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Volumn 266, Issue 1, 1999, Pages 228-235

GroEL is involved in activation of escherichia coli RNA polymerase devoid of the ω subunit in vivo

Author keywords

70 interaction; Activation; GroEL; Renaturation; RNA polymerase ( less)

Indexed keywords

CHAPERONIN; RNA POLYMERASE;

EID: 0033571313     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00848.x     Document Type: Article
Times cited : (47)

References (34)
  • 1
    • 0014691239 scopus 로고
    • Separation and characterization of the subunits of RNA polymerase
    • 1. Burgess, R.R. (1969) Separation and characterization of the subunits of RNA polymerase. J. Biol. Chem. 244, 6168-6176.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6168-6176
    • Burgess, R.R.1
  • 2
    • 0023918675 scopus 로고
    • Structure and function of bacterial σ factors
    • 2. Helmann, J.D. & Chamberlin, M. (1988) Structure and function of bacterial σ factors. Annu. Rev. Biochem. 57, 839-872.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 839-872
    • Helmann, J.D.1    Chamberlin, M.2
  • 3
    • 0009535373 scopus 로고
    • PhD Dissertation. University of Wisconsin
    • 3. Gentry, D.R. (1990) PhD Dissertation. University of Wisconsin.
    • (1990)
    • Gentry, D.R.1
  • 4
    • 0024593347 scopus 로고
    • RpoZ, encoding the omega subunit of Escherichia coli RNA polymerase is in the same operon as spoT
    • 4. Gentry, D.R. & Burgess, R.R. (1989) rpoZ, encoding the omega subunit of Escherichia coli RNA polymerase is in the same operon as spoT. J. Bacterial. 171, 1271-1277.
    • (1989) J. Bacterial. , vol.171 , pp. 1271-1277
    • Gentry, D.R.1    Burgess, R.R.2
  • 6
    • 0030832404 scopus 로고    scopus 로고
    • Studies on the ω-subunit of Escherichia coli RNA polymerase: Its role in the recovery of denatured enzyme activity
    • 6. Mukherjee, K. & Chatterji, D. (1997) Studies on the ω-subunit of Escherichia coli RNA polymerase: its role in the recovery of denatured enzyme activity. Eur. J. Biochem. 247, 884-889.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 884-889
    • Mukherjee, K.1    Chatterji, D.2
  • 7
    • 0027442911 scopus 로고
    • Cross-linking of E. Coli RNA polymerase subunits: Identification of the β′ as the binding site of ω-subunit
    • 7. Gentry, D.R. & Burgess, R.R. (1993) Cross-linking of E. coli RNA polymerase subunits: identification of the β′ as the binding site of ω-subunit. Biochemistry 32, 11224-11227.
    • (1993) Biochemistry , vol.32 , pp. 11224-11227
    • Gentry, D.R.1    Burgess, R.R.2
  • 8
    • 0023832198 scopus 로고
    • An improved method for the purification of DNA-dependent Escherichia coli RNA polymerase
    • 8. Kumar, K.P. & Chatterji, D. (1988) An improved method for the purification of DNA-dependent Escherichia coli RNA polymerase. J. Biochem. Biophys. Methods 15, 235-240.
    • (1988) J. Biochem. Biophys. Methods , vol.15 , pp. 235-240
    • Kumar, K.P.1    Chatterji, D.2
  • 10
    • 0004167360 scopus 로고    scopus 로고
    • Academic Press, San Diego, USA
    • 10. Ellis, R.J. (1996) The Chaperonins. Academic Press, San Diego, USA.
    • (1996) The Chaperonins
    • Ellis, R.J.1
  • 11
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • 11. Hartl, F.-U. (1996) Molecular chaperones in cellular protein folding. Nature (London) 381, 571-580.
    • (1996) Nature (London) , vol.381 , pp. 571-580
    • Hartl, F.-U.1
  • 12
    • 0024554107 scopus 로고
    • The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
    • 12. Fayet, O., Ziegelhoffer, T. & Georgopoulos, C.P. (1989) The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacterial. 171, 1379-1385.
    • (1989) J. Bacterial. , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.P.3
  • 13
    • 0020030003 scopus 로고
    • Evidence that the two Escherichia coli groE morphogenetic gene products interact in vivo
    • 13. Tilly, K. & Georgopoulos, C. (1982) Evidence that the two Escherichia coli groE morphogenetic gene products interact in vivo. J. Bacteriol. 149, 1082-1088.
    • (1982) J. Bacteriol. , vol.149 , pp. 1082-1088
    • Tilly, K.1    Georgopoulos, C.2
  • 14
    • 0022981315 scopus 로고
    • Purification and properties of the groES morphogenetic protein of Escherichia coli
    • 14. Chandrasekhar, G.N., Tilly, K., Woolford, C., Hendrix, R. & Georgopoulos, C. (1986) Purification and properties of the GroES morphogenetic protein of Escherichia coli. J. Biol. Chem. 261, 12414-12419.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12414-12419
    • Chandrasekhar, G.N.1    Tilly, K.2    Woolford, C.3    Hendrix, R.4    Georgopoulos, C.5
  • 15
    • 0017158534 scopus 로고
    • A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli I. Co-purification and separation
    • 15. Ishihama, A., Ikeuchi, T. & Yura, T. (1976) A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli I. Co-purification and separation. J. Biochem. (Tokyo) 79, 917-925.
    • (1976) J. Biochem. (Tokyo) , vol.79 , pp. 917-925
    • Ishihama, A.1    Ikeuchi, T.2    Yura, T.3
  • 16
    • 0017138218 scopus 로고
    • A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure
    • 16. Ishihama, A., Ikeuchi, T., Matsumoto, A. & Yamamoto, S. (1976) A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure. J. Biochem. (Tokyo) 79, 927-936.
    • (1976) J. Biochem. (Tokyo) , vol.79 , pp. 927-936
    • Ishihama, A.1    Ikeuchi, T.2    Matsumoto, A.3    Yamamoto, S.4
  • 17
    • 0027331573 scopus 로고
    • Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE can reactivate heat treated RNA polymerase
    • 17. Ziemienowicz, A., Skowyra, D., Zielstra-Ryalls, J., Fayet, O., Georgopoulos, C.P. & Zylicz, M. (1993) Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE can reactivate heat treated RNA polymerase. J. Biol. Chem. 268, 25425-25431.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25425-25431
    • Ziemienowicz, A.1    Skowyra, D.2    Zielstra-Ryalls, J.3    Fayet, O.4    Georgopoulos, C.P.5    Zylicz, M.6
  • 18
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA
    • 18. Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 19
    • 0024578552 scopus 로고
    • GroE heat shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
    • 19. Goloubinoff, P., Gatenby, A.A. & Lorimer, G.H. (1989) GroE heat shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature (London) 337, 44-47.
    • (1989) Nature (London) , vol.337 , pp. 44-47
    • Goloubinoff, P.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 20
    • 0024820705 scopus 로고
    • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg ATP
    • 20. Goloubinoff, P., Christeller, J.T., Gatenby, A.A. & Lorimer, G.H. (1989) Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg ATP. Nature (London) 342, 884-889.
    • (1989) Nature (London) , vol.342 , pp. 884-889
    • Goloubinoff, P.1    Christeller, J.T.2    Gatenby, A.A.3    Lorimer, G.H.4
  • 21
    • 0025778597 scopus 로고
    • Bipartite functional map of the Escherichia coli RNA polymerase a subunit: Involvement of C-terminal region in transcription activation by cAMP-CRP
    • 21. Igarashi, K. & Ishihama, A. (1991) Bipartite functional map of the Escherichia coli RNA polymerase a subunit: involvement of C-terminal region in transcription activation by cAMP-CRP. Cell 65, 1015-1022.
    • (1991) Cell , vol.65 , pp. 1015-1022
    • Igarashi, K.1    Ishihama, A.2
  • 22
    • 0018780589 scopus 로고
    • Purification and properties of the σ-subunit of Escherichia coli DNA-dependent RNA polymerase
    • 22. Lowe, P.A., Hager, D.A. & Burgess, R.R. (1979) Purification and properties of the σ-subunit of Escherichia coli DNA-dependent RNA polymerase. Biochemistry 18, 1344-1352.
    • (1979) Biochemistry , vol.18 , pp. 1344-1352
    • Lowe, P.A.1    Hager, D.A.2    Burgess, R.R.3
  • 23
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • 23. Blum, H., Beier, H. & Gross, J.H. (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, J.H.3
  • 24
    • 0028145153 scopus 로고
    • A point mutation at the junction of domain 2.3/2.4 transcription factor sigma-70 abrogates productive transcription and restores its expected mobility on a denaturing gel
    • 24. Gopal, V., Ma, H.W., Kumaran, M.K. & Chatterji, D. (1994) A point mutation at the junction of domain 2.3/2.4 transcription factor sigma-70 abrogates productive transcription and restores its expected mobility on a denaturing gel. J. Mol. Biol. 242, 9-22.
    • (1994) J. Mol. Biol. , vol.242 , pp. 9-22
    • Gopal, V.1    Ma, H.W.2    Kumaran, M.K.3    Chatterji, D.4
  • 25
    • 0025886298 scopus 로고
    • The omega subunit of Escherichia coli K-12 RNA polymerase is not required for stringent RNA control in vivo
    • 25. Gentry, D.R., Xiao, H., Burgess, R.R. & Cashel, M. (1991) The omega subunit of Escherichia coli K-12 RNA polymerase is not required for stringent RNA control in vivo. J. Bacterial. 173, 3901-3903.
    • (1991) J. Bacterial. , vol.173 , pp. 3901-3903
    • Gentry, D.R.1    Xiao, H.2    Burgess, R.R.3    Cashel, M.4
  • 26
    • 0001130675 scopus 로고
    • Purification of two forms of Escherichia coli RNA polymerase and of sigma component
    • 26. Berg, D., Barrett, K. & Chamberlin, M. (1971) Purification of two forms of Escherichia coli RNA polymerase and of sigma component. Methods Enzymol. 21, 506-519.
    • (1971) Methods Enzymol. , vol.21 , pp. 506-519
    • Berg, D.1    Barrett, K.2    Chamberlin, M.3
  • 27
    • 0024473535 scopus 로고
    • Promoter selectivity of E.Coli RNA polymerase: ω factor is responsible for the ppGpp sensitivity
    • 27. Igarashi, K., Fujita, N. & Ishihama, A. (1989) Promoter selectivity of E.coli RNA polymerase: ω factor is responsible for the ppGpp sensitivity. Nucleic Acids Res. 17, 8755-8765.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8755-8765
    • Igarashi, K.1    Fujita, N.2    Ishihama, A.3
  • 28
    • 0032032533 scopus 로고    scopus 로고
    • Conversion of the ω subunit of Escherichia coli RNA polymerase into a transcriptional activitor or an activation target
    • 28. Dove, S.L. & Hochschild, A. (1998) Conversion of the ω subunit of Escherichia coli RNA polymerase into a transcriptional activitor or an activation target. Genes Dev. 12, 745-754.
    • (1998) Genes Dev. , vol.12 , pp. 745-754
    • Dove, S.L.1    Hochschild, A.2
  • 29
    • 0026416043 scopus 로고
    • Chaperonin mediated protein folding at the surface of GroEL through a "molten globule" like intermediate
    • 29. Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A.L. & Hartl, F.-U. (1991) Chaperonin mediated protein folding at the surface of GroEL through a "molten globule" like intermediate. Nature (London) 352, 36-42.
    • (1991) Nature (London) , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A.L.5    Hartl, F.-U.6
  • 30
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the Bacterial Chaperonin system
    • 30. Ewait, K.L., Hendrick, J.P., Houry, W.A. & Hartl, F.-U. (1997) In vivo observation of polypeptide flux through the Bacterial Chaperonin system. Cell. 90, 491-500.
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewait, K.L.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.-U.4
  • 31
    • 0030792944 scopus 로고    scopus 로고
    • Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen Cage
    • 31. Hunt, J.F., Van der Vies, S.M., Henry, S. & Deisenhofer, J. (1997) Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen Cage. Cell 90, 361-371.
    • (1997) Cell , vol.90 , pp. 361-371
    • Hunt, J.F.1    Van Der Vies, S.M.2    Henry, S.3    Deisenhofer, J.4
  • 33
    • 0032574843 scopus 로고    scopus 로고
    • A stationary phase protein in Escherichia coli with binding activity to the major σ subunit of RNA polymerase
    • 33. Jishage, M. & Ishihama, A. (1998) A stationary phase protein in Escherichia coli with binding activity to the major σ subunit of RNA polymerase. Proc. Natl Acad. Sci. USA 95, 4953-4958.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 4953-4958
    • Jishage, M.1    Ishihama, A.2
  • 34
    • 0019444030 scopus 로고
    • Subunit assembly of E. coli RNA polymerase
    • 34. Ishihama, A. (1981) Subunit assembly of E. coli RNA polymerase. Adv. Biophys. 14, 1-35.
    • (1981) Adv. Biophys. , vol.14 , pp. 1-35
    • Ishihama, A.1


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