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Volumn 5, Issue , 2015, Pages

Exploring RNA polymerase regulation by NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED RNA POLYMERASE; PROTEIN BINDING; PROTEIN SUBUNIT; RIBOSOMAL PROTEIN S10; RIBOSOME PROTEIN; TRANSCRIPTION FACTOR;

EID: 84930679218     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep10825     Document Type: Article
Times cited : (12)

References (43)
  • 1
    • 78651504121 scopus 로고    scopus 로고
    • Evolution of multisubunit rna polymerases in the three domains of life
    • Werner, F. & Grohmann, D. Evolution of multisubunit RNA polymerases in the three domains of life. Nat. Rev. Microbiol. 9, 85-98. (2011
    • (2011) Nat. Rev. Microbiol , vol.9 , pp. 85-98
    • Werner, F.1    Grohmann, D.2
  • 2
    • 0014691239 scopus 로고
    • Separation and characterization of the subunits of ribonucleic acid polymerase
    • Burgess, R. R. Separation and characterization of the subunits of ribonucleic acid polymerase. J. Biol. Chem. 244, 6168-6176. (1969
    • (1969) J. Biol. Chem , vol.244 , pp. 6168-6176
    • Burgess, R.R.1
  • 3
    • 0032032533 scopus 로고    scopus 로고
    • Conversion of the ? Subunit of escherichia coli rna polymerase into a transcriptional activator or an activation target
    • Dove, S. L. & Hochschild, A. Conversion of the ? subunit of Escherichia coli RNA polymerase into a transcriptional activator or an activation target. Genes Dev. 12, 745-754. (1998
    • (1998) Genes Dev , vol.12 , pp. 745-754
    • Dove, S.L.1    Hochschild, A.2
  • 4
    • 0031564644 scopus 로고    scopus 로고
    • Flexible linker in the rna polymerase a subunit facilitates the independent motion of the c-Terminal activator contact domain
    • Jeon, Y. H., Yamazaki, T., Otomo, T., Ishihama, A. & Kyogoku, Y. Flexible linker in the RNA polymerase a subunit facilitates the independent motion of the C-Terminal activator contact domain. J. Mol. Biol. 267, 953-962. (1997
    • (1997) J. Mol. Biol , vol.267 , pp. 953-962
    • Jeon, Y.H.1    Yamazaki, T.2    Otomo, T.3    Ishihama, A.4    Kyogoku, Y.5
  • 5
    • 79958701958 scopus 로고    scopus 로고
    • Nusa interaction with the a -subunit of E Coli RNA polymerase is via the UP-element site and releases autoinhibition
    • Schweimer, K, et al. NusA interaction with the a -subunit of E. coli RNA polymerase is via the UP-element site and releases autoinhibition. Structure. 19, 945-954. (2011
    • (2011) Structure , vol.19 , pp. 945-954
    • Schweimer, K.1
  • 6
    • 0016782152 scopus 로고
    • Biosynthesis of rna polymerase in escherichia coli iii identification of intermediates in the assembly of rna polymerase
    • Ito, K., Iwakura, Y. & Ishihama, A. Biosynthesis of RNA polymerase in Escherichia coli. III. Identification of intermediates in the assembly of RNA polymerase. J. Mol. Biol. 96, 257-271. (1975
    • (1975) J. Mol. Biol , vol.96 , pp. 257-271
    • Ito, K.1    Iwakura, Y.2    Ishihama, A.3
  • 7
    • 0035725661 scopus 로고    scopus 로고
    • Escherichia coli rna polymerase subunit ? and its n-Terminal domain bind full-length β to facilitate incorporation into the a 2βsubassembly
    • Ghosh, P., Ishihama, A. & Chatterji, D. Escherichia coli RNA polymerase subunit ? and its N-Terminal domain bind full-length β to facilitate incorporation into the a 2βsubassembly. Eur. J. Biochem. 268, 4621-4627. (2001
    • (2001) Eur. J. Biochem , vol.268 , pp. 4621-4627
    • Ghosh, P.1    Ishihama, A.2    Chatterji, D.3
  • 8
    • 0030917007 scopus 로고    scopus 로고
    • Modular organization of the catalytic center of rna polymerase
    • Mustaev, A, et al. Modular organization of the catalytic center of RNA polymerase. Proc. Natl. Acad. Sci. U. S. A. 94, 6641-6645. (1997
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6641-6645
    • Mustaev, A.1
  • 9
    • 0033587756 scopus 로고    scopus 로고
    • Interactions of escherichia coli s 70 within the transcription elongation complex
    • Daube, S. S. & von Hippel, P. H. Interactions of Escherichia coli s 70 within the transcription elongation complex. Proc. Natl. Acad. Sci. U. S. A. 96, 8390-8395. (1999
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 8390-8395
    • Daube, S.S.1    Von Hippel, P.H.2
  • 10
    • 0035943446 scopus 로고    scopus 로고
    • Translocation of s 70 with rna polymerase during transcription: Fluorescence resonance energy transfer assay for movement relative to dna
    • Mukhopadhyay, J, et al. Translocation of s 70 with RNA polymerase during transcription: fluorescence resonance energy transfer assay for movement relative to DNA. Cell. 106, 453-463. (2001
    • (2001) Cell , vol.106 , pp. 453-463
    • Mukhopadhyay, J.1
  • 11
    • 0031801743 scopus 로고    scopus 로고
    • Information processing by rna polymerase: Recognition of regulatory signals during rna chain elongation
    • Mooney, R. A., Artsimovitch, I. & Landick, R. Information processing by RNA polymerase: recognition of regulatory signals during RNA chain elongation. J. Bacteriol. 180, 3265-3275. (1998
    • (1998) J. Bacteriol , vol.180 , pp. 3265-3275
    • Mooney, R.A.1    Artsimovitch, I.2    Landick, R.3
  • 12
    • 0034691146 scopus 로고    scopus 로고
    • Pausing by bacterial rna polymerase is mediated by mechanistically distinct classes of signals
    • Artsimovitch, I. & Landick, R. Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals. Proc. Natl. Acad. Sci. U. S. A. 97, 7090-7095. (2000
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 7090-7095
    • Artsimovitch, I.1    Landick, R.2
  • 13
    • 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. & Cramer, P. Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity. EMBO J. 30, 1302-1310. (2011
    • (2011) EMBO J. , vol.30 , pp. 1302-1310
    • Martinez-Rucobo, F.W.1    Sainsbury, S.2    Cheung, A.C.3    Cramer, P.4
  • 14
    • 79960449643 scopus 로고    scopus 로고
    • The βsubunit gate loop is required for rna polymerase modification by rfah and nusg
    • Sevostyanova, A., Belogurov, G. A., Mooney, R. A., Landick, R. & Artsimovitch, I. The βsubunit gate loop is required for RNA polymerase modification by RfaH and NusG. Mol. Cell. 43, 253-262. (2011
    • (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
  • 15
    • 14844329013 scopus 로고    scopus 로고
    • Bacterial transcription elongation factors: New insights into molecular mechanism of action
    • Borukhov, S., Lee, J. & Laptenko, O. Bacterial transcription elongation factors: new insights into molecular mechanism of action. Mol. Microbiol. 55, 1315-1324. (2005
    • (2005) Mol. Microbiol , vol.55 , pp. 1315-1324
    • Borukhov, S.1    Lee, J.2    Laptenko, O.3
  • 17
    • 79954597274 scopus 로고    scopus 로고
    • Termination and antitermination: Rna polymerase runs a stop sign
    • Santangelo, T. J. & Artsimovitch, I. Termination and antitermination: RNA polymerase runs a stop sign. Nat. Rev. Microbiol. 9, 319-329. (2011
    • (2011) Nat. Rev. Microbiol , vol.9 , pp. 319-329
    • Santangelo, T.J.1    Artsimovitch, I.2
  • 18
    • 77951541717 scopus 로고    scopus 로고
    • A nuse:nusg complex links transcription and translation
    • Burmann, B. M, et al. A NusE:NusG complex links transcription and translation. Science. 328, 501-504. (2010
    • (2010) Science , vol.328 , pp. 501-504
    • Burmann, B.M.1
  • 21
    • 0026095918 scopus 로고
    • Assembly of transcription elongation complexes containing the n protein of phage ? and the escherichia coli elongation factors nusa, nusb, nusg, and s10
    • Mason, S. W. & Greenblatt, J. Assembly of transcription elongation complexes containing the N protein of phage ? and the Escherichia coli elongation factors NusA, NusB, NusG, and S10. Genes Dev. 5, 1504-1512. (1991
    • (1991) Genes Dev , vol.5 , pp. 1504-1512
    • Mason, S.W.1    Greenblatt, J.2
  • 22
    • 84857031357 scopus 로고    scopus 로고
    • Structural basis of transcription by bacterial and eukaryotic rna polymerases
    • Sekine, S., Tagami, S. & Yokoyama, S. Structural basis of transcription by bacterial and eukaryotic RNA polymerases. Curr. Opin. Struct. Biol. 22, 110-118. (2012
    • (2012) Curr. Opin. Struct. Biol , vol.22 , pp. 110-118
    • Sekine, S.1    Tagami, S.2    Yokoyama, S.3
  • 23
    • 0024284781 scopus 로고
    • Nmr sequential assignment of escherichia coli thioredoxin utilizing random fractional deuteriation
    • LeMaster, D. M. & Richards, F. M. NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriation. Biochemistry. 27, 142-150. (1988
    • (1988) Biochemistry , vol.27 , pp. 142-150
    • Lemaster, D.M.1    Richards, F.M.2
  • 24
    • 0032506009 scopus 로고    scopus 로고
    • Trosy in triple-resonance experiments: New perspectives for sequential nmr assignment of large proteins
    • Salzmann, M., Pervushin, K., Wider, G., Senn, H. & Wüthrich, K. TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. Proc. Natl. Acad. Sci. U. S. A. 95, 13585-13590. (1998
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13585-13590
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wüthrich, K.5
  • 25
    • 0037432547 scopus 로고    scopus 로고
    • Quantitative nmr studies of high molecular weight proteins: Application to domain orientation and ligand binding in the 723 residue enzyme malate synthase g
    • Tugarinov, V. & Kay, L. E. Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the. 723 residue enzyme malate synthase G. J. Mol. Biol. 327, 1121-1133. (2003
    • (2003) J. Mol. Biol , vol.327 , pp. 1121-1133
    • Tugarinov, V.1    Kay, L.E.2
  • 26
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20s proteasome by nmr
    • Sprangers, R. & Kay, L. E. Quantitative dynamics and binding studies of the. 20S proteasome by NMR. Nature. 445, 618-622. (2007
    • (2007) Nature , vol.445 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 27
    • 0005443595 scopus 로고
    • Reconstitution of bacterial dna-dependent rna polymerase from isolated subunits as a tool for the elucidation of the role of the subunits in transcription
    • Heil, A. & Zillig, W. Reconstitution of bacterial DNA-dependent RNA polymerase from isolated subunits as a tool for the elucidation of the role of the subunits in transcription. FEBS Lett. 11, 165-168. (1970
    • (1970) FEBS Lett , vol.11 , pp. 165-168
    • Heil, A.1    Zillig, W.2
  • 28
    • 0027744758 scopus 로고
    • Recombinant escherichia coli rna polymerase: Purification of individually overexpressed subunits and in vitro assembly
    • Borukhov, S. & Goldfarb, A. Recombinant Escherichia coli RNA polymerase: purification of individually overexpressed subunits and in vitro assembly. Protein Expr. Purif. 4, 503-511. (1993
    • (1993) Protein Expr. Purif , vol.4 , pp. 503-511
    • Borukhov, S.1    Goldfarb, A.2
  • 29
    • 0029040106 scopus 로고
    • Rapid rna polymerase genetics: One-day, no-column preparation of reconstituted recombinant escherichia coli rna polymerase
    • Tang, H., Severinov, K., Goldfarb, A. & Ebright, R. H. Rapid RNA polymerase genetics: one-day, no-column preparation of reconstituted recombinant Escherichia coli RNA polymerase. Proc. Natl. Acad. Sci. U. S. A. 92, 4902-4906. (1995
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 4902-4906
    • Tang, H.1    Severinov, K.2    Goldfarb, A.3    Ebright, R.H.4
  • 30
    • 0025886298 scopus 로고
    • The ? Subunit of escherichia coli k-12 rna polymerase is not required for stringent rna control in vivo
    • Gentry, D., Xiao, H., Burgess, R. & Cashel, M. The ? subunit of Escherichia coli K-12 RNA polymerase is not required for stringent RNA control in vivo. J. Bacteriol. 173, 3901-3903. (1991
    • (1991) J. Bacteriol , vol.173 , pp. 3901-3903
    • Gentry, D.1    Xiao, H.2    Burgess, R.3    Cashel, M.4
  • 31
    • 0033571313 scopus 로고    scopus 로고
    • Groel is involved in activation of escherichia coli rna polymerase devoid of the ? Subunit in vivo
    • Mukherjee, K., Nagai, H., Shimamoto, N. & Chatterji, D. GroEL is involved in activation of Escherichia coli RNA polymerase devoid of the ? subunit in vivo. Eur. J. Biochem. 266, 228-235. (1999
    • (1999) Eur. J. Biochem , vol.266 , pp. 228-235
    • Mukherjee, K.1    Nagai, H.2    Shimamoto, N.3    Chatterji, D.4
  • 32
    • 0034602995 scopus 로고    scopus 로고
    • Mapping of subunit-subunit contact surfaces on the βsubunit of escherichia coli rna polymerase
    • Katayama, A., Fujita, N. & Ishihama, A. Mapping of subunit-subunit contact surfaces on the βsubunit of Escherichia coli RNA polymerase. J. Biol. Chem. 275, 3583-3592. (2000
    • (2000) J. Biol. Chem , vol.275 , pp. 3583-3592
    • Katayama, A.1    Fujita, N.2    Ishihama, A.3
  • 33
    • 23644454655 scopus 로고    scopus 로고
    • The e coli nusa carboxy-terminal domains are structurally similar and show specific rnap- and ? N interaction
    • Eisenmann, A., Schwarz, S., Prasch, S., Schweimer, K. & Rfsch, P. The E. coli NusA carboxy-Terminal domains are structurally similar and show specific RNAP- And ? N interaction. Protein Sci. 14, 2018-2029. (2005
    • (2005) Protein Sci , vol.14 , pp. 2018-2029
    • Eisenmann, A.1    Schwarz, S.2    Prasch, S.3    Schweimer, K.4    Rösch, P.5
  • 34
    • 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. & Wahl, M. C. An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. Mol. Cell. 7, 1177-1189. (2001
    • (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
  • 35
    • 0035957687 scopus 로고    scopus 로고
    • Allosteric control of rna polymerase by a site that contacts nascent rna hairpins
    • Toulokhonov, I., Artsimovitch, I. & Landick, R. Allosteric control of RNA polymerase by a site that contacts nascent RNA hairpins. Science. 292, 730-733. (2001
    • (2001) Science , vol.292 , pp. 730-733
    • Toulokhonov, I.1    Artsimovitch, I.2    Landick, R.3
  • 36
    • 69949141607 scopus 로고    scopus 로고
    • The structure of bacterial rna polymerase in complex with the essential transcription elongation factor nusa
    • Yang, X, et al. The structure of bacterial RNA polymerase in complex with the essential transcription elongation factor NusA. EMBO Rep. 10, 997-1002. (2009
    • (2009) EMBO Rep , vol.10 , pp. 997-1002
    • Yang, X.1
  • 37
    • 57749115164 scopus 로고    scopus 로고
    • Structural and functional analysis of the e coli nusb-s10 transcription antitermination complex
    • Luo, X, et al. Structural and functional analysis of the E. coli NusB-S10 transcription antitermination complex. Mol. Cell. 32, 791-802. (2008
    • (2008) Mol. Cell , vol.32 , pp. 791-802
    • Luo, X.1
  • 38
    • 0038823636 scopus 로고    scopus 로고
    • Co-overexpression of escherichia coli rna polymerase subunits allows isolation and analysis of mutant enzymes lacking lineage-specific sequence insertions
    • Artsimovitch, I., Svetlov, V., Murakami, K. S. & Landick, R. Co-overexpression of Escherichia coli RNA polymerase subunits allows isolation and analysis of mutant enzymes lacking lineage-specific sequence insertions. J. Biol. Chem. 278, 12344-12355. (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 12344-12355
    • Artsimovitch, I.1    Svetlov, V.2    Murakami, K.S.3    Landick, R.4
  • 39
    • 0020653833 scopus 로고
    • Biology of aerobic carbon monoxide-oxidizing bacteria
    • Meyer, O. & Schlegel, H. G. Biology of aerobic carbon monoxide-oxidizing bacteria. Annu. Rev. Microbiol. 37, 277-310. (1983
    • (1983) Annu. Rev. Microbiol , vol.37 , pp. 277-310
    • Meyer, O.1    Schlegel, H.G.2
  • 42
    • 4644259437 scopus 로고    scopus 로고
    • Using nmrview to visualize and analyze the nmr spectra of macromolecules
    • Johnson, B. A. Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278, 313-352. (2004
    • (2004) Methods Mol. Biol , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 43
    • 33846561471 scopus 로고    scopus 로고
    • Practical aspects of 1h transverse paramagnetic relaxation enhancement measurements on macromolecules
    • Iwahara, J., Tang, C. & Marius Clore, G. Practical aspects of 1H transverse paramagnetic relaxation enhancement measurements on macromolecules. J. Magn. Reson. 184, 185-195. (2007
    • (2007) J. Magn. Reson , vol.184 , pp. 185-195
    • Iwahara, J.1    Tang, C.2    Marius Clore, G.3


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