353
    • Landick, R.1    Wang, D.2    Chan, C.3
  • 36
    • 84861892611 scopus 로고    scopus 로고
    • A rule of seven in Watson-Crick base-pairing of mismatched sequences
    • Cisse, I. I., Kim, H., and Ha, T. (2012) A rule of seven in Watson-Crick base-pairing of mismatched sequences. Nat. Struct. Mol. Biol. 19, 623-627
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 623-627
    • Cisse, I.I.1    Kim, H.2    Ha, T.3
  • 37
  • 38
    • 67650676737 scopus 로고    scopus 로고
    • Two structurally independent domains of E coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators
    • Mooney, R. A., Schweimer, K., Rösch, P., Gottesman, M., and Landick, R. (2009) Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators. J. Mol. Biol. 391, 341-358
    • (2009) J. Mol. Biol. , vol.391 , pp. 341-358
    • Mooney, R.A.1    Schweimer, K.2    Rösch, P.3    Gottesman, M.4    Landick, R.5
  • 39
    • 0032190641 scopus 로고    scopus 로고
    • Interaction of a nascent RNA structure with RNA polymerase is required for hairpin-dependent transcriptional pausing but not for transcript release
    • Artsimovitch, I., and Landick, R. (1998) Interaction of a nascent RNA structure with RNA polymerase is required for hairpin-dependent transcriptional pausing but not for transcript release. Genes Dev. 12, 3110-3122
    • (1998) Genes Dev. , vol.12 , pp. 3110-3122
    • Artsimovitch, I.1    Landick, R.2
  • 40
    • 0031585988 scopus 로고    scopus 로고
    • Effects of neutral salts on RNA chain elongation and pausing by Escherichia coli RNA polymerase
    • Chan, C. L., and Landick, R. (1997) Effects of neutral salts on RNA chain elongation and pausing by Escherichia coli RNA polymerase. J. Mol. Biol. 268, 37-53
    • (1997) J. Mol. Biol. , vol.268 , pp. 37-53
    • Chan, C.L.1    Landick, R.2
  • 41
    • 0033565267 scopus 로고    scopus 로고
    • Nucleic acid duplex stability. Influence of base composition on cation effects
    • Nakano, S., Fujimoto, M., Hara, H., and Sugimoto, N. (1999) Nucleic acid duplex stability. Influence of base composition on cation effects. Nucleic Acids Res. 27, 2957-2965
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2957-2965
    • Nakano, S.1    Fujimoto, M.2    Hara, H.3    Sugimoto, N.4
  • 42
    • 43249095784 scopus 로고    scopus 로고
    • Predicting stability of DNA duplexes in solutions containing magnesium and monovalent cations
    • Owczarzy, R., Moreira, B. G., You, Y., Behlke, M. A., and Walder, J. A. (2008) Predicting stability of DNA duplexes in solutions containing magnesium and monovalent cations. Biochemistry 47, 5336-5353
    • (2008) Biochemistry , vol.47 , pp. 5336-5353
    • Owczarzy, R.1    Moreira, B.G.2    You, Y.3    Behlke, M.A.4    Walder, J.A.5
  • 43
    • 1642380887 scopus 로고    scopus 로고
    • Effects of sodium ions on DNA duplex oligomers. Improved predictions of melting temperatures
    • Owczarzy, R., You, Y., Moreira, B. G., Manthey, J. A., Huang, L., Behlke, M. A., and Walder, J. A. (2004) Effects of sodium ions on DNA duplex oligomers. Improved predictions of melting temperatures. Biochemistry 43, 3537-3554
    • (2004) Biochemistry , vol.43 , pp. 3537-3554
    • Owczarzy, R.1    You, Y.2    Moreira, B.G.3    Manthey, J.A.4    Huang, L.5    Behlke, M.A.6    Walder, J.A.7
  • 44
    • 0032552882 scopus 로고    scopus 로고
    • Thermodynamic parameters for an expanded nearest-neighbor model for formation of RNA duplexes with Watson-Crick base pairs
    • Xia, T., SantaLucia, J., Jr., Burkard, M. E., Kierzek, R., Schroeder, S. J., Jiao, X., Cox, C., and Turner, D. H. (1998) Thermodynamic parameters for an expanded nearest-neighbor model for formation of RNA duplexes with Watson-Crick base pairs. Biochemistry 37, 14719-14735
    • (1998) Biochemistry , vol.37 , pp. 14719-14735
    • Xia, T.1    SantaLucia Jr., J.2    Burkard, M.E.3    Kierzek, R.4    Schroeder, S.J.5    Jiao, X.6    Cox, C.7    Turner, D.H.8
  • 46
    • 0019942479 scopus 로고
    • Effects of NusA protein on transcription termination of the tryptophan operon of Escherichia coli
    • Farnham, P. J., Greenblatt, J., and Platt, T. (1982) Effects of NusA protein on transcription termination of the tryptophan operon of Escherichia coli. Cell 29, 945-951
    • (1982) Cell , vol.29 , pp. 945-951
    • Farnham, P.J.1    Greenblatt, J.2    Platt, T.3
  • 47
    • 0021217722 scopus 로고
    • Stability of an RNA secondary structure affects in vitro transcription pausing in the trp operon leader region
    • Landick, R., and Yanofsky, C. (1984) Stability of an RNA secondary structure affects in vitro transcription pausing in the trp operon leader region. J. Biol. Chem. 259, 11550-11555
    • (1984) J. Biol. Chem. , vol.259 , pp. 11550-11555
    • Landick, R.1    Yanofsky, C.2
  • 48
    • 34748854260 scopus 로고    scopus 로고
    • A transcription antiterminator constructs a NusA-dependent shield to the emerging transcript
    • Shankar, S., Hatoum, A., and Roberts, J. W. (2007) A transcription antiterminator constructs a NusA-dependent shield to the emerging transcript. Mol. Cell 27, 914-927
    • (2007) Mol. Cell , vol.27 , pp. 914-927
    • Shankar, S.1    Hatoum, A.2    Roberts, J.W.3
  • 49
    • 77954840190 scopus 로고    scopus 로고
    • The interaction between RNA polymerase and the elongation factor NusA
    • Yang, X., and Lewis, P. J. (2010) The interaction between RNA polymerase and the elongation factor NusA. RNA Biol. 7, 272-275
    • (2010) RNA Biol. , vol.7 , pp. 272-275
    • Yang, X.1    Lewis, P.J.2
  • 52
    • 79953779997 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity
    • Martinez-Rucobo, F. W., Sainsbury, S., Cheung, A. C., and Cramer, P. (2011) Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity. EMBO J. 30, 1302-1310
    • (2011) EMBO J. , vol.30 , pp. 1302-1310
    • Martinez-Rucobo, F.W.1    Sainsbury, S.2    Cheung, A.C.3    Cramer, P.4
  • 53
    • 55849112295 scopus 로고    scopus 로고
    • Function of the Bacillus subtilis transcription elongation factor NusG in hairpin-dependent RNA polymerase pausing in the trp leader
    • Yakhnin, A. V., Yakhnin, H., and Babitzke, P. (2008) Function of the Bacillus subtilis transcription elongation factor NusG in hairpin-dependent RNA polymerase pausing in the trp leader. Proc. Natl. Acad. Sci. U.S.A. 105, 16131-16136
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 16131-16136
    • Yakhnin, A.V.1    Yakhnin, H.2    Babitzke, P.3
  • 55
    • 0038823636 scopus 로고    scopus 로고
    • Cooverexpression of E coli RNA polymerase subunits allows isolation and analysis of mutant enzymes lacking lineage-specific sequence insertions
    • Artsimovitch, I., Svetlov, V., Murakami, K. S., and Landick, R. (2003) Cooverexpression of E. coli RNA polymerase subunits allows isolation and analysis of mutant enzymes lacking lineage-specific sequence insertions. J. Biol. Chem. 278, 12344-12355
    • (2003) J. Biol. Chem. , vol.278 , pp. 12344-12355
    • Artsimovitch, I.1    Svetlov, V.2    Murakami, K.S.3    Landick, R.4
  • 56
    • 0034973423 scopus 로고    scopus 로고
    • An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA
    • Worbs, M., Bourenkov, G. P., Bartunik, H. D., Huber, R., and Wahl, M. C. (2001) An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. Mol. Cell 7, 1177-1189
    • (2001) Mol. Cell , vol.7 , pp. 1177-1189
    • Worbs, M.1    Bourenkov, G.P.2    Bartunik, H.D.3    Huber, R.4    Wahl, M.C.5
  • 58
    • 0030572981 scopus 로고    scopus 로고
    • The structure of an RNA/DNA hybrid.Asubstrate of the ribonuclease activity of HIV-1 reverse transcriptase
    • Horton, N. C., and Finzel, B. C. (1996) The structure of an RNA/DNA hybrid.Asubstrate of the ribonuclease activity of HIV-1 reverse transcriptase. J. Mol. Biol. 264, 521-533
    • (1996) J. Mol. Biol. , vol.264 , pp. 521-533
    • Horton, N.C.1    Finzel, B.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.