메뉴 건너뛰기




Volumn 587, Issue , 2010, Pages 137-154

Simple enzymatic assays for the in vitro motor activity of transcription termination factor rho from escherichia coli

Author keywords

helicase; hexamer; molecular motor; Rho; ring shaped; termination; transcription

Indexed keywords

ESCHERICHIA COLI;

EID: 77953012026     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-60327-355-8_10     Document Type: Article
Times cited : (18)

References (20)
  • 1
    • 0014685875 scopus 로고
    • Termination factor for RNA synthesis
    • Roberts J. W. (1969) Termination factor for RNA synthesis. Nature 224, 1168-1174.
    • (1969) Nature , vol.224 , pp. 1168-1174
    • Roberts, J.W.1
  • 2
    • 33748767376 scopus 로고    scopus 로고
    • Rho-dependent terminators and transcription termination
    • DOI 10.1099/mic.0.28982-0
    • Ciampi M. S. (2006) Rho-dependent terminators and transcription termination. Microbiology 152, 2515-2528. (Pubitemid 44405077)
    • (2006) Microbiology , vol.152 , Issue.9 , pp. 2515-2528
    • Ciampi, M.S.1
  • 3
    • 0037073063 scopus 로고    scopus 로고
    • Rho-dependent termination and ATPases in transcript termination
    • Richardson J. P. (2002) Rho-dependent termination and ATPases in transcript termination. Biochim. Biophys. Acta. 1577, 251-2560.
    • (2002) Biochim. Biophys. Acta. , vol.1577 , pp. 251-2560
    • Richardson, J.P.1
  • 4
    • 0037559627 scopus 로고    scopus 로고
    • Structure of the Rho transcription terminator: Mechanism of mRNA recognition and helicase loading
    • DOI 10.1016/S0092-8674(03)00512-9
    • Skordalakes E. and Berger J. M. (2003) Structure of the rho transcription terminator. Mechanism of mRNA recognition and helicase loading. Cell 114, 135-146. (Pubitemid 36869001)
    • (2003) Cell , vol.114 , Issue.1 , pp. 135-146
    • Skordalakes, E.1    Berger, J.M.2
  • 5
    • 33750477997 scopus 로고    scopus 로고
    • Structural Insights into RNA-Dependent Ring Closure and ATPase Activation by the Rho Termination Factor
    • DOI 10.1016/j.cell.2006.08.051, PII S0092867406012797
    • Skordalakes E. and Berger J. M. (2006) Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor. Cell 127, 553-564. (Pubitemid 44647425)
    • (2006) Cell , vol.127 , Issue.3 , pp. 553-564
    • Skordalakes, E.1    Berger, J.M.2
  • 6
    • 0011101816 scopus 로고
    • An RNA-dependent nucleoside triphosphate phosphohydrolase (ATPase) associated with rho termination factor
    • Lowery-Goldhammer C. and Richardson J. P. (1974) An RNA-dependent nucleoside triphosphate phosphohydrolase (ATPase) associated with rho termination factor. Proc. Natl. Acad. Sci. USA 71, 2003-2007.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 2003-2007
    • Lowery-Goldhammer, C.1    Richardson, J.P.2
  • 7
    • 0023666140 scopus 로고
    • Transcription termination factor rho is an RNA-DNA helicase
    • Brennan C. A., Dombroski A. J., and Platt T. (1987) Transcription termination factor rho is an RNA-DNA helicase. Cell 48, 945-952.
    • (1987) Cell , vol.48 , pp. 945-952
    • Brennan, C.A.1    Dombroski, A.J.2    Platt, T.3
  • 8
    • 0032213250 scopus 로고    scopus 로고
    • A simple polypyrimidine repeat acts as an artificial Rho-dependent terminator in vivo and in vitro
    • DOI 10.1093/nar/26.21.4895
    • Guerin M., Robichon N., Geiselmann J., and Rahmouni A. R. (1998) A simple polypyrimidine repeat acts as an artificial Rhodependent terminator in vivo and in vitro. Nucleic Acids Res. 26, 4895-4900. (Pubitemid 28491167)
    • (1998) Nucleic Acids Research , vol.26 , Issue.21 , pp. 4895-4900
    • Guerin, M.1    Robichon, N.2    Geiselmann, J.3    Rahmouni, A.R.4
  • 9
    • 0020490675 scopus 로고
    • Activation of rho protein ATPase requires simultaneous interaction at two kinds of nucleic acid-binding sites
    • Richardson J. P. (1982) Activation of rho protein ATPase requires simultaneous interaction at two kinds of nucleic acid-binding sites. J. Biol. Chem. 257, 5760-5766.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5760-5766
    • Richardson, J.P.1
  • 10
    • 0027274614 scopus 로고
    • Deletion analysis of the Escherichia coli rho-dependent transcription terminator trp t'
    • Zalatan F., Galloway-Salvo J., and Platt T. (1993) Deletion analysis of the Escherichia coli rho-dependent transcription terminator trp t0. J. Biol. Chem. 268, 17051-17056. (Pubitemid 23236932)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.23 , pp. 17051-17056
    • Zalatan, F.1    Galloway-Salvo, J.2    Platt, T.3
  • 11
    • 0023655931 scopus 로고
    • Sequence elements essential for rho-dependent transcription termination at lambda tR1
    • Chen C. Y. and Richardson J. P. (1987) Sequence elements essential for rho-dependent transcription termination at lambda tR1. J. Biol. Chem. 262, 11292-11299.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11292-11299
    • Chen, C.Y.1    Richardson, J.P.2
  • 12
    • 0033120903 scopus 로고    scopus 로고
    • The structural basis for terminator recognition by the Rho transcription termination factor
    • DOI 10.1016/S1097-2765(00)80476-1
    • Bogden C. E., Fass D., Bergman N., Nichols M. D., and Berger J. M. (1999) The structural basis for terminator recognition by the Rho transcription termination factor. Mol. Cell 3, 487-493. (Pubitemid 29292605)
    • (1999) Molecular Cell , vol.3 , Issue.4 , pp. 487-493
    • Bogden, C.E.1    Fass, D.2    Bergman, N.3    Nichols, M.D.4    Berger, J.M.5
  • 13
    • 0035958964 scopus 로고    scopus 로고
    • Identification of an RNA-binding site in the ATP binding domain of Escherichia coli Rho by H2O2/Fe-EDTA cleavage protection studies
    • Wei R. R., and Richardson J. P. (2001) Identification of an RNA-binding site in the ATP binding domain of Escherichia coli Rho by H2O2/Fe-EDTA cleavage protection studies. J. Biol. Chem. 276, 28380-28387.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28380-28387
    • Wei, R.R.1    Richardson, J.P.2
  • 14
    • 4344661527 scopus 로고    scopus 로고
    • Influence of substrate composition on the helicase activity of transcription termination factor Rho: Reduced processivity of Rho hexamers during unwinding of RNA-DNA hybrid regions
    • DOI 10.1016/j.jmb.2004.07.026, PII S0022283604008538
    • Walmacq C.,Rahmouni A. R., and Boudvillain M. (2004) Influence of substrate composition on the helicase activity of transcription termination factor Rho: reduced processivity of Rho hexamers during unwinding of RNA-DNA hybrid regions. J. Mol. Biol. 342, 403-420. (Pubitemid 39149747)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.2 , pp. 403-420
    • Walmacq, C.1    Rahmouni, A.R.2    Boudvillain, M.3
  • 15
    • 33646489157 scopus 로고    scopus 로고
    • Testing the steric exclusion model for hexameric helicases: Substrate features that alter RNA-DNA unwinding by the transcription termination factor Rho
    • Walmacq C.,Rahmouni A. R., and Boudvillain M. (2006) Testing the steric exclusion model for hexameric helicases: substrate features that alter RNA-DNA unwinding by the transcription termination factor Rho. Biochemistry 45, 5885-5895.
    • (2006) Biochemistry , vol.45 , pp. 5885-5895
    • Walmacq, C.1    Rahmouni, A.R.2    Boudvillain, M.3
  • 16
    • 34548104113 scopus 로고    scopus 로고
    • Noncanonical interactions in the management of RNA structural blocks by the transcription termination Rho helicase
    • DOI 10.1021/bi700493m
    • Schwartz A., Walmacq C., Rahmouni A. R., and Boudvillain M. (2007) Noncanonicalinteractions in the management of RNA structural blocks by the transcription termination rho helicase. Biochemistry 46, 9366-9379. (Pubitemid 47291944)
    • (2007) Biochemistry , vol.46 , Issue.33 , pp. 9366-9379
    • Schwartz, A.1    Walmacq, C.2    Rahmouni, A.R.3    Boudvillain, M.4
  • 17
    • 35748950148 scopus 로고    scopus 로고
    • Transcription termination factor Rho can displace streptavidin from biotinylated RNA
    • DOI 10.1074/jbc.M706935200
    • Schwartz A., Margeat E., Rahmouni A. R., and Boudvillain M. (2007) Transcription termination factor Rho can displace streptavidin from biotinylated RNA. J. Biol. Chem. 282, 31469-31476. (Pubitemid 350044863)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.43 , pp. 31469-31476
    • Schwartz, A.1    Margeat, E.2    Rahmouni, A.R.3    Boudvillain, M.4
  • 18
    • 0029807436 scopus 로고    scopus 로고
    • Purification of transcription termination factor Rho from Escherichia coli and Micrococcus luteus
    • DOI 10.1016/S0076-6879(96)74030-2
    • Nowatzke W., Richardson L., and Richardson J. P. (1996) Purification of transcription termination factor Rho from Escherichia coli and Micrococcus luteus. Methods Enzymol. 274, 353-363. (Pubitemid 26353090)
    • (1996) Methods in Enzymology , vol.274 , pp. 353-363
    • Nowatzke, W.1    Richardson, L.2    Richardson, J.P.3
  • 19
    • 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., Gill S., Calmettes P., and von Hippel P. (1992) Physical properties of the Escherichia coli transcription termination factor rho. 1. Association states and geometry of the rho hexamer. Biochemistry 31, 111-121.
    • (1992) Biochemistry , vol.31 , pp. 111-121
    • Geiselmann, J.1    Yager, T.2    Gill, S.3    Calmettes, P.4    Von Hippel, P.5
  • 20
    • 0034840623 scopus 로고    scopus 로고
    • A simple and efficient method to transcribe RNAs with reduced 3′ heterogeneity
    • DOI 10.1006/meth.2000.1131
    • Kao C., Rudisser S., and Zheng M. (2001) A simple and efficient method to transcribe RNAs with reduced 30 heterogeneity. Methods 23, 201-205. (Pubitemid 32848420)
    • (2001) Methods , vol.23 , Issue.3 , pp. 201-205
    • Kao, C.1    Rudisser, S.2    Zheng, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.