메뉴 건너뛰기




Volumn 405, Issue 1, 2011, Pages 49-64

Interaction surface of the transcription terminator rho required to form a complex with the C-terminal domain of the antiterminator NusG

Author keywords

NusG; Rho; RNA polymerase; transcription termination

Indexed keywords

NUSG; RNA POLYMERASE; TRANSCRIPTION ELONGATION FACTOR; TRANSCRIPTION TERMINATION FACTOR RHO; UNCLASSIFIED DRUG;

EID: 78650418915     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.10.044     Document Type: Article
Times cited : (40)

References (29)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 0023666140 scopus 로고
    • Transcription termination factor Rho is an RNA:DNA helicase
    • Brenan C.A., Dombrowski 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
    • Brenan, C.A.1    Dombrowski, A.J.2    Platt, T.3
  • 4
    • 50649101517 scopus 로고    scopus 로고
    • Transcription termination factor Rho prefers catalytically active elongation complex for releasing RNA
    • Dutta D., Chalissery J., and Sen R. Transcription termination factor Rho prefers catalytically active elongation complex for releasing RNA J. Biol. Chem 283 2008 20243 20251
    • (2008) J. Biol. Chem , vol.283 , pp. 20243-20251
    • Dutta, D.1    Chalissery, J.2    Sen, R.3
  • 5
    • 74549191169 scopus 로고    scopus 로고
    • An allosteric mechanism of Rho-dependent transcription termination
    • Epshtein V., Dutta D., Wade J., and Evgeny N. An allosteric mechanism of Rho-dependent transcription termination Nature 463 2010 245 249
    • (2010) Nature , vol.463 , pp. 245-249
    • Epshtein, V.1    Dutta, D.2    Wade, J.3    Evgeny, N.4
  • 6
    • 0026527997 scopus 로고
    • Requirement for E. coli NusG protein in factor-dependent transcription termination
    • Sullivan S.L., and Gottesman M.E. Requirement for E. coli NusG protein in factor-dependent transcription termination Cell 68 1992 989 995
    • (1992) Cell , vol.68 , pp. 989-995
    • Sullivan, S.L.1    Gottesman, M.E.2
  • 8
    • 0028905513 scopus 로고
    • Escherichia coli NusG protein stimulates transcription elongation rates in vivo and in vitro
    • Burova E., Hung S.C., Sagitov V., Stitt B.L., and Gottesman M.E. Escherichia coli NusG protein stimulates transcription elongation rates in vivo and in vitro J. Bacteriol. 177 1995 1388 1392
    • (1995) J. Bacteriol. , vol.177 , pp. 1388-1392
    • Burova, E.1    Hung, S.C.2    Sagitov, V.3    Stitt, B.L.4    Gottesman, M.E.5
  • 9
    • 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
  • 10
    • 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., and 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 2007 855 872
    • (2007) J. Mol. Biol. , vol.371 , pp. 855-872
    • Chalissery, J.1    Banerjee, S.2    Bandey, I.3    Sen, R.4
  • 12
    • 12044255564 scopus 로고
    • Elongation factor NusG interacts with termination factor rho to regulate termination and antitermination of transcription
    • Li J., Mason S.W., and Greenblatt J. Elongation factor NusG interacts with termination factor rho to regulate termination and antitermination of transcription Genes Dev. 7 1993 161 172
    • (1993) Genes Dev. , vol.7 , pp. 161-172
    • Li, J.1    Mason, S.W.2    Greenblatt, J.3
  • 13
    • 0034625124 scopus 로고    scopus 로고
    • Regulation of rho-dependent transcription termination by NusG is specific to the Escherichia coli elongation complex
    • Passman Z., and vonHippel P.H. Regulation of rho-dependent transcription termination by NusG is specific to the Escherichia coli elongation complex Biochemistry 39 2000 5573 5585
    • (2000) Biochemistry , vol.39 , pp. 5573-5585
    • Passman, Z.1    Vonhippel, P.H.2
  • 14
    • 0242515770 scopus 로고    scopus 로고
    • A spring-loaded state of NusG in its functional cycle is suggested by X-ray crystallography and supported by site-directed mutants
    • Knowlton J.R., Bubunenko M., Andrykovitch M., Guo W., Routzahn K.M., and Waugh D.S. A spring-loaded state of NusG in its functional cycle is suggested by X-ray crystallography and supported by site-directed mutants Biochemistry 42 2003 2275 2281
    • (2003) Biochemistry , vol.42 , pp. 2275-2281
    • Knowlton, J.R.1    Bubunenko, M.2    Andrykovitch, M.3    Guo, W.4    Routzahn, K.M.5    Waugh, D.S.6
  • 15
    • 0037009445 scopus 로고    scopus 로고
    • Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities
    • Steiner T., Kaiser J.T., Marinkovic S., Huber R., and Wahl M.C. Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities EMBO J. 21 2002 4641 4653
    • (2002) EMBO J. , vol.21 , pp. 4641-4653
    • Steiner, T.1    Kaiser, J.T.2    Marinkovic, S.3    Huber, R.4    Wahl, M.C.5
  • 16
    • 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., Rosch P., Gottesman M., and Landick R. Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators J. Mol. Biol. 391 2009 341 358
    • (2009) J. Mol. Biol. , vol.391 , pp. 341-358
    • Mooney, R.A.1    Schweimer, K.2    Rosch, P.3    Gottesman, M.4    Landick, R.5
  • 17
    • 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
  • 18
    • 65849200100 scopus 로고    scopus 로고
    • Interaction surface of bacteriophage P4 protein psu required for complex formation with the transcription terminator Rho
    • Pani B., Ranjan A., and Sen R. Interaction surface of bacteriophage P4 protein psu required for complex formation with the transcription terminator Rho J. Mol. Biol. 389 2009 647 660
    • (2009) J. Mol. Biol. , vol.389 , pp. 647-660
    • Pani, B.1    Ranjan, A.2    Sen, R.3
  • 19
    • 23944518352 scopus 로고    scopus 로고
    • E. coli RNA polymerase mutations impaired for H19B N specific transcription antitermination are located close to the upstream edge of RNA:DNA hybrid and beginning of RNA exit channel of elongation complex
    • Cheeran A., Suganthan R., Swapna G., Bandey I., Acharya S., Nagarajaram H.A., and Sen R. E. coli RNA polymerase mutations impaired for H19B N specific transcription antitermination are located close to the upstream edge of RNA:DNA hybrid and beginning of RNA exit channel of elongation complex J. Mol. Biol. 252 2005 28 43
    • (2005) J. Mol. Biol. , vol.252 , pp. 28-43
    • Cheeran, A.1    Suganthan, R.2    Swapna, G.3    Bandey, I.4    Acharya, S.5    Nagarajaram, H.A.6    Sen, R.7
  • 20
    • 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., Ramya M.L., 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    Ramya, M.L.5    Suganthan, R.6    Sen, R.7
  • 21
    • 20444410362 scopus 로고    scopus 로고
    • Identification of a structural element that is essential for two functions of transcription factor NusG
    • Richardson L.V., and Richardson J.P. Identification of a structural element that is essential for two functions of transcription factor NusG Biochim. Biophys. Acta 1729 2005 135 140
    • (2005) Biochim. Biophys. Acta , vol.1729 , pp. 135-140
    • Richardson, L.V.1    Richardson, J.P.2
  • 22
    • 0027749638 scopus 로고
    • NusG alters rho-dependent termination of transcription in vitro independent of kinetic coupling
    • Nehrke K.W., Zalatan F., and Platt T. NusG alters rho-dependent termination of transcription in vitro independent of kinetic coupling Gene Expression 3 1993 119 133
    • (1993) Gene Expression , vol.3 , pp. 119-133
    • Nehrke, K.W.1    Zalatan, F.2    Platt, T.3
  • 23
    • 0034691146 scopus 로고    scopus 로고
    • Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals
    • Artsimovitch I., and Landick R. Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals Proc. Natl Acad. Sci. USA 97 2000 7090 7095
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 7090-7095
    • Artsimovitch, I.1    Landick, R.2
  • 24
    • 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
  • 25
    • 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
  • 29
    • 13444283630 scopus 로고    scopus 로고
    • Interaction network containing conserved and essential protein complexes in Escherichia coli
    • Butland G., Peregrín-Alvarez J.M., Li J., Yang W., Yang X., and Canadien V. Interaction network containing conserved and essential protein complexes in Escherichia coli Nature 433 2005 531 537
    • (2005) Nature , vol.433 , pp. 531-537
    • Butland, G.1    Peregrín-Alvarez, J.M.2    Li, J.3    Yang, W.4    Yang, X.5    Canadien, V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.