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Volumn , Issue , 2010, Pages 357-375

cAMP Signaling in Prokaryotes

Author keywords

CAMP; CAMP receptor protein; Carbon catabolite repression; Phosphotransferase system; Prokaryote; Signaling

Indexed keywords


EID: 84856309171     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527629237.ch20     Document Type: Chapter
Times cited : (2)

References (93)
  • 2
    • 0001523133 scopus 로고
    • Adenosine 30,50-phosphate in Escherichia coli
    • Makman, R.S. and Sutherland, E.W. (1965) Adenosine 30,50-phosphate in Escherichia coli. J. Biol. Chem., 240, 1309-1314.
    • (1965) J. Biol. Chem. , vol.240 , pp. 1309-1314
    • Makman, R.S.1    Sutherland, E.W.2
  • 4
    • 0021858740 scopus 로고
    • Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria
    • Postma, P.W. and Lengeler, J.W. (1985) Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev., 49, 232-269.
    • (1985) Microbiol. Rev. , vol.49 , pp. 232-269
    • Postma, P.W.1    Lengeler, J.W.2
  • 6
    • 0000819850 scopus 로고
    • Adenosine 30:50-cyclic monophosphate as mediator of catabolite repression in Escherichia coli
    • Epstein, W., Rothman-Denes, L.B., and Hesse, J. (1975) Adenosine 30:50-cyclic monophosphate as mediator of catabolite repression in Escherichia coli. Proc. Natl. Acad. Sci., 72, 2300-2304.
    • (1975) Proc. Natl. Acad. Sci. , vol.72 , pp. 2300-2304
    • Epstein, W.1    Rothman-Denes, L.B.2    Hesse, J.3
  • 7
    • 0030905517 scopus 로고    scopus 로고
    • Catabolite repression by glucose- 6-phosphate, gluconate and lactose in Escherichia coli
    • Hogema, B.M., Arents, J.C., Inada, T., Aiba, H., van Dam, K., and Postma, P.W. (1997) Catabolite repression by glucose- 6-phosphate, gluconate and lactose in Escherichia coli. Mol. Microbiol., 24, 857-867.
    • (1997) Mol. Microbiol. , vol.24 , pp. 857-867
    • Hogema, B.M.1    Arents, J.C.2    Inada, T.3    Aiba, H.4    van Dam, K.5    Postma, P.W.6
  • 8
    • 0035909791 scopus 로고    scopus 로고
    • Modeling of inducer exclusion and catabolite repression based on a PTS-dependent sucrose and non-PTS-dependent glycerol transport systems in Escherichia coli K-12 and its experimental verification
    • Wang, J., Gilles, E.D., Lengeler, J.W., and Jahreis, K. (2001) Modeling of inducer exclusion and catabolite repression based on a PTS-dependent sucrose and non-PTS-dependent glycerol transport systems in Escherichia coli K-12 and its experimental verification. J. Biotechnol., 92, 133-158.
    • (2001) J. Biotechnol. , vol.92 , pp. 133-158
    • Wang, J.1    Gilles, E.D.2    Lengeler, J.W.3    Jahreis, K.4
  • 10
    • 0020415825 scopus 로고
    • Regulation of adenylate cyclase synthesis in Escherichia coli: studies with cya-lac operon and protein fusion strains
    • Bankaitis, V.A. and Bassford, P.J. Jr. (1982) Regulation of adenylate cyclase synthesis in Escherichia coli: studies with cya-lac operon and protein fusion strains. J. Bacteriol., 151, 1346-1357.
    • (1982) J. Bacteriol. , vol.151 , pp. 1346-1357
    • Bankaitis, V.A.1    Bassford Jr., P.J.2
  • 11
    • 0021965147 scopus 로고
    • Regulation of cya-lacZ fusions by cyclic AMP in Salmonella typhimurium
    • Jovanovitch, S.B. (1985) Regulation of cya-lacZ fusions by cyclic AMP in Salmonella typhimurium. J. Bacteriol., 161, 641-649.
    • (1985) J. Bacteriol. , vol.161 , pp. 641-649
    • Jovanovitch, S.B.1
  • 12
    • 0023837101 scopus 로고
    • Aspects of the regulation of adenylate cyclase synthesis in Escherichia coli K12
    • Roy, A., Glaser, P., and Danchin, A. (1988) Aspects of the regulation of adenylate cyclase synthesis in Escherichia coli K12. J. Gen. Microbiol., 134, 359-367.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 359-367
    • Roy, A.1    Glaser, P.2    Danchin, A.3
  • 13
    • 0021958061 scopus 로고
    • Transcription of the Escherichia coli adenylate cyclase gene is negatively regulated by cAMP-cAMP receptor protein
    • Aiba, H. (1984) Transcription of the Escherichia coli adenylate cyclase gene is negatively regulated by cAMP-cAMP receptor protein. J. Biol. Chem., 260, 3063-3070.
    • (1984) J. Biol. Chem. , vol.260 , pp. 3063-3070
    • Aiba, H.1
  • 14
    • 0016820211 scopus 로고
    • Interaction of enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system with adenylate cyclase of Escherichia coli
    • Peterkofsky, A. and Gazdar, C. (1975) Interaction of enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system with adenylate cyclase of Escherichia coli. Proc. Natl. Acad. Sci. USA, 72, 2920-2924.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 2920-2924
    • Peterkofsky, A.1    Gazdar, C.2
  • 15
    • 0016817503 scopus 로고
    • Coordinate regulation of adenylate cyclase and carbohydrate permeases by the phosphoenolpyruvate: sugar phosphotransferase system in Salmonella typhimurium
    • Saier, M.H.j. and Feucht, B.U. (1975) Coordinate regulation of adenylate cyclase and carbohydrate permeases by the phosphoenolpyruvate: sugar phosphotransferase system in Salmonella typhimurium. J. Biol. Chem., 250, 7078-7080.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7078-7080
    • Saier, M.H.J.1    Feucht, B.U.2
  • 16
    • 0017063591 scopus 로고
    • Involvement of the glucose enzymes II of the sugar phosphotransferase system in the regulation of adenylate cyclase by glucose in Escherichia coli
    • Harwood, J.P., Gazdar, C., Prasad, C., Peterkofsky, A., Curtis, S.J., and Epstein,W. (1976) Involvement of the glucose enzymes II of the sugar phosphotransferase system in the regulation of adenylate cyclase by glucose in Escherichia coli. J. Biol. Chem., 251, 2462-2468.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2462-2468
    • Harwood, J.P.1    Gazdar, C.2    Prasad, C.3    Peterkofsky, A.4    Curtis, S.J.5    Epstein, W.6
  • 17
    • 0018818715 scopus 로고
    • Fine control of adenylate cyclase by the phosphoenolpyruvate: sugar phosphotransferase systems in Escherichia coli and Salmonella typhimurium
    • Feucht, B.U. and Saier, M.H. Jr (1980) Fine control of adenylate cyclase by the phosphoenolpyruvate: sugar phosphotransferase systems in Escherichia coli and Salmonella typhimurium. J. Bacteriol., 141, 603-610.
    • (1980) J. Bacteriol. , vol.141 , pp. 603-610
    • Feucht, B.U.1    Saier Jr., M.H.2
  • 18
    • 33845626641 scopus 로고    scopus 로고
    • How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria
    • Deutscher, J. and Postma, P.W. (2004) How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. Microbiol. Mol. Biol. Rev., 70, 939-1031.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 939-1031
    • Deutscher, J.1    Postma, P.W.2
  • 19
    • 0029795442 scopus 로고    scopus 로고
    • Enzyme I: the first protein and potential regulator of the bacterial phosphoenolpyruvate: glycose phosphotransferase system
    • Chauvin, F., Brand, L., and Roseman, S. (1996) Enzyme I: the first protein and potential regulator of the bacterial phosphoenolpyruvate: glycose phosphotransferase system. Res. Microbiol., 147, 471-479.
    • (1996) Res. Microbiol. , vol.147 , pp. 471-479
    • Chauvin, F.1    Brand, L.2    Roseman, S.3
  • 20
    • 25444463274 scopus 로고    scopus 로고
    • Transient state kinetics of Enzyme I of the phosphoenolpyruvate: glycose phosphotransferase system of Escherichia coli: equilibrium and second-order rate constants for the phosphotransfer reactions with phosphoenolpyruvate and HPr
    • Meadow, N.D., Mattoo, R.L., Savtchenko, R.S., and Roseman, S. (2005) Transient state kinetics of Enzyme I of the phosphoenolpyruvate: glycose phosphotransferase system of Escherichia coli: equilibrium and second-order rate constants for the phosphotransfer reactions with phosphoenolpyruvate and HPr. Biochemistry, 44, 12790-12796.
    • (2005) Biochemistry , vol.44 , pp. 12790-12796
    • Meadow, N.D.1    Mattoo, R.L.2    Savtchenko, R.S.3    Roseman, S.4
  • 21
    • 67651205583 scopus 로고    scopus 로고
    • Bacterial PEP-dependent carbohydrate: phosphotransferase systems couple sensing and global control mechanisms
    • Lengeler, J.W. and Jahreis, K. (2009) Bacterial PEP-dependent carbohydrate: phosphotransferase systems couple sensing and global control mechanisms. Contribut. Microbiol., 16, 65-87.
    • (2009) Contribut. Microbiol. , vol.16 , pp. 65-87
    • Lengeler, J.W.1    Jahreis, K.2
  • 22
    • 0031912637 scopus 로고    scopus 로고
    • Glc of the phosphoenolpyruvate: sugar phosphotransferase system
    • Glc of the phosphoenolpyruvate: sugar phosphotransferase system. J. Bacteriol., 180, 732-736.
    • (1998) J. Bacteriol. , vol.180 , pp. 732-736
    • Reddy, P.1    Kamireddi, M.2
  • 23
  • 24
    • 0021111712 scopus 로고
    • Two functional domains in adenylate cyclase of Escherichia coli
    • Roy, A., Danchin, A., Joseph, E., and Ullmann, A. (1983) Two functional domains in adenylate cyclase of Escherichia coli. J. Mol. Biol., 165, 197-202.
    • (1983) J. Mol. Biol. , vol.165 , pp. 197-202
    • Roy, A.1    Danchin, A.2    Joseph, E.3    Ullmann, A.4
  • 25
    • 0028879941 scopus 로고
    • Mapping domains in proteins: dissection and expression of Escherichia coli adenylyl cyclase
    • Reddy, P., Hoskins, J., and McKenney, K. (1995) Mapping domains in proteins: dissection and expression of Escherichia coli adenylyl cyclase. Anal. Biochem., 231, 282-286.
    • (1995) Anal. Biochem. , vol.231 , pp. 282-286
    • Reddy, P.1    Hoskins, J.2    McKenney, K.3
  • 26
    • 0024989681 scopus 로고
    • Characterization of Escherichia coli adenylate cyclase mutants with modified regulation
    • Crasnier, M. and Danchin, A. (1990) Characterization of Escherichia coli adenylate cyclase mutants with modified regulation. J. Gen. Microbiol., 136, 1825-1831.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 1825-1831
    • Crasnier, M.1    Danchin, A.2
  • 27
    • 0028239040 scopus 로고
    • The catalytic domain of Escherichia coli K-12 adenylate cyclase as revealed by deletion analysis of the cya gene
    • Crasnier, M., Dumay, V., and Danchin, A. (1994) The catalytic domain of Escherichia coli K-12 adenylate cyclase as revealed by deletion analysis of the cya gene. Mol. Gen. Genet., 243, 409-416.
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 409-416
    • Crasnier, M.1    Dumay, V.2    Danchin, A.3
  • 28
    • 0020619694 scopus 로고
    • Purification and characterization of adenylate cyclase from Escherichia coli K12
    • Yang, J.K. and Epstein, W. (1983) Purification and characterization of adenylate cyclase from Escherichia coli K12. J. Biol. Chem., 258, 3750-3758.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3750-3758
    • Yang, J.K.1    Epstein, W.2
  • 29
    • 0022295182 scopus 로고
    • Reconstitution of regulatory properties of adenylate cyclase in Escherichia coli extracts
    • Reddy, P., Meadow, N., Roseman, S., and Peterkofsky, A. (1985) Reconstitution of regulatory properties of adenylate cyclase in Escherichia coli extracts. Proc. Natl. Acad. Sci. USA, 82, 8300-8304.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8300-8304
    • Reddy, P.1    Meadow, N.2    Roseman, S.3    Peterkofsky, A.4
  • 30
    • 33646570920 scopus 로고    scopus 로고
    • In vitro reconstitution of catabolite repression in Escherichia coli
    • Park, Y.H., Lee, B.R., Seok, Y.J., and Peterkofsky, A. (2006) In vitro reconstitution of catabolite repression in Escherichia coli. J. Biol. Chem., 281, 6448-6454.
    • (2006) J. Biol. Chem. , vol.281 , pp. 6448-6454
    • Park, Y.H.1    Lee, B.R.2    Seok, Y.J.3    Peterkofsky, A.4
  • 31
    • 0033787566 scopus 로고    scopus 로고
    • Metabolic networks: a signal-oriented approach to cellular models
    • Lengeler, J.W. (2000) Metabolic networks: a signal-oriented approach to cellular models. Biol. Chem., 381, 911-920.
    • (2000) Biol. Chem. , vol.381 , pp. 911-920
    • Lengeler, J.W.1
  • 33
    • 0029669943 scopus 로고    scopus 로고
    • Regulation of Escherichia coli adenylate cyclase activity during hexose phosphate transport
    • Dumay, V., Danchin, A., and Crasnier, M. (1996) Regulation of Escherichia coli adenylate cyclase activity during hexose phosphate transport. Microbiology, 142, 575-583.
    • (1996) Microbiology , vol.142 , pp. 575-583
    • Dumay, V.1    Danchin, A.2    Crasnier, M.3
  • 34
    • 0016193261 scopus 로고
    • Cyclic AMP phosphodiesterase of Escherichia coli
    • Nielsen, L.D. and Rickenberg, H.V. (1974) Cyclic AMP phosphodiesterase of Escherichia coli. Methods Enzymol., 38, 249-256.
    • (1974) Methods Enzymol. , vol.38 , pp. 249-256
    • Nielsen, L.D.1    Rickenberg, H.V.2
  • 35
    • 0018600852 scopus 로고
    • Transport of cyclic adenosine 30,50- monophosphate across Escherichia coli vesicle membranes
    • Goldenbaum, P.E. and Hall, G.A. (1979) Transport of cyclic adenosine 30,50- monophosphate across Escherichia coli vesicle membranes. J. Bacteriol., 140, 459-467.
    • (1979) J. Bacteriol. , vol.140 , pp. 459-467
    • Goldenbaum, P.E.1    Hall, G.A.2
  • 38
    • 0018117107 scopus 로고
    • The cyclic 30,50-adenosine monophosphate receptor protein and regulation of cyclic 30,50-adenosine monophosphate synthesis in Escherichia coli
    • Botsford, J.L. and Drexler, M. (1978) The cyclic 30,50-adenosine monophosphate receptor protein and regulation of cyclic 30,50-adenosine monophosphate synthesis in Escherichia coli. Mol. Gen. Genet., 165, 47-56.
    • (1978) Mol. Gen. Genet. , vol.165 , pp. 47-56
    • Botsford, J.L.1    Drexler, M.2
  • 39
    • 0018178465 scopus 로고
    • Determination of the rates of synthesis and degradation of adenosine 30,50-cyclic monophosphate in Escherichia coli CRP- and CRP+ strains
    • Fraser, A.D. and Yamazaki, H. (1978) Determination of the rates of synthesis and degradation of adenosine 30,50-cyclic monophosphate in Escherichia coli CRP- and CRP+ strains. Can. J. Biochem., 56, 849-852.
    • (1978) Can. J. Biochem. , vol.56 , pp. 849-852
    • Fraser, A.D.1    Yamazaki, H.2
  • 40
    • 0015956395 scopus 로고
    • Abnormally high rate of cyclic AMP excretion from an Escherichia coli mutant deficient in cyclic AMP receptor protein
    • Potter, K., Chaloner-Larsson, G., and Yamazaki, H. (1974) Abnormally high rate of cyclic AMP excretion from an Escherichia coli mutant deficient in cyclic AMP receptor protein. Biochem. Biophys. Res. Commun., 57, 379-385.
    • (1974) Biochem. Biophys. Res. Commun. , vol.57 , pp. 379-385
    • Potter, K.1    Chaloner-Larsson, G.2    Yamazaki, H.3
  • 41
    • 0026800962 scopus 로고
    • A new aspect of transcriptional control of the Escherichia coli crp gene: positive autoregulation
    • Hanamura, A. and Aiba, H. (1992) A new aspect of transcriptional control of the Escherichia coli crp gene: positive autoregulation. Mol. Microbiol., 6, 2489-2497.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2489-2497
    • Hanamura, A.1    Aiba, H.2
  • 42
    • 0022452957 scopus 로고
    • Mechanism for the autogenous control of the crp operon: transcriptional inhibition by a divergent RNA transcript
    • Okamoto, K. and Freundlich, M. (1986) Mechanism for the autogenous control of the crp operon: transcriptional inhibition by a divergent RNA transcript. Proc. Natl. Acad. Sci. USA, 83, 5000-5004.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5000-5004
    • Okamoto, K.1    Freundlich, M.2
  • 43
    • 0024110098 scopus 로고
    • Evidence in vivo for autogenous control of the cyclic AMP receptor protein gene (crp) in Escherichia coli by divergent RNA
    • Okamoto, K., Hara, S., Bhasin, R., and Freundlich, M. (1988) Evidence in vivo for autogenous control of the cyclic AMP receptor protein gene (crp) in Escherichia coli by divergent RNA. J. Bacteriol., 170, 5076-5079.
    • (1988) J. Bacteriol. , vol.170 , pp. 5076-5079
    • Okamoto, K.1    Hara, S.2    Bhasin, R.3    Freundlich, M.4
  • 44
    • 0037582107 scopus 로고    scopus 로고
    • Regulation of crp transcription by oscillation between distinct nucleoprotein complexes
    • Gonzalez-Gil, G., Kahmann, R., and Muskhelishvili, G. (1998) Regulation of crp transcription by oscillation between distinct nucleoprotein complexes. EMBO J., 17, 2877-2885.
    • (1998) EMBO J. , vol.17 , pp. 2877-2885
    • Gonzalez-Gil, G.1    Kahmann, R.2    Muskhelishvili, G.3
  • 45
    • 0034682744 scopus 로고    scopus 로고
    • Nucleoid proteins stimulate stringently controlled bacterial promoters: a link between the cAMP-CRP and the (p)ppGpp regulons in Escherichia coli
    • Johansson, J., Balsalobre, C., Wang, S.Y., Urbonaviciene, J., Jin, D.J., Sonden, B., and Uhlin, B.E. (2000) Nucleoid proteins stimulate stringently controlled bacterial promoters: a link between the cAMP-CRP and the (p)ppGpp regulons in Escherichia coli. Cell, 102, 475-485.
    • (2000) Cell , vol.102 , pp. 475-485
    • Johansson, J.1    Balsalobre, C.2    Wang, S.Y.3    Urbonaviciene, J.4    Jin, D.J.5    Sonden, B.6    Uhlin, B.E.7
  • 46
    • 0023661228 scopus 로고
    • Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 A resolution
    • Weber, I.T. and Steitz, T.A. (1987) Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 A resolution. J. Mol. Biol., 198, 311-326.
    • (1987) J. Mol. Biol. , vol.198 , pp. 311-326
    • Weber, I.T.1    Steitz, T.A.2
  • 47
    • 0021225932 scopus 로고
    • Model of specific complex between catabolite gene activator protein and B-DNA suggested by electrostatic complementarity
    • Weber, I.T. and Steitz, T.A. (1984) Model of specific complex between catabolite gene activator protein and B-DNA suggested by electrostatic complementarity. Proc. Natl. Acad. Sci. USA, 81, 3973-3977.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3973-3977
    • Weber, I.T.1    Steitz, T.A.2
  • 48
    • 0025306524 scopus 로고
    • Lysine 188 of the catabolite gene activator protein (CAP) plays no role in specificity at base pair 7 of the DNA half site
    • Ebright, R.H., Gunasekera, A., Zhang, X.P., Kunkel, T.A., and Krakow, J.S. (1990) Lysine 188 of the catabolite gene activator protein (CAP) plays no role in specificity at base pair 7 of the DNA half site. Nucleic Acids Res., 18, 1457-1464.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1457-1464
    • Ebright, R.H.1    Gunasekera, A.2    Zhang, X.P.3    Kunkel, T.A.4    Krakow, J.S.5
  • 49
    • 0030593510 scopus 로고    scopus 로고
    • Structure of the CAP-DNA complex at 2.5 angstroms resolution: a complete picture of the protein-DNA interface
    • Parkinson, G., Wilson, C., Gunasekera, A., Ebright, Y.W., Ebright, R.E., and Berman, H.M. (1996) Structure of the CAP-DNA complex at 2.5 angstroms resolution: a complete picture of the protein-DNA interface. J. Mol. Biol., 260, 395-408.
    • (1996) J. Mol. Biol. , vol.260 , pp. 395-408
    • Parkinson, G.1    Wilson, C.2    Gunasekera, A.3    Ebright, Y.W.4    Ebright, R.E.5    Berman, H.M.6
  • 50
    • 0021245317 scopus 로고
    • Cyclic AMP receptor protein: role in transcription activation
    • de Crombrugghe, B., Busby, S., and Buc, H. (1984) Cyclic AMP receptor protein: role in transcription activation. Science, 224, 831-838.
    • (1984) Science , vol.224 , pp. 831-838
    • de Crombrugghe, B.1    Busby, S.2    Buc, H.3
  • 51
    • 0024844517 scopus 로고
    • Consensus DNA site for the Escherichia coli catabolite gene activator protein (CAP): CAP exhibits a 450-fold higher affinity for the consensus DNA site than for the E. coli lac DNA site
    • Ebright, R.H., Ebright, Y.W., and Gunasekera, A. (1989) Consensus DNA site for the Escherichia coli catabolite gene activator protein (CAP): CAP exhibits a 450-fold higher affinity for the consensus DNA site than for the E. coli lac DNA site. Nucleic Acids Res., 17, 10295-10305.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 10295-10305
    • Ebright, R.H.1    Ebright, Y.W.2    Gunasekera, A.3
  • 52
    • 0026033201 scopus 로고
    • Sequence-dependent contribution of distal binding domains to CAP protein-DNA binding affinity
    • Dalma-Weiszhausz, D.D., Gartenberg, M.R., and Crothers, D.M. (1991) Sequence-dependent contribution of distal binding domains to CAP protein-DNA binding affinity. Nucleic Acids Res., 19, 611-616.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 611-616
    • Dalma-Weiszhausz, D.D.1    Gartenberg, M.R.2    Crothers, D.M.3
  • 53
    • 0020625051 scopus 로고
    • Mechanism of CRP-mediated cya suppression in Escherichia coli
    • Harman, J.G. and Dobrogosz, W.J. (1983) Mechanism of CRP-mediated cya suppression in Escherichia coli. J. Bacteriol., 153, 191-199.
    • (1983) J. Bacteriol. , vol.153 , pp. 191-199
    • Harman, J.G.1    Dobrogosz, W.J.2
  • 54
    • 0023002026 scopus 로고
    • Properties of cyclic AMP-independent catabolite gene activator proteins of Escherichia coli
    • Blazy, B. and Ullmann, A. (1986) Properties of cyclic AMP-independent catabolite gene activator proteins of Escherichia coli. J. Biol. Chem., 261, 11645-11649.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11645-11649
    • Blazy, B.1    Ullmann, A.2
  • 55
    • 0022902508 scopus 로고
    • Structure-function analysis of three cAMP-independent forms of thecAMPreceptor protein
    • Harman, J.G., McKenney, K., and Peterkofsky, A. (1986) Structure-function analysis of three cAMP-independent forms of thecAMPreceptor protein. J. Biol. Chem., 261, 16332-16339.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16332-16339
    • Harman, J.G.1    McKenney, K.2    Peterkofsky, A.3
  • 56
    • 0023918854 scopus 로고
    • Arginine substituted for leucine at position 195 produces a cyclic AMP-independent form of the Escherichia coli cyclic AMP receptor protein
    • Harman, J.G., Peterkofsky, A., and McKenney, K. (1988) Arginine substituted for leucine at position 195 produces a cyclic AMP-independent form of the Escherichia coli cyclic AMP receptor protein. J. Biol. Chem., 263, 8072-8077.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8072-8077
    • Harman, J.G.1    Peterkofsky, A.2    McKenney, K.3
  • 57
    • 0027236999 scopus 로고
    • Transcriptional regulation by cAMP and its receptor protein
    • Kolb, A., Busby, S., Buc, H.,Garges, S., and Adhya, S. (1993) Transcriptional regulation by cAMP and its receptor protein. Annu. Rev. Biochem., 62, 749-795.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 749-795
    • Kolb, A.1    Busby, S.2    Buc, H.3    Garges, S.4    Adhya, S.5
  • 58
    • 0031909984 scopus 로고    scopus 로고
    • Catabolite gene activator protein mutations affecting activity of the araBAD promoter
    • Zhang, X. and Schleif, R. (1998) Catabolite gene activator protein mutations affecting activity of the araBAD promoter. J. Bacteriol., 180, 195-200.
    • (1998) J. Bacteriol. , vol.180 , pp. 195-200
    • Zhang, X.1    Schleif, R.2
  • 59
    • 0025886425 scopus 로고
    • A new mechanism for coactivation of transcription initiation: repositioning of an activator triggered by the binding of a second activator
    • Richet, E., Vidal-Ingigliardi, D., and Raibaud, O. (1991) A new mechanism for coactivation of transcription initiation: repositioning of an activator triggered by the binding of a second activator. Cell, 66, 1185-1195.
    • (1991) Cell , vol.66 , pp. 1185-1195
    • Richet, E.1    Vidal-Ingigliardi, D.2    Raibaud, O.3
  • 60
    • 0025185784 scopus 로고
    • Helical phase dependent action of CRP: effect of the distance between the CRP site and the -35 region on promoter activity
    • Ushida, C. and Aiba, H. (1990) Helical phase dependent action of CRP: effect of the distance between the CRP site and the -35 region on promoter activity. Nucleic Acids Res., 18, 6325-6330.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6325-6330
    • Ushida, C.1    Aiba, H.2
  • 61
    • 0025072237 scopus 로고
    • Stringent spacing requirements for transcription activation by CRP
    • Gaston, K., Bell, A., Kolb, A., Buc, H., and Busby, S. (1990) Stringent spacing requirements for transcription activation by CRP. Cell, 62, 733-743.
    • (1990) Cell , vol.62 , pp. 733-743
    • Gaston, K.1    Bell, A.2    Kolb, A.3    Buc, H.4    Busby, S.5
  • 63
    • 0028024291 scopus 로고
    • The functional subunit of a dimeric transcription activator protein depends on promoter architecture
    • Zhou, Y., Pendergrast, P.S., Bell, A., Williams, R., Busby, S., and Ebright, R.H. (1994) The functional subunit of a dimeric transcription activator protein depends on promoter architecture. EMBO J., 13, 4549-4557.
    • (1994) EMBO J. , vol.13 , pp. 4549-4557
    • Zhou, Y.1    Pendergrast, P.S.2    Bell, A.3    Williams, R.4    Busby, S.5    Ebright, R.H.6
  • 64
    • 0029987740 scopus 로고    scopus 로고
    • Orientation of functional activating regions in the Escherichia coli CRP protein during transcription activation at class II promoters
    • Williams, R.M., Rhodius, V.A., Bell, A.I., Kolb, A., and Busby, S.J. (1996) Orientation of functional activating regions in the Escherichia coli CRP protein during transcription activation at class II promoters. Nucleic Acids Res., 24, 1112-1118.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1112-1118
    • Williams, R.M.1    Rhodius, V.A.2    Bell, A.I.3    Kolb, A.4    Busby, S.J.5
  • 65
    • 0034595498 scopus 로고    scopus 로고
    • Interactions between activating region 3 of the Escherichia coli cyclic AMP receptor protein and region 4 of the RNA polymerase sigma70 subunit: application of suppression genetics
    • Rhodius, V.A. and Busby, S.J. (2000) Interactions between activating region 3 of the Escherichia coli cyclic AMP receptor protein and region 4 of the RNA polymerase sigma70 subunit: application of suppression genetics. J. Mol. Biol., 299, 311-324.
    • (2000) J. Mol. Biol. , vol.299 , pp. 311-324
    • Rhodius, V.A.1    Busby, S.J.2
  • 66
    • 0032698634 scopus 로고    scopus 로고
    • Transcription activation by catabolite activator protein (CAP)
    • Busby, S. and Ebright, R.H. (1999) Transcription activation by catabolite activator protein (CAP). J. Mol. Biol., 293, 199-213.
    • (1999) J. Mol. Biol. , vol.293 , pp. 199-213
    • Busby, S.1    Ebright, R.H.2
  • 68
    • 0022885153 scopus 로고
    • The DNA binding domain and bending angle of E. coli CAP protein
    • Liu-Johnson, H.N., Gartenberg, M.R., and Crothers, D.M. (1986) The DNA binding domain and bending angle of E. coli CAP protein. Cell, 47, 995-1005.
    • (1986) Cell , vol.47 , pp. 995-1005
    • Liu-Johnson, H.N.1    Gartenberg, M.R.2    Crothers, D.M.3
  • 69
    • 0025736763 scopus 로고
    • Synthetic DNA bending sequences increase the rate of in vitro transcription initiation at the Escherichia coli lac promoter
    • Gartenberg, M.R. and Crothers, D.M. (1991) Synthetic DNA bending sequences increase the rate of in vitro transcription initiation at the Escherichia coli lac promoter. J. Mol. Biol., 219, 217-230.
    • (1991) J. Mol. Biol. , vol.219 , pp. 217-230
    • Gartenberg, M.R.1    Crothers, D.M.2
  • 70
    • 0029927561 scopus 로고    scopus 로고
    • A flexible partnership: theCytR anti-activator and the cAMP-CRP activator protein, comrades in transcription control
    • Valentin-Hansen, P., Sogaard-Andersen, L., and Pedersen, H. (1996) A flexible partnership: theCytR anti-activator and the cAMP-CRP activator protein, comrades in transcription control. Mol. Microbiol., 20, 461-466.
    • (1996) Mol. Microbiol. , vol.20 , pp. 461-466
    • Valentin-Hansen, P.1    Sogaard-Andersen, L.2    Pedersen, H.3
  • 71
    • 2442655332 scopus 로고    scopus 로고
    • Transcriptome analysis of Crp-dependent catabolite control of gene expression in Escherichia coli
    • Gosset, G., Zhang, Z., Nayyar, S., Cuevas, W.A., and Saier, M.H. Jr. (2004) Transcriptome analysis of Crp-dependent catabolite control of gene expression in Escherichia coli. J. Bacteriol., 186, 3516-3524.
    • (2004) J. Bacteriol. , vol.186 , pp. 3516-3524
    • Gosset, G.1    Zhang, Z.2    Nayyar, S.3    Cuevas, W.A.4    Saier Jr., M.H.5
  • 72
    • 7444245668 scopus 로고    scopus 로고
    • Identification of the CRP regulon using in vitro and in vivo transcriptional profiling
    • Zheng, D., Constantinidou, C., Hobman, J.L., and Minchin, S.D. (2004) Identification of the CRP regulon using in vitro and in vivo transcriptional profiling. Nucleic Acids Res., 32, 5874-5893.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5874-5893
    • Zheng, D.1    Constantinidou, C.2    Hobman, J.L.3    Minchin, S.D.4
  • 73
    • 29144431508 scopus 로고    scopus 로고
    • Studies of the distribution of Escherichia coli cAMP-receptor protein and RNA polymerase along the E. coli chromosome
    • Grainger, D.C., Hurd, D., Harrison, M., Holdstock, J., and Busby, S.J. (2005) Studies of the distribution of Escherichia coli cAMP-receptor protein and RNA polymerase along the E. coli chromosome. Proc. Natl. Acad. Sci. USA, 102, 17693-17698.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17693-17698
    • Grainger, D.C.1    Hurd, D.2    Harrison, M.3    Holdstock, J.4    Busby, S.J.5
  • 74
    • 0032573426 scopus 로고    scopus 로고
    • A comprehensive library of DNA-binding site matrices for 55 proteins applied to the complete Escherichia coli K-12 genome
    • Robison,K., McGuire, A.M., andChurch, G.M. (1998) A comprehensive library of DNA-binding site matrices for 55 proteins applied to the complete Escherichia coli K-12 genome. J. Mol. Biol., 284, 241-254.
    • (1998) J. Mol. Biol. , vol.284 , pp. 241-254
    • Robison, K.1    McGuire, A.M.2    Church, G.M.3
  • 76
    • 0023105965 scopus 로고
    • Indirect role of adenylate cyclase and cyclic AMP in chemotaxis to phosphotransferase system carbohydrates in Escherichia coli K-12
    • Vogler, A.P. and Lengeler, J.W. (1987) Indirect role of adenylate cyclase and cyclic AMP in chemotaxis to phosphotransferase system carbohydrates in Escherichia coli K-12. J. Bacteriol., 169, 593-599.
    • (1987) J. Bacteriol. , vol.169 , pp. 593-599
    • Vogler, A.P.1    Lengeler, J.W.2
  • 77
    • 34547394297 scopus 로고    scopus 로고
    • New targets for the cyclic AMP receptor protein in the Escherichia coli K-12 genome
    • Hollands, K., Busby, S.J., and Lloyd, G.S. (2007) New targets for the cyclic AMP receptor protein in the Escherichia coli K-12 genome. FEMS Microbiol. Lett., 274, 89-94.
    • (2007) FEMS Microbiol. Lett. , vol.274 , pp. 89-94
    • Hollands, K.1    Busby, S.J.2    Lloyd, G.S.3
  • 78
    • 34247146736 scopus 로고    scopus 로고
    • Interplay between CRP-cAMP and PII-Ntr systems forms novel regulatory network between carbon metabolism and nitrogen assimilation in Escherichia coli
    • Mao, X.J., Huo, Y.X., Buck, M., Kolb, A., and Wang, Y.P. (2007) Interplay between CRP-cAMP and PII-Ntr systems forms novel regulatory network between carbon metabolism and nitrogen assimilation in Escherichia coli. Nucleic Acids Res., 35, 1432-1440.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 1432-1440
    • Mao, X.J.1    Huo, Y.X.2    Buck, M.3    Kolb, A.4    Wang, Y.P.5
  • 79
    • 33748660467 scopus 로고    scopus 로고
    • Cyclic AMP-dependent osmoregulation of crp gene expression in Escherichia coli
    • Balsalobre, C., Johansson, J., and Uhlin, B.E. (2006) Cyclic AMP-dependent osmoregulation of crp gene expression in Escherichia coli. J. Bacteriol., 188, 5935-5944.
    • (2006) J. Bacteriol. , vol.188 , pp. 5935-5944
    • Balsalobre, C.1    Johansson, J.2    Uhlin, B.E.3
  • 81
    • 0029016352 scopus 로고
    • Control of glucose metabolism by the enzymes of the glucose phosphotransferase system in Salmonella typhimurium
    • van der Vlag, J., van't Hof, R., van Dam, K., and Postma, P.W. (1995) Control of glucose metabolism by the enzymes of the glucose phosphotransferase system in Salmonella typhimurium. Eur. J. Biochem., 230, 170-182.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 170-182
    • van der Vlag, J.1    van't Hof, R.2    van Dam, K.3    Postma, P.W.4
  • 82
    • 85007744911 scopus 로고
    • Decreasing accumulation of acetate in a rich medium by Escherichia coli on introduction of genes on a multicopy plasmid
    • Hosono, K., Kakuda, H., and Ichihara, S. (1995) Decreasing accumulation of acetate in a rich medium by Escherichia coli on introduction of genes on a multicopy plasmid. Biosci. Biotechnol. Biochem., 59, 256-261.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 256-261
    • Hosono, K.1    Kakuda, H.2    Ichihara, S.3
  • 83
    • 0034675992 scopus 로고    scopus 로고
    • Signal transduction between a membrane-bound transporter, PtsG, and a soluble transcription factor, Mlc, of Escherichia coli
    • Lee, S.J., Boos, W., Bouche, J.P., and Plumbridge, J. (2000) Signal transduction between a membrane-bound transporter, PtsG, and a soluble transcription factor, Mlc, of Escherichia coli. EMBO J., 19, 5353-5361.
    • (2000) EMBO J. , vol.19 , pp. 5353-5361
    • Lee, S.J.1    Boos, W.2    Bouche, J.P.3    Plumbridge, J.4
  • 85
    • 0034675924 scopus 로고    scopus 로고
    • A novel regulatory role of glucose transporter of Escherichia coli: membrane sequestration of a global repressor Mlc
    • Tanaka, Y., Kimata, K., and Aiba, H. (2000) A novel regulatory role of glucose transporter of Escherichia coli: membrane sequestration of a global repressor Mlc. EMBO J., 19, 5344-5352.
    • (2000) EMBO J. , vol.19 , pp. 5344-5352
    • Tanaka, Y.1    Kimata, K.2    Aiba, H.3
  • 87
    • 2342588097 scopus 로고    scopus 로고
    • Modeling and experimental validation of the signal transduction via the Escherichia coli sucrose phosphotransferase system
    • Sauter, T. and Gilles, E.D. (2004) Modeling and experimental validation of the signal transduction via the Escherichia coli sucrose phosphotransferase system. J. Biotechnol., 110, 181-199.
    • (2004) J. Biotechnol. , vol.110 , pp. 181-199
    • Sauter, T.1    Gilles, E.D.2
  • 88
    • 0037973668 scopus 로고    scopus 로고
    • Why the phosphotransferase system of Escherichia coli escapes diffusion limitation
    • Francke, C.P.P., Westerhoff, H.V., Blom, J.G., and Peletier, M.A. (2002) Why the phosphotransferase system of Escherichia coli escapes diffusion limitation. Biophys. J., 85, 612-622.
    • (2002) Biophys. J. , vol.85 , pp. 612-622
    • Francke, C.P.P.1    Westerhoff, H.V.2    Blom, J.G.3    Peletier, M.A.4
  • 90
    • 0347670033 scopus 로고    scopus 로고
    • Regulation of glycogen concentration by the histidine-containing phosphocarrier protein HPr in Escherichia coli
    • Koo, B.M. and Seok, Y.-J. (2001) Regulation of glycogen concentration by the histidine-containing phosphocarrier protein HPr in Escherichia coli. J. Microbiol., 39, 24-30.
    • (2001) J. Microbiol. , vol.39 , pp. 24-30
    • Koo, B.M.1    Seok, Y.-J.2
  • 92
    • 33746636058 scopus 로고    scopus 로고
    • YeeI, a novel protein involved in modulation of the activity of the glucosephosphotransferase system in Escherichia coli K-12
    • Becker, A.K., Zeppenfeld, T., Staab, A., Seitz, S., Boos, W., Morita, T., Aiba, H., Mahr, K., Titgemeyer, F., and Jahreis, K. (2006) YeeI, a novel protein involved in modulation of the activity of the glucosephosphotransferase system in Escherichia coli K-12. J. Bacteriol., 188, 5439-5449.
    • (2006) J. Bacteriol. , vol.188 , pp. 5439-5449
    • Becker, A.K.1    Zeppenfeld, T.2    Staab, A.3    Seitz, S.4    Boos, W.5    Morita, T.6    Aiba, H.7    Mahr, K.8    Titgemeyer, F.9    Jahreis, K.10
  • 93
    • 38049115217 scopus 로고    scopus 로고
    • A dual function for a bacterial small RNA: SgrS performs base pairing-dependent regulation and encodes a functional polypeptide
    • Wadler, C. and Vanderpool, C.K. (2007) A dual function for a bacterial small RNA: SgrS performs base pairing-dependent regulation and encodes a functional polypeptide. Proc. Natl. Acad. Sci. USA, 104, 20454-20459.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20454-20459
    • Wadler, C.1    Vanderpool, C.K.2


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