메뉴 건너뛰기




Volumn 463, Issue 7278, 2010, Pages 245-249

An allosteric mechanism of Rho-dependent transcription termination

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR; RHO FACTOR; RNA POLYMERASE;

EID: 74549191169     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08669     Document Type: Article
Times cited : (149)

References (34)
  • 1
    • 0017868340 scopus 로고
    • Control of transcription termination
    • Adhya, S. & Gottesman, M. Control of transcription termination. Annu. Rev. Biochem. 47, 967-996 (1978).
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 967-996
    • Adhya, S.1    Gottesman, M.2
  • 2
    • 0026035521 scopus 로고
    • Preventing the synthesis of unused transcripts by Rho factor
    • Richardson, J. P. Preventing the synthesis of unused transcripts by Rho factor. Cell 64, 1047-1049 (1991).
    • (1991) Cell , vol.64 , pp. 1047-1049
    • Richardson, J.P.1
  • 3
    • 44249091644 scopus 로고    scopus 로고
    • Termination factor Rho and its cofactors NusA and NusG silence foreign DNA in E. coli
    • Cardinale, C. J. et al. Termination factor Rho and its cofactors NusA and NusG silence foreign DNA in E. coli. Science 320, 935-938 (2008).
    • (2008) Science , vol.320 , pp. 935-938
    • Cardinale, C.J.1
  • 4
    • 0014685875 scopus 로고
    • Termination factor for RNA synthesis
    • Roberts, J. W. Termination factor for RNA synthesis. Nature224, 1168-1174 (1969).
    • (1969) Nature , vol.224 , pp. 1168-1174
    • Roberts, J.W.1
  • 5
    • 0026526765 scopus 로고
    • Physical properties of the Escherichia coli transcription termination factor Rho. 1. Association states and geometry of the Rho hexamer
    • Geiselmann, J., Yager, T. D., Gill, S. C., Calmettes, P. & von Hippel, P. H. Physical properties of the Escherichia coli transcription termination factor Rho. 1. Association states and geometry of the Rho hexamer. Biochemistry 31, 111-121 (1992).
    • (1992) Biochemistry , vol.31 , pp. 111-121
    • Geiselmann, J.1    Yager, T.D.2    Gill, S.C.3    Calmettes, P.4    Von Hippel, P.H.5
  • 6
    • 17144418445 scopus 로고    scopus 로고
    • Catalytic cooperativity among subunits of Escherichia coli transcription termination factor Rho. Kinetics and substrate structural requirements
    • Browne, R. J., Barr, E. W. & Stitt, B. L. Catalytic cooperativity among subunits of Escherichia coli transcription termination factor Rho. Kinetics and substrate structural requirements. J. Biol. Chem. 280, 13292-13299 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 13292-13299
    • Browne, R.J.1    Barr, E.W.2    Stitt, B.L.3
  • 7
    • 33750477997 scopus 로고    scopus 로고
    • Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor
    • Skordalakes, E. & Berger, J. M. Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor. Cell 127, 553-564 (2006).
    • (2006) Cell , vol.127 , pp. 553-564
    • Skordalakes, E.1    Berger, J.M.2
  • 8
    • 33744529571 scopus 로고    scopus 로고
    • Mechanochemistry of transcription termination factor Rho
    • Adelman, J. L. et al. Mechanochemistry of transcription termination factor Rho. Mol. Cell 22, 611-621 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 611-621
    • Adelman, J.L.1
  • 9
    • 33646849728 scopus 로고    scopus 로고
    • Rho-dependent transcription termination: More questions than answers
    • Banerjee, S., Chalissery, J., Bandey, I. & Sen, R. Rho-dependent transcription termination: more questions than answers. J. Microbiol. 44, 11-22 (2006).
    • (2006) J. Microbiol. , vol.44 , pp. 11-22
    • Banerjee, S.1    Chalissery, J.2    Bandey, I.3    Sen, R.4
  • 10
    • 0028223611 scopus 로고
    • Rho and RNA: Models for recognition and response
    • Platt, T. Rho and RNA: models for recognition and response. Mol. Microbiol. 11, 983-990 (1994).
    • (1994) Mol. Microbiol. , vol.11 , pp. 983-990
    • Platt, T.1
  • 11
    • 0035957998 scopus 로고    scopus 로고
    • The kinetic pathway of RNA binding to the Escherichia coli transcription termination factor Rho
    • Kim, D. E. & Patel, S. S. The kinetic pathway of RNA binding to the Escherichia coli transcription termination factor Rho. J. Biol. Chem. 276, 13902-13910 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 13902-13910
    • Kim, D.E.1    Patel, S.S.2
  • 13
    • 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. & Gross, C. A. Termination efficiency at Rho-dependent terminators depends on kinetic coupling between RNA polymerase and Rho. Proc. Natl Acad. Sci. USA 89, 1453-1457 (1992).
    • (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
  • 14
    • 0032508387 scopus 로고    scopus 로고
    • Rho-dependent termination within the trp t9 terminator. II. Effects of kinetic competition and rho processivity
    • Zhu, A. Q. & von Hippel, P. H. Rho-dependent termination within the trp t9 terminator. II. Effects of kinetic competition and rho processivity. Biochemistry 37, 11215-11222 (1998).
    • (1998) Biochemistry , vol.37 , pp. 11215-11222
    • Zhu, A.Q.1    Von Hippel, P.H.2
  • 15
    • 0032213250 scopus 로고    scopus 로고
    • A simple polypyrimidine repeat acts as an artificial rho-dependent terminator in vivo and in vitro
    • Guerin, M., Robichon, N., Geiselmann, J. & Rahmouni, A. R. A simple polypyrimidine repeat acts as an artificial rho-dependent terminator in vivo and in vitro. Nucleic Acids Res. 26, 4895-4900 (1998).
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4895-4900
    • Guerin, M.1    Robichon, N.2    Geiselmann, J.3    Rahmouni, A.R.4
  • 16
    • 34548667500 scopus 로고    scopus 로고
    • Transcription termination defective mutants of Rho: Role of different functions of Rho in releasing RNA from the elongation complex
    • Chalissery, J., Banerjee, S., Bandey, I. & Sen, R. Transcription termination defective mutants of Rho: role of different functions of Rho in releasing RNA from the elongation complex. J. Mol. Biol. 371, 855-872 (2007).
    • (2007) J. Mol. Biol. , vol.371 , pp. 855-872
    • Chalissery, J.1    Banerjee, S.2    Bandey, I.3    Sen, R.4
  • 17
    • 12944324227 scopus 로고    scopus 로고
    • A ratchet mechanism of transcription elongation and its control
    • Bar-Nahum, G., Epshtein, V., Ruckenstein, A. E., Mustaev, A. & Nudler, E. A ratchet mechanism of transcription elongation and its control. Cell 120, 183-193 (2005).
    • (2005) Cell , vol.120 , pp. 183-193
    • Bar-Nahum, G.1    Epshtein, V.2    Ruckenstein, A.E.3    Mustaev, A.4    Nudler, E.5
  • 18
    • 28544453415 scopus 로고    scopus 로고
    • Structural basis for transcription inhibition by tagetitoxin
    • Vassylyev, D. G. at al. Structural basis for transcription inhibition by tagetitoxin. Nature Struct. Mol. Biol. 12, 1086-1093 (2005).
    • (2005) Nature Struct. Mol. Biol. , vol.12 , pp. 1086-1093
    • Vassylyev, D.G.1
  • 19
    • 0034613030 scopus 로고    scopus 로고
    • Characterization of halted T7 RNA polymerase elongation complexes reveals multiple factors that contribute to stability
    • Mentesana, P. E., Chin-Bow, S. T., Sousa, R. & McAllister, W. T. Characterization of halted T7 RNA polymerase elongation complexes reveals multiple factors that contribute to stability. J. Mol. Biol. 302, 1049-1062 (2000).
    • (2000) J. Mol. Biol. , vol.302 , pp. 1049-1062
    • Mentesana, P.E.1    Chin-Bow, S.T.2    Sousa, R.3    McAllister, W.T.4
  • 20
    • 10944232674 scopus 로고    scopus 로고
    • Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
    • Kettenberger, H., Armache, K. J. & Cramer, P. Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Mol. Cell 16, 955-965 (2004).
    • (2004) Mol. Cell , vol.16 , pp. 955-965
    • Kettenberger, H.1    Armache, K.J.2    Cramer, P.3
  • 21
    • 33751235874 scopus 로고    scopus 로고
    • Structural basis of transcription: Role of the trigger loop in substrate specificity and catalysis
    • Wang, D., Bushnell, D. A., Westover, K. D., Kaplan, C. D. & Kornberg, R. D. Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis. Cell 127, 941-954 (2006).
    • (2006) Cell , vol.127 , pp. 941-954
    • Wang, D.1    Bushnell, D.A.2    Westover, K.D.3    Kaplan, C.D.4    Kornberg, R.D.5
  • 23
    • 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. & Landick, R. A central role of the RNA polymerase trigger loop in active-site rearrangement during transcriptional pausing. Mol. Cell 27, 406-419 (2007).
    • (2007) Mol. Cell , vol.27 , pp. 406-419
    • Toulokhonov, I.1    Zhang, J.2    Palangat, M.3    Landick, R.4
  • 24
    • 0023666140 scopus 로고
    • Transcription termination factor rho is an RNA-DNA helicase
    • Brennan, C. A., Dombroski, A. J. & Platt, T. Transcription termination factor rho is an RNA-DNA helicase. Cell 48, 945-952 (1987).
    • (1987) Cell , vol.48 , pp. 945-952
    • Brennan, C.A.1    Dombroski, A.J.2    Platt, T.3
  • 25
    • 35748950148 scopus 로고    scopus 로고
    • Transcription termination factor rho can displace streptavidin from biotinylated RNA
    • Schwartz, A., Margeat, E., Rahmouni, A. R. & Boudvillain, M. Transcription termination factor rho can displace streptavidin from biotinylated RNA. J. Biol. Chem. 282, 1469-1476 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 1469-1476
    • Schwartz, A.1    Margeat, E.2    Rahmouni, A.R.3    Boudvillain, M.4
  • 26
    • 0033120034 scopus 로고    scopus 로고
    • The mechanism of intrinsic transcription termination
    • Gusarov, I. & Nudler, E. The mechanism of intrinsic transcription termination. Mol. Cell 3, 495-504 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 495-504
    • Gusarov, I.1    Nudler, E.2
  • 27
    • 0036863659 scopus 로고    scopus 로고
    • Shortening of RNA:DNA hybrid in the elongation complex of RNA polymerase is a prerequisite for transcription termination
    • Komissarova, N., Becker, J., Solter, S., Kireeva, M. & Kashlev, M. Shortening of RNA:DNA hybrid in the elongation complex of RNA polymerase is a prerequisite for transcription termination. Mol. Cell 10, 1151-1162 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 1151-1162
    • Komissarova, N.1    Becker, J.2    Solter, S.3    Kireeva, M.4    Kashlev, M.5
  • 29
    • 1142310578 scopus 로고    scopus 로고
    • Structural basis of transcription: Separation of RNA from DNA by RNA polymerase II
    • Westover, K. D., Bushnell, D. A. & Kornberg, R. D. Structural basis of transcription: separation of RNA from DNA by RNA polymerase II. Science 303, 1014-1016 (2004).
    • (2004) Science , vol.303 , pp. 1014-1016
    • Westover, K.D.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 30
    • 33746827367 scopus 로고    scopus 로고
    • The role of the largest RNA polymerase subunit lid element in preventing the formation of extended RNA-DNA hybrid
    • Naryshkina, T., Kuznedelov, K. & Severinov, K. The role of the largest RNA polymerase subunit lid element in preventing the formation of extended RNA-DNA hybrid. J. Mol. Biol. 361, 634-643 (2006).
    • (2006) J. Mol. Biol. , vol.361 , pp. 634-643
    • Naryshkina, T.1    Kuznedelov, K.2    Severinov, K.3
  • 31
    • 0345884910 scopus 로고    scopus 로고
    • Methods of walking with the RNA polymerase
    • Nudler, E., Gusarov, I. & Bar-Nahum, G. Methods of walking with the RNA polymerase. Methods Enzymol. 371, 160-169 (2003).
    • (2003) Methods Enzymol. , vol.371 , pp. 160-169
    • Nudler, E.1    Gusarov, I.2    Bar-Nahum, G.3
  • 32
    • 0024359479 scopus 로고
    • The negative charge of Glu-111 is required to activate the cleavage center of EcoRI endonuclease
    • Wright, D. J., King, K. & Modrich, P. The negative charge of Glu-111 is required to activate the cleavage center of EcoRI endonuclease. J. Biol. Chem. 264, 11816-11821 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 11816-11821
    • Wright, D.J.1    King, K.2    Modrich, P.3
  • 33
    • 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
  • 34
    • 0032541021 scopus 로고    scopus 로고
    • Spatial organization of transcription elongation complex in Escherichia coli
    • Nudler, E., Gusarov, I., Avetissova, E., Kozlov, M. & Goldfarb, A. Spatial organization of transcription elongation complex in Escherichia coli. Science 281, 424-428 (1998).
    • (1998) Science , vol.281 , pp. 424-428
    • Nudler, E.1    Gusarov, I.2    Avetissova, E.3    Kozlov, M.4    Goldfarb, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.