메뉴 건너뛰기




Volumn 20, Issue 3, 2005, Pages 335-345

Sigma and RNA polymerase: An on-again, off-again relationship?

Author keywords

[No Author keywords available]

Indexed keywords

HOLOENZYME; RNA POLYMERASE; SIGMA FACTOR;

EID: 27644560257     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.10.015     Document Type: Review
Times cited : (129)

References (81)
  • 1
    • 0023711743 scopus 로고
    • Transcription termination in Escherichia coli. Measurement of the rate of enzyme release from Rho-independent terminators
    • K.M. Arndt, and M.J. Chamberlin Transcription termination in Escherichia coli. Measurement of the rate of enzyme release from Rho-independent terminators J. Mol. Biol. 202 1988 271 285
    • (1988) J. Mol. Biol. , vol.202 , pp. 271-285
    • Arndt, K.M.1    Chamberlin, M.J.2
  • 2
    • 0037133970 scopus 로고    scopus 로고
    • The transcriptional regulator RfaH stimulates RNA chain synthesis after recruitment to elongation complexes by the exposed nontemplate DNA strand
    • I. Artsimovitch, and R. Landick The transcriptional regulator RfaH stimulates RNA chain synthesis after recruitment to elongation complexes by the exposed nontemplate DNA strand Cell 109 2002 193 203
    • (2002) Cell , vol.109 , pp. 193-203
    • Artsimovitch, I.1    Landick, R.2
  • 3
    • 0035943341 scopus 로고    scopus 로고
    • Isolation and characterization of sigma(70)-retaining transcription elongation complexes from Escherichia coli
    • G. Bar-Nahum, and E. Nudler Isolation and characterization of sigma(70)-retaining transcription elongation complexes from Escherichia coli Cell 106 2001 443 451
    • (2001) Cell , vol.106 , pp. 443-451
    • Bar-Nahum, G.1    Nudler, E.2
  • 4
    • 0035951305 scopus 로고    scopus 로고
    • Mechanism of regulation of transcription initiation by ppGpp. I. Effects of ppGpp on transcription initiation in vivo and in vitro
    • M.M. Barker, T. Gaal, C.A. Josaitis, and R.L. Gourse Mechanism of regulation of transcription initiation by ppGpp. I. Effects of ppGpp on transcription initiation in vivo and in vitro J. Mol. Biol. 305 2001 673 688
    • (2001) J. Mol. Biol. , vol.305 , pp. 673-688
    • Barker, M.M.1    Gaal, T.2    Josaitis, C.A.3    Gourse, R.L.4
  • 6
    • 12844288620 scopus 로고    scopus 로고
    • Altering the interaction between sigma70 and RNA polymerase generates complexes with distinct transcription-elongation properties
    • Y. Berghofer-Hochheimer, C.Z. Lu, and C.A. Gross Altering the interaction between sigma70 and RNA polymerase generates complexes with distinct transcription-elongation properties Proc. Natl. Acad. Sci. USA 102 2005 1157 1162
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1157-1162
    • Berghofer-Hochheimer, Y.1    Lu, C.Z.2    Gross, C.A.3
  • 7
    • 0038013991 scopus 로고    scopus 로고
    • RNA polymerase holoenzyme: Structure, function and biological implications
    • S. Borukhov, and E. Nudler RNA polymerase holoenzyme: structure, function and biological implications Curr. Opin. Microbiol. 6 2003 93 100
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 93-100
    • Borukhov, S.1    Nudler, E.2
  • 8
    • 14844329013 scopus 로고    scopus 로고
    • Bacterial transcription elongation factors: New insights into molecular mechanism of action
    • S. Borukhov, J. Lee, and O. Laptenko Bacterial transcription elongation factors: new insights into molecular mechanism of action Mol. Microbiol. 55 2005 1315 1324
    • (2005) Mol. Microbiol. , vol.55 , pp. 1315-1324
    • Borukhov, S.1    Lee, J.2    Laptenko, O.3
  • 9
    • 2542456496 scopus 로고    scopus 로고
    • The sigma 70 subunit of RNA polymerase induces lacUV5 promoter-proximal pausing of transcription
    • K. Brodolin, N. Zenkin, A. Mustaev, D. Mamaeva, and H. Heumann The sigma 70 subunit of RNA polymerase induces lacUV5 promoter-proximal pausing of transcription Nat. Struct. Mol. Biol. 11 2004 551 557
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 551-557
    • Brodolin, K.1    Zenkin, N.2    Mustaev, A.3    Mamaeva, D.4    Heumann, H.5
  • 10
    • 0036789619 scopus 로고    scopus 로고
    • Physics of protein-DNA interaction
    • R. Bruinsma Physics of protein-DNA interaction Physica A (Amsterdam) 313 2002 211 237
    • (2002) Physica a (Amsterdam) , vol.313 , pp. 211-237
    • Bruinsma, R.1
  • 12
    • 27644515130 scopus 로고    scopus 로고
    • Regulation of bacterial transcription by anti-s factors
    • G. Waksman M. Caparon S. Hultgren American Society of Microbiology Washington, D.C.
    • E. Campbell, and S. Darst Regulation of bacterial transcription by anti-s factors G. Waksman M. Caparon S. Hultgren Structural Biology of Bacterial Pathogenesis 2005 American Society of Microbiology Washington, D.C. 1 15
    • (2005) Structural Biology of Bacterial Pathogenesis , pp. 1-15
    • Campbell, E.1    Darst, S.2
  • 13
    • 0037155726 scopus 로고    scopus 로고
    • Crystal structure of the Bacillus stearothermophilus anti-sigma factor SpoIIAB with the sporulation sigma factor sigmaF
    • E.A. Campbell, S. Masuda, J.L. Sun, O. Muzzin, C.A. Olson, S. Wang, and S.A. Darst Crystal structure of the Bacillus stearothermophilus anti-sigma factor SpoIIAB with the sporulation sigma factor sigmaF Cell 108 2002 795 807
    • (2002) Cell , vol.108 , pp. 795-807
    • Campbell, E.A.1    Masuda, S.2    Sun, J.L.3    Muzzin, O.4    Olson, C.A.5    Wang, S.6    Darst, S.A.7
  • 15
    • 0012837562 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA
    • E.A. Campbell, J.L. Tupy, T.M. Gruber, S. Wang, M.M. Sharp, C.A. Gross, and S.A. Darst Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA Mol. Cell 11 2003 1067 1078
    • (2003) Mol. Cell , vol.11 , pp. 1067-1078
    • Campbell, E.A.1    Tupy, J.L.2    Gruber, T.M.3    Wang, S.4    Sharp, M.M.5    Gross, C.A.6    Darst, S.A.7
  • 16
    • 0032190622 scopus 로고    scopus 로고
    • The flagellar anti-sigma factor FlgM actively dissociates Salmonella typhimurium sigma28 RNA polymerase holoenzyme
    • M.S. Chadsey, J.E. Karlinsey, and K.T. Hughes The flagellar anti-sigma factor FlgM actively dissociates Salmonella typhimurium sigma28 RNA polymerase holoenzyme Genes Dev. 12 1998 3123 3136
    • (1998) Genes Dev. , vol.12 , pp. 3123-3136
    • Chadsey, M.S.1    Karlinsey, J.E.2    Hughes, K.T.3
  • 17
    • 0001796834 scopus 로고
    • RNA polymerase - An overview
    • R. Losick M. Chamberlin Cold Spring Harbor Laboratory Cold Spring Harbor
    • M. Chamberlin RNA polymerase - an overview R. Losick M. Chamberlin RNA Polymerase 1976 Cold Spring Harbor Laboratory Cold Spring Harbor 17 68
    • (1976) RNA Polymerase , pp. 17-68
    • Chamberlin, M.1
  • 18
    • 1942535198 scopus 로고    scopus 로고
    • RNA polymerase II structure: From core to functional complexes
    • P. Cramer RNA polymerase II structure: from core to functional complexes Curr. Opin. Genet. Dev. 14 2004 218 226
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 218-226
    • Cramer, P.1
  • 19
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 Å resolution
    • P. Cramer, D. Bushnell, and R. Kornberg Structural basis of transcription: RNA polymerase II at 2.8 Å resolution Science 292 2001 1863 1876
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.2    Kornberg, R.3
  • 21
    • 0033587756 scopus 로고    scopus 로고
    • Interactions of Escherichia coli sigma(70) within the transcription elongation complex
    • S.S. Daube, and P.H. von Hippel Interactions of Escherichia coli sigma(70) within the transcription elongation complex Proc. Natl. Acad. Sci. USA 96 1999 8390 8395
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8390-8395
    • Daube, S.S.1    Von Hippel, P.H.2
  • 22
    • 0034737593 scopus 로고    scopus 로고
    • Single-molecule study of transcriptional pausing and arrest by E. coli RNA polymerase
    • R.J. Davenport, G.J. Wuite, R. Landick, and C. Bustamante Single-molecule study of transcriptional pausing and arrest by E. coli RNA polymerase Science 287 2000 2497 2500
    • (2000) Science , vol.287 , pp. 2497-2500
    • Davenport, R.J.1    Wuite, G.J.2    Landick, R.3    Bustamante, C.4
  • 23
    • 0025288050 scopus 로고
    • Abortive intermediates in transcription by wheat-germ RNA polymerase II. Dynamic aspects of enzyme/template interactions in selection of the enzyme synthetic mode
    • L. de Mercoyrol, J.M. Souhie, C. Job, D. Job, C. Dussert, J. Palmari, M. Rasigni, and G. Rasigni Abortive intermediates in transcription by wheat-germ RNA polymerase II. Dynamic aspects of enzyme/template interactions in selection of the enzyme synthetic mode Biochem. J. 269 1990 651 658
    • (1990) Biochem. J. , vol.269 , pp. 651-658
    • De Mercoyrol, L.1    Souhie, J.M.2    Job, C.3    Job, D.4    Dussert, C.5    Palmari, J.6    Rasigni, M.7    Rasigni, G.8
  • 25
    • 0025744584 scopus 로고
    • Escherichia coli sigma 70 and NusA proteins. I. Binding interactions with core RNA polymerase in solution and within the transcription complex
    • S.C. Gill, S.E. Weitzel, and P.H. von Hippel Escherichia coli sigma 70 and NusA proteins. I. Binding interactions with core RNA polymerase in solution and within the transcription complex J. Mol. Biol. 220 1991 307 324
    • (1991) J. Mol. Biol. , vol.220 , pp. 307-324
    • Gill, S.C.1    Weitzel, S.E.2    Von Hippel, P.H.3
  • 26
    • 0024815188 scopus 로고
    • Sequences required for antitermination by phage 82 Q protein
    • J.A. Goliger, and J.W. Roberts Sequences required for antitermination by phage 82 Q protein J. Mol. Biol. 210 1989 461 471
    • (1989) J. Mol. Biol. , vol.210 , pp. 461-471
    • Goliger, J.A.1    Roberts, J.W.2
  • 27
    • 14644407528 scopus 로고    scopus 로고
    • Thinking quantitatively about transcriptional regulation
    • S.J. Greive, and P.H. von Hippel Thinking quantitatively about transcriptional regulation Nat. Rev. Mol. Cell Biol. 6 2005 221 232
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 221-232
    • Greive, S.J.1    Von Hippel, P.H.2
  • 28
    • 0019216997 scopus 로고
    • Role of the sigma subunit of Escherichia coli RNA polymerase in initiation. II. Release of sigma from ternary complexes
    • U.M. Hansen, and W.R. McClure Role of the sigma subunit of Escherichia coli RNA polymerase in initiation. II. Release of sigma from ternary complexes J. Biol. Chem. 255 1980 9564 9570
    • (1980) J. Biol. Chem. , vol.255 , pp. 9564-9570
    • Hansen, U.M.1    McClure, W.R.2
  • 29
    • 0023918675 scopus 로고
    • Structure and function of bacterial sigma factors
    • J.D. Helmann, and M.J. Chamberlin Structure and function of bacterial sigma factors Annu. Rev. Biochem. 57 1988 839 872
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 839-872
    • Helmann, J.D.1    Chamberlin, M.J.2
  • 30
    • 24344447800 scopus 로고    scopus 로고
    • Immobilization of Escherichia coli RNA polymerase and location of binding sites by use of chromatin immunoprecipitation and microarrays
    • C.D. Herring, M. Raffaelle, T.E. Allen, E.I. Kanin, R. Landick, A.Z. Ansari, and B.O. Palsson Immobilization of Escherichia coli RNA polymerase and location of binding sites by use of chromatin immunoprecipitation and microarrays J. Bacteriol. 187 2005 6166 6174
    • (2005) J. Bacteriol. , vol.187 , pp. 6166-6174
    • Herring, C.D.1    Raffaelle, M.2    Allen, T.E.3    Kanin, E.I.4    Landick, R.5    Ansari, A.Z.6    Palsson, B.O.7
  • 32
    • 0033765113 scopus 로고    scopus 로고
    • Functional modulation of Escherichia coli RNA polymerase
    • A. Ishihama Functional modulation of Escherichia coli RNA polymerase Annu. Rev. Microbiol. 54 2000 499 518
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 499-518
    • Ishihama, A.1
  • 33
    • 0037093379 scopus 로고    scopus 로고
    • Regulation of sigma factor competition by the alarmone ppGpp
    • M. Jishage, K. Kvint, V. Shingler, and T. Nystrom Regulation of sigma factor competition by the alarmone ppGpp Genes Dev. 16 2002 1260 1270
    • (2002) Genes Dev. , vol.16 , pp. 1260-1270
    • Jishage, M.1    Kvint, K.2    Shingler, V.3    Nystrom, T.4
  • 34
    • 0032561131 scopus 로고    scopus 로고
    • Stopped-flow kinetic analysis of the interaction of Escherichia coli RNA polymerase with the bacteriophage T7 A1 promoter
    • R.S. Johnson, and R.E. Chester Stopped-flow kinetic analysis of the interaction of Escherichia coli RNA polymerase with the bacteriophage T7 A1 promoter J. Mol. Biol. 283 1998 353 370
    • (1998) J. Mol. Biol. , vol.283 , pp. 353-370
    • Johnson, R.S.1    Chester, R.E.2
  • 35
    • 0025968513 scopus 로고
    • Preparation and characterization of N-(1-pyrenyl)iodoacetamide-labeled Escherichia coli RNA polymerase
    • R.S. Johnson, M. Bowers, and Q. Eaton Preparation and characterization of N-(1-pyrenyl)iodoacetamide-labeled Escherichia coli RNA polymerase Biochemistry 30 1991 189 198
    • (1991) Biochemistry , vol.30 , pp. 189-198
    • Johnson, R.S.1    Bowers, M.2    Eaton, Q.3
  • 37
    • 0032532456 scopus 로고    scopus 로고
    • A surface of Escherichia coli sigma 70 required for promoter function and antitermination by phage lambda Q protein
    • D.C. Ko, M.T. Marr, J. Guo, and J.W. Roberts A surface of Escherichia coli sigma 70 required for promoter function and antitermination by phage lambda Q protein Genes Dev. 12 1998 3276 3285
    • (1998) Genes Dev. , vol.12 , pp. 3276-3285
    • Ko, D.C.1    Marr, M.T.2    Guo, J.3    Roberts, J.W.4
  • 41
    • 0033659766 scopus 로고    scopus 로고
    • Regulation of sigma factor activity during Bacillus subtilis development
    • L. Kroos, and Y.T. Yu Regulation of sigma factor activity during Bacillus subtilis development Curr. Opin. Microbiol. 3 2000 553 560
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 553-560
    • Kroos, L.1    Yu, Y.T.2
  • 42
    • 0024974056 scopus 로고
    • RNA chain initiation by Escherichia coli RNA polymerase. Structural transitions of the enzyme in early ternary complexes
    • B. Krummel, and M.J. Chamberlin RNA chain initiation by Escherichia coli RNA polymerase. Structural transitions of the enzyme in early ternary complexes Biochemistry 28 1989 7829 7842
    • (1989) Biochemistry , vol.28 , pp. 7829-7842
    • Krummel, B.1    Chamberlin, M.J.2
  • 43
    • 0026612797 scopus 로고
    • The sigma 70 family: Sequence conservation and evolutionary relationships
    • M. Lonetto, M. Gribskov, and C.A. Gross The sigma 70 family: sequence conservation and evolutionary relationships J. Bacteriol. 174 1992 3843 3849
    • (1992) J. Bacteriol. , vol.174 , pp. 3843-3849
    • Lonetto, M.1    Gribskov, M.2    Gross, C.A.3
  • 44
    • 0019442506 scopus 로고
    • Cascades of Sigma factors
    • R. Losick, and J. Pero Cascades of Sigma factors Cell 25 1981 582 584
    • (1981) Cell , vol.25 , pp. 582-584
    • Losick, R.1    Pero, J.2
  • 45
    • 0030271890 scopus 로고    scopus 로고
    • Crystal structure of a sigma 70 subunit fragment from E. coli RNA polymerase
    • A. Malhotra, E. Severinova, and S.A. Darst Crystal structure of a sigma 70 subunit fragment from E. coli RNA polymerase Cell 87 1996 127 136
    • (1996) Cell , vol.87 , pp. 127-136
    • Malhotra, A.1    Severinova, E.2    Darst, S.A.3
  • 46
    • 0035979245 scopus 로고    scopus 로고
    • Restructuring of an RNA polymerase holoenzyme elongation complex by lambdoid phage Q proteins
    • M.T. Marr, S.A. Datwyler, C.F. Meares, and J.W. Roberts Restructuring of an RNA polymerase holoenzyme elongation complex by lambdoid phage Q proteins Proc. Natl. Acad. Sci. USA 98 2001 8972 8978
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8972-8978
    • Marr, M.T.1    Datwyler, S.A.2    Meares, C.F.3    Roberts, J.W.4
  • 48
    • 0027236182 scopus 로고
    • Nucleation of RNA chain formation by Escherichia coli DNA-dependent RNA polymerase
    • W. Metzger, P. Schickor, T. Meier, W. Werel, and H. Heumann Nucleation of RNA chain formation by Escherichia coli DNA-dependent RNA polymerase J. Mol. Biol. 232 1993 35 49
    • (1993) J. Mol. Biol. , vol.232 , pp. 35-49
    • Metzger, W.1    Schickor, P.2    Meier, T.3    Werel, W.4    Heumann, H.5
  • 49
    • 0344011547 scopus 로고    scopus 로고
    • Tethering sigma70 to RNA polymerase reveals high in vivo activity of sigma factors and sigma70-dependent pausing at promoter-distal locations
    • R.A. Mooney, and R. Landick Tethering sigma70 to RNA polymerase reveals high in vivo activity of sigma factors and sigma70-dependent pausing at promoter-distal locations Genes Dev. 17 2003 2839 2851
    • (2003) Genes Dev. , vol.17 , pp. 2839-2851
    • Mooney, R.A.1    Landick, R.2
  • 50
    • 0035943446 scopus 로고    scopus 로고
    • Translocation of sigma(70) with RNA polymerase during transcription: Fluorescence resonance energy transfer assay for movement relative to DNA
    • J. Mukhopadhyay, A.N. Kapanidis, V. Mekler, E. Kortkhonjia, Y.W. Ebright, and R.H. Ebright Translocation of sigma(70) with RNA polymerase during transcription: fluorescence resonance energy transfer assay for movement relative to DNA Cell 106 2001 453 463
    • (2001) Cell , vol.106 , pp. 453-463
    • Mukhopadhyay, J.1    Kapanidis, A.N.2    Mekler, V.3    Kortkhonjia, E.4    Ebright, Y.W.5    Ebright, R.H.6
  • 52
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription Initiation: An RNA polymerase holoenzyme/DNA complex
    • K.S. Murakami, S. Masuda, E.A. 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.S.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.5
  • 53
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 a resolution
    • K.S. Murakami, S. Masuda, and S.A. Darst Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 A resolution Science 296 2002 1280 1284
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.S.1    Masuda, S.2    Darst, S.A.3
  • 54
    • 0036753065 scopus 로고    scopus 로고
    • The sigma(70) subunit of RNA polymerase is contacted by the (lambda)Q antiterminator during early elongation
    • B.E. Nickels, C.W. Roberts, H. Sun, J.W. Roberts, and A. Hochschild The sigma(70) subunit of RNA polymerase is contacted by the (lambda)Q antiterminator during early elongation Mol. Cell 10 2002 611 622
    • (2002) Mol. Cell , vol.10 , pp. 611-622
    • Nickels, B.E.1    Roberts, C.W.2    Sun, H.3    Roberts, J.W.4    Hochschild, A.5
  • 56
    • 15444366146 scopus 로고    scopus 로고
    • The interaction between sigma70 and the beta-flap of Escherichia coli RNA polymerase inhibits extension of nascent RNA during early elongation
    • B.E. Nickels, S.J. Garrity, V. Mekler, L. Minakhin, K. Severinov, R.H. Ebright, and A. Hochschild The interaction between sigma70 and the beta-flap of Escherichia coli RNA polymerase inhibits extension of nascent RNA during early elongation Proc. Natl. Acad. Sci. USA 102 2005 4488 4493
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4488-4493
    • Nickels, B.E.1    Garrity, S.J.2    Mekler, V.3    Minakhin, L.4    Severinov, K.5    Ebright, R.H.6    Hochschild, A.7
  • 58
    • 0036385743 scopus 로고    scopus 로고
    • Active Escherichia coli transcription elongation complexes are functionally homogeneous
    • Z. Pasman, and P.H. von Hippel Active Escherichia coli transcription elongation complexes are functionally homogeneous J. Mol. Biol. 322 2002 505 519
    • (2002) J. Mol. Biol. , vol.322 , pp. 505-519
    • Pasman, Z.1    Von Hippel, P.H.2
  • 59
    • 27644473223 scopus 로고    scopus 로고
    • Holoenzyme switching and stochastic release of sigma factors from RNA polymerase
    • M. Raffaelle, E. Kanin, J. Vogt, R. Burgess, and A. Ansari Holoenzyme switching and stochastic release of sigma factors from RNA polymerase Mol. Cell 20 2005 357 366 this issue
    • (2005) Mol. Cell , vol.20 , pp. 357-366
    • Raffaelle, M.1    Kanin, E.2    Vogt, J.3    Burgess, R.4    Ansari, A.5
  • 60
    • 0028230951 scopus 로고
    • Factor independent activation of rrnB P1. An "extended" promoter with an upstream element that dramatically increases promoter strength
    • L. Rao, W. Ross, J.A. Appleman, T. Gaal, S. Leirmo, P.J. Schlax, M.T. Record Jr., and R.L. Gourse Factor independent activation of rrnB P1. An "extended" promoter with an upstream element that dramatically increases promoter strength J. Mol. Biol. 235 1994 1421 1435
    • (1994) J. Mol. Biol. , vol.235 , pp. 1421-1435
    • Rao, L.1    Ross, W.2    Appleman, J.A.3    Gaal, T.4    Leirmo, S.5    Schlax, P.J.6    Record Jr., M.T.7    Gourse, R.L.8
  • 61
    • 0016302334 scopus 로고
    • Diffusion controlled reaction rates in spheroidal geometry. Application to repressor-operator association and membrane bound enzymes
    • P.H. Richter, and M. Eigen Diffusion controlled reaction rates in spheroidal geometry. Application to repressor-operator association and membrane bound enzymes Biophys. Chem. 2 1974 255 263
    • (1974) Biophys. Chem. , vol.2 , pp. 255-263
    • Richter, P.H.1    Eigen, M.2
  • 62
    • 0030576532 scopus 로고    scopus 로고
    • Function of E. coli RNA polymerase sigma factor sigma 70 in promoter-proximal pausing
    • B.Z. Ring, W.S. Yarnell, and J.W. Roberts Function of E. coli RNA polymerase sigma factor sigma 70 in promoter-proximal pausing Cell 86 1996 485 493
    • (1996) Cell , vol.86 , pp. 485-493
    • Ring, B.Z.1    Yarnell, W.S.2    Roberts, J.W.3
  • 63
    • 0023029081 scopus 로고
    • Release of the sigma subunit of Escherichia coli DNA-dependent RNA polymerase depends mainly on time elapsed after the start of initiation, not on length of product RNA
    • N. Shimamoto, T. Kamigochi, and H. Utiyama Release of the sigma subunit of Escherichia coli DNA-dependent RNA polymerase depends mainly on time elapsed after the start of initiation, not on length of product RNA J. Biol. Chem. 261 1986 11859 11865
    • (1986) J. Biol. Chem. , vol.261 , pp. 11859-11865
    • Shimamoto, N.1    Kamigochi, T.2    Utiyama, H.3
  • 64
    • 0032113494 scopus 로고    scopus 로고
    • Crucial role of the RNA:DNA hybrid in the processivity of transcription
    • I. Sidorenkov, N. Komissarova, and M. Kashlev Crucial role of the RNA:DNA hybrid in the processivity of transcription Mol. Cell 2 1998 55 64
    • (1998) Mol. Cell , vol.2 , pp. 55-64
    • Sidorenkov, I.1    Komissarova, N.2    Kashlev, M.3
  • 65
    • 5444225805 scopus 로고    scopus 로고
    • Elongation by RNA polymerase II: The short and long of it
    • R.J. Sims 3rd, R. Belotserkovskaya, and D. Reinberg Elongation by RNA polymerase II: the short and long of it Genes Dev. 18 2004 2437 2468
    • (2004) Genes Dev. , vol.18 , pp. 2437-2468
    • Sims III, R.J.1    Belotserkovskaya, R.2    Reinberg, D.3
  • 66
    • 1842766125 scopus 로고    scopus 로고
    • Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation
    • M.K. Sorenson, S.S. Ray, and S.A. Darst Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation Mol. Cell 14 2004 127 138
    • (2004) Mol. Cell , vol.14 , pp. 127-138
    • Sorenson, M.K.1    Ray, S.S.2    Darst, S.A.3
  • 67
    • 0025132506 scopus 로고
    • Cascades of sigma factors revisited
    • P. Stragier, and R. Losick Cascades of sigma factors revisited Mol. Microbiol. 4 1990 1801 1806
    • (1990) Mol. Microbiol. , vol.4 , pp. 1801-1806
    • Stragier, P.1    Losick, R.2
  • 68
    • 0022401520 scopus 로고
    • Intermediates in transcription initiation from the E. coli lac UV5 promoter
    • D.C. Straney, and D.M. Crothers Intermediates in transcription initiation from the E. coli lac UV5 promoter Cell 43 1985 449 459
    • (1985) Cell , vol.43 , pp. 449-459
    • Straney, D.C.1    Crothers, D.M.2
  • 69
    • 0023102647 scopus 로고
    • A stressed intermediate in the formation of stably initiated RNA chains at the Escherichia coli lac UV5 promoter
    • D.C. Straney, and D.M. Crothers A stressed intermediate in the formation of stably initiated RNA chains at the Escherichia coli lac UV5 promoter J. Mol. Biol. 193 1987 267 278
    • (1987) J. Mol. Biol. , vol.193 , pp. 267-278
    • Straney, D.C.1    Crothers, D.M.2
  • 70
    • 1542328272 scopus 로고    scopus 로고
    • The RNA polymerase II transcription cycle: Cycling through chromatin
    • J.Q. Svejstrup The RNA polymerase II transcription cycle: cycling through chromatin Biochim. Biophys. Acta 1677 2004 64 73
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 64-73
    • Svejstrup, J.Q.1
  • 71
    • 0024564062 scopus 로고
    • Sequences linked to prokaryotic promoters can affect the efficiency of downstream termination sites
    • A.P.W. Telesnitsky, and M.J. Chamberlin Sequences linked to prokaryotic promoters can affect the efficiency of downstream termination sites J. Mol. Biol. 205 1989 315 330
    • (1989) J. Mol. Biol. , vol.205 , pp. 315-330
    • Telesnitsky, A.P.W.1    Chamberlin, M.J.2
  • 72
    • 19244382579 scopus 로고    scopus 로고
    • Diversity in the rates of transcript elongation by single RNA polymerase molecules
    • S. Toli-Nørrelykke, A. Engh, R. Landick, and J. Gelles Diversity in the rates of transcript elongation by single RNA polymerase molecules J. Biol. Chem. 279 2004 3292 3299
    • (2004) J. Biol. Chem. , vol.279 , pp. 3292-3299
    • Toli-Nørrelykke, S.1    Engh, A.2    Landick, R.3    Gelles, J.4
  • 73
    • 1342325469 scopus 로고    scopus 로고
    • In vivo effect of NusB and NusG on rRNA transcription antitermination
    • M. Torres, J.M. Balada, M. Zellars, C. Squires, and C.L. Squires In vivo effect of NusB and NusG on rRNA transcription antitermination J. Bacteriol. 186 2004 1304 1310
    • (2004) J. Bacteriol. , vol.186 , pp. 1304-1310
    • Torres, M.1    Balada, J.M.2    Zellars, M.3    Squires, C.4    Squires, C.L.5
  • 74
    • 0035957687 scopus 로고    scopus 로고
    • Allosteric control of RNA polymerase by a site that contacts nascent RNA hairpins
    • I. Toulokhonov, I. Artsimovitch, and R. Landick Allosteric control of RNA polymerase by a site that contacts nascent RNA hairpins Science 292 2001 730 733
    • (2001) Science , vol.292 , pp. 730-733
    • Toulokhonov, I.1    Artsimovitch, I.2    Landick, R.3
  • 75
    • 0014669901 scopus 로고
    • Cyclic re-use of the RNA polymerase sigma factor
    • A.A. Travers, and R.R. Burgess Cyclic re-use of the RNA polymerase sigma factor Nature 222 1969 537 540
    • (1969) Nature , vol.222 , pp. 537-540
    • Travers, A.A.1    Burgess, R.R.2
  • 76
    • 0033619725 scopus 로고    scopus 로고
    • Targeted protein footprinting: Where different transcription factors bind to RNA polymerase
    • S.L. Traviglia, S.A. Datwyler, D. Yan, A. Ishihama, and C.F. Meares Targeted protein footprinting: where different transcription factors bind to RNA polymerase Biochemistry 38 1999 15774 15778
    • (1999) Biochemistry , vol.38 , pp. 15774-15778
    • Traviglia, S.L.1    Datwyler, S.A.2    Yan, D.3    Ishihama, A.4    Meares, C.F.5
  • 78
    • 0028227702 scopus 로고
    • The RNA chain elongation rate in Escherichia coli depends on the growth rate
    • U. Vogel, and K.F. Jensen The RNA chain elongation rate in Escherichia coli depends on the growth rate J. Bacteriol. 176 1994 2807 2813
    • (1994) J. Bacteriol. , vol.176 , pp. 2807-2813
    • Vogel, U.1    Jensen, K.F.2
  • 79
    • 11144228250 scopus 로고    scopus 로고
    • Association of RNA polymerase with transcribed regions in Escherichia coli
    • J.T. Wade, and K. Struhl Association of RNA polymerase with transcribed regions in Escherichia coli Proc. Natl. Acad. Sci. USA 101 2004 17777 17782
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17777-17782
    • Wade, J.T.1    Struhl, K.2
  • 80
    • 0032901203 scopus 로고    scopus 로고
    • Processive antitermination
    • R. Weisberg, and M. Gottesman Processive antitermination J. Bacteriol. 181 1999 359 367
    • (1999) J. Bacteriol. , vol.181 , pp. 359-367
    • Weisberg, R.1    Gottesman, M.2
  • 81
    • 0026663397 scopus 로고
    • The phage l gene Q transcription antiterminator binds DNA in the late gene promoter as it modifies RNA polymerase
    • W.S. Yarnell, and J.W. Roberts The phage l gene Q transcription antiterminator binds DNA in the late gene promoter as it modifies RNA polymerase Cell 69 1992 1181 1189
    • (1992) Cell , vol.69 , pp. 1181-1189
    • Yarnell, W.S.1    Roberts, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.