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Volumn 16, Issue 9, 2000, Pages 404-409

Learning new tricks from an old dog: MalT of the Escherichia coli maltose system is part of a complex regulatory network

Author keywords

[No Author keywords available]

Indexed keywords

4ALPHA GLUCANOTRANSFERASE; ABC TRANSPORTER; AMYLASE; CYCLIC AMP BINDING PROTEIN; GLUCOSE; GLUCOSE 1 PHOSPHATE; GLUCOSIDASE; MALTODEXTRIN; MALTOPORIN; MALTOSE; MALTOTRIOSE; PHOSPHORYLASE; UNCLASSIFIED DRUG;

EID: 0034283843     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9525(00)02086-2     Document Type: Review
Times cited : (57)

References (42)
  • 1
    • 54249116230 scopus 로고
    • Genetic regulatory mechanisms in the synthesis of proteins
    • Jacob, F. and Monod, J. (1961) Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 3, 318-356
    • (1961) J. Mol. Biol. , vol.3 , pp. 318-356
    • Jacob, F.1    Monod, J.2
  • 3
    • 0031887807 scopus 로고    scopus 로고
    • The maltose/maltodextrin system of Escherichia coli; transport, metabolism and regulation
    • Boos, W. and Shuman, H.A. (1998) The maltose/maltodextrin system of Escherichia coli; transport, metabolism and regulation. Microbiol. Mol. Biol. Rev. 62, 204-229
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 204-229
    • Boos, W.1    Shuman, H.A.2
  • 4
    • 0031046574 scopus 로고    scopus 로고
    • Identification and characterization of acoK, a regulatory gene of the Klebsiella pneumoniae acoABCD operon
    • Peng, H-L. et al. (1997) Identification and characterization of acoK, a regulatory gene of the Klebsiella pneumoniae acoABCD operon. J. Bacteriol. 179, 1497-1504
    • (1997) J. Bacteriol. , vol.179 , pp. 1497-1504
    • Peng, H.-L.1
  • 5
    • 0024424649 scopus 로고
    • MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator
    • Richet, E. and Raibaud, O. (1989) MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator. EMBO J. 8, 981-987
    • (1989) EMBO J. , vol.8 , pp. 981-987
    • Richet, E.1    Raibaud, O.2
  • 6
    • 0001014412 scopus 로고    scopus 로고
    • Phosphoenolpyruvate:Carbohydrate phosphotransferase system
    • (Neidhardt, F.C. et al., eds), American Society of Microbiology
    • Postma, P.W. et al. (1996) Phosphoenolpyruvate:Carbohydrate phosphotransferase system. In Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology (Neidhardt, F.C. et al., eds), pp. 1149-1174, American Society of Microbiology
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 1149-1174
    • Postma, P.W.1
  • 7
    • 0031983641 scopus 로고    scopus 로고
    • Negative transcriptional regulation of a positive regulator: The expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc
    • Decker, K. et al. (1998) Negative transcriptional regulation of a positive regulator: The expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc. Mol. Microbiol. 27, 381-390
    • (1998) Mol. Microbiol. , vol.27 , pp. 381-390
    • Decker, K.1
  • 8
    • 0033585068 scopus 로고    scopus 로고
    • Self-association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP
    • Schreiber, V. and Richet, E. (1999) Self-association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP. J. Biol. Chem. 274, 33220-33226
    • (1999) J. Biol. Chem. , vol.274 , pp. 33220-33226
    • Schreiber, V.1    Richet, E.2
  • 9
    • 0023656085 scopus 로고
    • Purification and properties of the MalT protein, the transcription activator of the Escherichia coli maltose regulon
    • Richet, E. and Raibaud, O. (1987) Purification and properties of the MalT protein, the transcription activator of the Escherichia coli maltose regulon. J. Biol. Chem. 262, 12647-12653
    • (1987) J. Biol. Chem. , vol.262 , pp. 12647-12653
    • Richet, E.1    Raibaud, O.2
  • 10
    • 0027943595 scopus 로고
    • Multiple protein-DNA and protein-protein interactions are involved in transcriptional activation by MalT
    • Danot, O. and Raibaud, O. (1994) Multiple protein - DNA and protein - protein interactions are involved in transcriptional activation by MalT. Mol. Microbiol. 14, 335-346
    • (1994) Mol. Microbiol. , vol.14 , pp. 335-346
    • Danot, O.1    Raibaud, O.2
  • 11
    • 0025849091 scopus 로고
    • Two MalT binding sites in direct repeat. A structural motif involved in the activation of all the promoters of the maltose regulons in Escherichia coli and Klebsiella pneumoniae
    • Vidal-Ingigliardi, D. et al. (1991) Two MalT binding sites in direct repeat. A structural motif involved in the activation of all the promoters of the maltose regulons in Escherichia coli and Klebsiella pneumoniae. J. Mol. Biol. 218, 323-334
    • (1991) J. Mol. Biol. , vol.218 , pp. 323-334
    • Vidal-Ingigliardi, D.1
  • 12
    • 0030582422 scopus 로고    scopus 로고
    • Two amino acid residues from the DNA-binding domain of MalT play a crucial role in transcriptional activation
    • Danot, O. et al. (1996) Two amino acid residues from the DNA-binding domain of MalT play a crucial role in transcriptional activation. J. Mol. Biol. 262, 1-11
    • (1996) J. Mol. Biol. , vol.262 , pp. 1-11
    • Danot, O.1
  • 13
    • 0001769249 scopus 로고    scopus 로고
    • Periplasmic binding protein-dependent ABC transporters
    • Neidhardt, F.C. et al., eds., American Society of Microbiology
    • Boos, W. and Lucht, J.M. (1996) Periplasmic binding protein-dependent ABC transporters. In Escherichia Coli and Salmonella Typhimurium; Cellular and Molecular Biology (Neidhardt, F.C. et al., eds.), pp. 1175-1209, American Society of Microbiology
    • (1996) Escherichia Coli and Salmonella Typhimurium; Cellular and Molecular Biology , pp. 1175-1209
    • Boos, W.1    Lucht, J.M.2
  • 14
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits
    • Mourez, M. et al. (1997) Subunit interactions in ABC transporters: A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits. EMBO J. 16, 3066-3077
    • (1997) EMBO J. , vol.16 , pp. 3066-3077
    • Mourez, M.1
  • 15
    • 0026549522 scopus 로고
    • Mechanism of maltose transport in Escherichia coli
    • Transmembrane signaling by periplasmic binding proteins
    • Davidson, A.L. et al. (1992) Mechanism of maltose transport in Escherichia coli. Transmembrane signaling by periplasmic binding proteins. Proc. Natl. Acad. Sci. U. S. A. 89, 2360-2364
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 2360-2364
    • Davidson, A.L.1
  • 16
    • 0025904264 scopus 로고
    • The activities of the Escherichia coli MalK protein in maltose transport, regulation and inducer exclusion can be separated by mutations
    • Kühnau, S. et al. (1991) The activities of the Escherichia coli MalK protein in maltose transport, regulation and inducer exclusion can be separated by mutations. J. Bacteriol. 173, 2180-2186
    • (1991) J. Bacteriol. , vol.173 , pp. 2180-2186
    • Kühnau, S.1
  • 17
    • 0024095619 scopus 로고
    • Overproduction of MalK protein prevents expression of the Escherichia coli mal regulon
    • Reyes, M. and Shuman, H.A. (1988) Overproduction of MalK protein prevents expression of the Escherichia coli mal regulon. J. Bacteriol. 170, 4598-4602
    • (1988) J. Bacteriol. , vol.170 , pp. 4598-4602
    • Reyes, M.1    Shuman, H.A.2
  • 18
    • 0031704443 scopus 로고    scopus 로고
    • Domain structure of the ATP-binding-cassette protein MalK of Salmonella typhimurium as assessed by coexpressed half molecules and LacK'-'MalK chimeras
    • Schmees, G. and Schneider, E. (1998) Domain structure of the ATP-binding-cassette protein MalK of Salmonella typhimurium as assessed by coexpressed half molecules and LacK'-'MalK chimeras. J. Bacteriol. 180, 5299-5305
    • (1998) J. Bacteriol. , vol.180 , pp. 5299-5305
    • Schmees, G.1    Schneider, E.2
  • 19
    • 0031768746 scopus 로고    scopus 로고
    • The ATP-binding cassette subunit of the maltose transporter MalK antagonizes MalT, the activator of the Escherichia coli mal regulon
    • Panagiotidis, C.H. et al. (1998) The ATP-binding cassette subunit of the maltose transporter MalK antagonizes MalT, the activator of the Escherichia coli mal regulon. Mol. Microbiol. 30, 535-546
    • (1998) Mol. Microbiol. , vol.30 , pp. 535-546
    • Panagiotidis, C.H.1
  • 20
    • 0023394131 scopus 로고
    • Identification of endogenous inducers of the mal system in Escherichia coli
    • Ehrmann, M. and Boos, W. (1987) Identification of endogenous inducers of the mal system in Escherichia coli. J. Bacteriol. 169, 3539-3545
    • (1987) J. Bacteriol. , vol.169 , pp. 3539-3545
    • Ehrmann, M.1    Boos, W.2
  • 21
    • 0024729941 scopus 로고
    • Mall, a novel protein involved in regulation of the maltose system of Escherichia coli, is highly homologous to the repressor proteins GalR, CytR, and Lacl
    • Reidl, J. et al. (1989) Mall, a novel protein involved in regulation of the maltose system of Escherichia coli, is highly homologous to the repressor proteins GalR, CytR, and Lacl. J. Bacteriol. 171, 4888-4899
    • (1989) J. Bacteriol. , vol.171 , pp. 4888-4899
    • Reidl, J.1
  • 22
    • 0025848324 scopus 로고
    • The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system
    • Reidl, J. and Boos, W. (1991) The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system. J. Bacteriol. 173, 4862-4876
    • (1991) J. Bacteriol. , vol.173 , pp. 4862-4876
    • Reidl, J.1    Boos, W.2
  • 23
    • 0029127483 scopus 로고
    • MalY of Escherichia coli is an enzyme with the activity of a βC-S lyase (cystathionase)
    • Zdych, E. et al. (1995) MalY of Escherichia coli is an enzyme with the activity of a βC-S lyase (cystathionase). J. Bacteriol. 177, 5035-5039
    • (1995) J. Bacteriol. , vol.177 , pp. 5035-5039
    • Zdych, E.1
  • 24
    • 0033968803 scopus 로고    scopus 로고
    • A new mechanism for the control of a prokaryotic transcriptional regulator: Antagonistic binding of positive and negative effectors
    • Schreiber, V. et al. (2000) A new mechanism for the control of a prokaryotic transcriptional regulator: Antagonistic binding of positive and negative effectors. Mol. Microbiol. 35, 765-776
    • (2000) Mol. Microbiol. , vol.35 , pp. 765-776
    • Schreiber, V.1
  • 25
    • 0034161568 scopus 로고    scopus 로고
    • X-ray structure of MalY from Escherichia coli: A pyridoxal 5′-phosphate-dependent enzyme acting as a modulator in mal gene expression
    • Clausen, T. et al. (2000) X-ray structure of MalY from Escherichia coli: A pyridoxal 5′-phosphate-dependent enzyme acting as a modulator in mal gene expression. EMBO J. 19, 831-842
    • (2000) EMBO J. , vol.19 , pp. 831-842
    • Clausen, T.1
  • 26
    • 0030463224 scopus 로고    scopus 로고
    • Sugar transport by the marine chitinolytic bacterium Vibrio furnissii
    • Molecular cloning and analysis of the glucose and N-acetylglucosamine permeases
    • Bouma, C.L. and Roseman, S. (1996) Sugar transport by the marine chitinolytic bacterium Vibrio furnissii. Molecular cloning and analysis of the glucose and N-acetylglucosamine permeases. J. Biol. Chem. 271, 33457-33467
    • (1996) J. Biol. Chem. , vol.271 , pp. 33457-33467
    • Bouma, C.L.1    Roseman, S.2
  • 27
  • 28
    • 0030781626 scopus 로고    scopus 로고
    • Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity
    • Peist, R. et al. (1997) Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity. J. Bacteriol. 179, 7679-7686
    • (1997) J. Bacteriol. , vol.179 , pp. 7679-7686
    • Peist, R.1
  • 29
    • 0014149432 scopus 로고
    • Sur l'existence chez Escherichia coli K12 d'une régulation commune à la biosynthèse des récepteurs du bacteriophage l et au métabolisme du maltose
    • Schwartz, M. (1967) Sur l'existence chez Escherichia coli K12 d'une régulation commune à la biosynthèse des récepteurs du bacteriophage l et au métabolisme du maltose. Ann. Inst. Pasteur Microbiol. 113, 687-704
    • (1967) Ann. Inst. Pasteur Microbiol. , vol.113 , pp. 687-704
    • Schwartz, M.1
  • 30
    • 0027536158 scopus 로고
    • Induction of the λ receptor is essential for the effective uptake of trehalose in Escherichia coli
    • Klein, W. and Boos, W. (1993) Induction of the λ receptor is essential for the effective uptake of trehalose in Escherichia coli. J. Bacteriol. 175, 1682-1686
    • (1993) J. Bacteriol. , vol.175 , pp. 1682-1686
    • Klein, W.1    Boos, W.2
  • 31
    • 0028061196 scopus 로고
    • Trehalose-6-phosphate hydrolase of Escherichia coli
    • Rimmele, M. and Boos, W. (1994) Trehalose-6-phosphate hydrolase of Escherichia coli. J. Bacteriol. 176, 5654-5664
    • (1994) J. Bacteriol. , vol.176 , pp. 5654-5664
    • Rimmele, M.1    Boos, W.2
  • 32
    • 0033047695 scopus 로고    scopus 로고
    • The role of the trehalose system in regulating the maltose regulon of Escherichia coli
    • Decker, K. et al. (1999) The role of the trehalose system in regulating the maltose regulon of Escherichia coli. Mol. Microbiol. 32, 777-788
    • (1999) Mol. Microbiol. , vol.32 , pp. 777-788
    • Decker, K.1
  • 33
    • 0027457784 scopus 로고
    • Derepression of LamB protein facilitates outer membrane permeation of carbohydrates into Escherichia coli under conditions of nutrient stress
    • Death, A. et al. (1993) Derepression of LamB protein facilitates outer membrane permeation of carbohydrates into Escherichia coli under conditions of nutrient stress. J. Bacteriol. 175, 1475-1483
    • (1993) J. Bacteriol. , vol.175 , pp. 1475-1483
    • Death, A.1
  • 34
    • 0033068946 scopus 로고    scopus 로고
    • The generation of multiple co-existing mal-regulatory mutations through polygenic evolution in glucose-limited populations of Escherichia coli
    • Notley-McRobb, L. and Ferenci, T. (1999) The generation of multiple co-existing mal-regulatory mutations through polygenic evolution in glucose-limited populations of Escherichia coli. Environ. Microbiol. 1, 45-52
    • (1999) Environ. Microbiol. , vol.1 , pp. 45-52
    • Notley-McRobb, L.1    Ferenci, T.2
  • 35
    • 0027200708 scopus 로고
    • Maltose and maltotriose can be formed endogenously in Escherichia coli from glucose and glucose-1-phosphate independently of enzymes of the maltose system
    • Decker, K. et al. (1993) Maltose and maltotriose can be formed endogenously in Escherichia coli from glucose and glucose-1-phosphate independently of enzymes of the maltose system. J. Bacteriol. 175, 5655-5665
    • (1993) J. Bacteriol. , vol.175 , pp. 5655-5665
    • Decker, K.1
  • 36
    • 0026739805 scopus 로고
    • Modulation of the dimerization of a transcriptional antiterminator protein by phosphorylation
    • Amster-Choder, O. and Wright, A. (1992) Modulation of the dimerization of a transcriptional antiterminator protein by phosphorylation. Science 257, 1395-1398
    • (1992) Science , vol.257 , pp. 1395-1398
    • Amster-Choder, O.1    Wright, A.2
  • 37
    • 0031035649 scopus 로고    scopus 로고
    • Transcription induction of the ferric citrate transport genes via the N-terminus of the FecA outer membrane protein, the ton system and the electrochemical potential of the cytoplasmic membrane
    • Kim, I. et al. (1997) Transcription induction of the ferric citrate transport genes via the N-terminus of the FecA outer membrane protein, the ton system and the electrochemical potential of the cytoplasmic membrane. Mol. Microbiol. 23, 333-344
    • (1997) Mol. Microbiol. , vol.23 , pp. 333-344
    • Kim, I.1
  • 38
    • 0030976040 scopus 로고    scopus 로고
    • Regulation of gene expression by repressor localization: Biochemical evidence that membrane and DNA binding by the PutA protein are mutually exclusive
    • Muro-Pastor, A.M. et al. (1997) Regulation of gene expression by repressor localization: Biochemical evidence that membrane and DNA binding by the PutA protein are mutually exclusive. J. Bacteriol. 179, 2788-2791
    • (1997) J. Bacteriol. , vol.179 , pp. 2788-2791
    • Muro-Pastor, A.M.1
  • 39
    • 0033062699 scopus 로고    scopus 로고
    • Expression of the phosphotransferase system both mediates and is mediated by Mlc regulation in Escherichia coli
    • Plumbridge, J. (1999) Expression of the phosphotransferase system both mediates and is mediated by Mlc regulation in Escherichia coli. Mol. Microbiol. 33, 260-273
    • (1999) Mol. Microbiol. , vol.33 , pp. 260-273
    • Plumbridge, J.1
  • 40
    • 0031738688 scopus 로고    scopus 로고
    • Identification of a co-repressor binding site in catabolite control protein CcpA
    • Kraus, A. et al. (1998) Identification of a co-repressor binding site in catabolite control protein CcpA. Mol. Microbiol. 30, 955-963
    • (1998) Mol. Microbiol. , vol.30 , pp. 955-963
    • Kraus, A.1


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