메뉴 건너뛰기




Volumn 82, Issue 2, 2014, Pages 268-277

Structural and mutational analyses of Aes, an inhibitor of MalT in Escherichia coli

Author keywords

Acyl esterase; Aes; Inhibition of MalT; MalT dependent regulation; Site directed mutagenesis; X ray crystallography

Indexed keywords

ACYL ESTERASE; ALPHA HYDROLASE; ASPARTIC ACID; BACTERIAL PROTEIN; BETA HYDROLASE; DIMER; ESTERASE; HISTIDINE; HOMODIMER; MALTODEXTRIN; MALTOSE; PROTEIN MALT; SERINE; SULFONE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84892672372     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24383     Document Type: Article
Times cited : (6)

References (48)
  • 1
    • 0023192487 scopus 로고
    • Maltotriose is the inducer of the maltose regulon of Escherichia coli
    • Raibaud O, Richet E. Maltotriose is the inducer of the maltose regulon of Escherichia coli. J Bacteriol 1987;169(7):3059-3061.
    • (1987) J Bacteriol , vol.169 , Issue.7 , pp. 3059-3061
    • Raibaud, O.1    Richet, E.2
  • 2
    • 0034597003 scopus 로고    scopus 로고
    • Synergistic transcription activation: a dual role for CRP in the activation of an Escherichia coli promoter depending on MalT and CRP
    • Richet E. Synergistic transcription activation: a dual role for CRP in the activation of an Escherichia coli promoter depending on MalT and CRP. EMBO J 2000;19(19):5222-5232.
    • (2000) EMBO J , vol.19 , Issue.19 , pp. 5222-5232
    • Richet, E.1
  • 3
    • 0024424649 scopus 로고
    • MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator
    • Richet E, Raibaud O. MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator. EMBO J 1989;8(3):981-987.
    • (1989) EMBO J , vol.8 , Issue.3 , pp. 981-987
    • Richet, E.1    Raibaud, O.2
  • 4
    • 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, Plumbridge J, Boos W. 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 1998;27(2):381-390.
    • (1998) Mol Microbiol , vol.27 , Issue.2 , pp. 381-390
    • Decker, K.1    Plumbridge, J.2    Boos, W.3
  • 5
    • 0034675992 scopus 로고    scopus 로고
    • Signal transduction between a membrane-bound |transporter, PtsG, and a soluble transcription factor, Mlc, of Escherichia coli
    • Lee SJ, Boos W, Bouche JP, Plumbridge J. Signal transduction between a membrane-bound |transporter, PtsG, and a soluble transcription factor, Mlc, of Escherichia coli. EMBO J 2000;19(20):5353-5361.
    • (2000) EMBO J , vol.19 , Issue.20 , pp. 5353-5361
    • Lee, S.J.1    Boos, W.2    Bouche, J.P.3    Plumbridge, J.4
  • 6
    • 0037855776 scopus 로고    scopus 로고
    • Analysis of the interaction between the global regulator Mlc and EIIBGlc of the glucose-specific phosphotransferase system in Escherichia coli
    • Seitz S, Lee SJ, Pennetier C, Boos W, Plumbridge J. Analysis of the interaction between the global regulator Mlc and EIIBGlc of the glucose-specific phosphotransferase system in Escherichia coli. J Biol Chem 2003;278(12):10744-10751.
    • (2003) J Biol Chem , vol.278 , Issue.12 , pp. 10744-10751
    • Seitz, S.1    Lee, S.J.2    Pennetier, C.3    Boos, W.4    Plumbridge, J.5
  • 7
    • 1842610493 scopus 로고    scopus 로고
    • Gene regulation in prokaryotes by subcellular relocalization of transcription factors
    • Böhm A, Boos W. Gene regulation in prokaryotes by subcellular relocalization of transcription factors. Curr Opin Microbiol 2004;7(2):151-156.
    • (2004) Curr Opin Microbiol , vol.7 , Issue.2 , pp. 151-156
    • Böhm, A.1    Boos, W.2
  • 8
    • 0034283843 scopus 로고    scopus 로고
    • Learning new tricks from an old dog: MalT of the Escherichia coli maltose system is part of a complex regulatory network
    • Boos W, Böhm A. Learning new tricks from an old dog: MalT of the Escherichia coli maltose system is part of a complex regulatory network. Trends Genet 2000;16(9):404-409.
    • (2000) Trends Genet , vol.16 , Issue.9 , pp. 404-409
    • Boos, W.1    Böhm, A.2
  • 9
    • 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, Steegborn C, Clausen T, Boos W, Richet E. A new mechanism for the control of a prokaryotic transcriptional regulator: antagonistic binding of positive and negative effectors. Mol Microbiol 2000;35(4):765-776.
    • (2000) Mol Microbiol , vol.35 , Issue.4 , pp. 765-776
    • Schreiber, V.1    Steegborn, C.2    Clausen, T.3    Boos, W.4    Richet, E.5
  • 10
    • 0031887807 scopus 로고    scopus 로고
    • Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation
    • Boos W, Shuman H. Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation. Microbiol Mol Biol Rev 1998;62(1):204-229.
    • (1998) Microbiol Mol Biol Rev , vol.62 , Issue.1 , pp. 204-229
    • Boos, W.1    Shuman, H.2
  • 11
    • 0020320406 scopus 로고
    • Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane
    • Shuman HA. Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane. J Biol Chem 1982;257(10):5455-5461.
    • (1982) J Biol Chem , vol.257 , Issue.10 , pp. 5455-5461
    • Shuman, H.A.1
  • 12
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen J, Lu G, Lin J, Davidson AL, Quiocho FA. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol Cell 2003;12(3):651-661.
    • (2003) Mol Cell , vol.12 , Issue.3 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 13
    • 0034669176 scopus 로고    scopus 로고
    • Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis
    • Diederichs K, Diez J, Greller G, Müller C, Breed J, Schnell C, Vonrhein C, Boos W, Welte W. Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. EMBO J 2000;19(22):5951-5961.
    • (2000) EMBO J , vol.19 , Issue.22 , pp. 5951-5961
    • Diederichs, K.1    Diez, J.2    Greller, G.3    Müller, C.4    Breed, J.5    Schnell, C.6    Vonrhein, C.7    Boos, W.8    Welte, W.9
  • 14
    • 0036479107 scopus 로고    scopus 로고
    • Structural model of MalK, the ABC subunit of the maltose transporter of Escherichia coli: implications for mal gene regulation, inducer exclusion, and subunit assembly
    • Böhm A, Diez J, Diederichs K, Welte W, Boos W. Structural model of MalK, the ABC subunit of the maltose transporter of Escherichia coli: implications for mal gene regulation, inducer exclusion, and subunit assembly. J Biol Chem 2002;277(5):3708-3717.
    • (2002) J Biol Chem , vol.277 , Issue.5 , pp. 3708-3717
    • Böhm, A.1    Diez, J.2    Diederichs, K.3    Welte, W.4    Boos, W.5
  • 15
    • 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, Reyes M, Sievertsen A, Shuman HA, Boos W. The activities of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations. J Bacteriol 1991;173(7):2180-2186.
    • (1991) J Bacteriol , vol.173 , Issue.7 , pp. 2180-2186
    • Kühnau, S.1    Reyes, M.2    Sievertsen, A.3    Shuman, H.A.4    Boos, W.5
  • 16
    • 84864799816 scopus 로고    scopus 로고
    • The ABC transporter MalFGK(2) sequesters the MalT transcription factor at the membrane in the absence of cognate substrate
    • Richet E, Davidson AL, Joly N. The ABC transporter MalFGK(2) sequesters the MalT transcription factor at the membrane in the absence of cognate substrate. Mol Microbiol 2012;85(4):632-647.
    • (2012) Mol Microbiol , vol.85 , Issue.4 , pp. 632-647
    • Richet, E.1    Davidson, A.L.2    Joly, N.3
  • 17
    • 4043050193 scopus 로고    scopus 로고
    • MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator MalT by antagonizing inducer binding
    • Joly N, Böhm A, Boos W, Richet E. MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator MalT by antagonizing inducer binding. J Biol Chem 2004;279(32):33123-33130.
    • (2004) J Biol Chem , vol.279 , Issue.32 , pp. 33123-33130
    • Joly, N.1    Böhm, A.2    Boos, W.3    Richet, E.4
  • 18
    • 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 CH, Boos W, Shuman HA. The ATP-binding cassette subunit of the maltose transporter MalK antagonizes MalT, the activator of the Escherichia coli mal regulon. Mol Microbiol 1998;30(3):535-546.
    • (1998) Mol Microbiol , vol.30 , Issue.3 , pp. 535-546
    • Panagiotidis, C.H.1    Boos, W.2    Shuman, H.A.3
  • 19
    • 14144251709 scopus 로고    scopus 로고
    • Two domains of MalT, the activator of the Escherichia coli maltose regulon, bear determinants essential for anti-activation by MalK
    • Richet E, Joly N, Danot O. Two domains of MalT, the activator of the Escherichia coli maltose regulon, bear determinants essential for anti-activation by MalK. J Mol Biol 2005;347(1):1-10.
    • (2005) J Mol Biol , vol.347 , Issue.1 , pp. 1-10
    • Richet, E.1    Joly, N.2    Danot, O.3
  • 20
    • 0036096732 scopus 로고    scopus 로고
    • The N-terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY
    • Schlegel A, Danot O, Richet E, Ferenci T, Boos W. The N-terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY. J Bacteriol 2002;184(11):3069-3077.
    • (2002) J Bacteriol , vol.184 , Issue.11 , pp. 3069-3077
    • Schlegel, A.1    Danot, O.2    Richet, E.3    Ferenci, T.4    Boos, W.5
  • 21
    • 0029127483 scopus 로고
    • MalY of Escherichia coli is an enzyme with the activity of a beta C-S lyase (cystathionase)
    • Zdych E, Peist R, Reidl J, Boos W. MalY of Escherichia coli is an enzyme with the activity of a beta C-S lyase (cystathionase). J Bacteriol 1995;177(17):5035-5039.
    • (1995) J Bacteriol , vol.177 , Issue.17 , pp. 5035-5039
    • Zdych, E.1    Peist, R.2    Reidl, J.3    Boos, W.4
  • 23
    • 0030781626 scopus 로고    scopus 로고
    • Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity
    • Peist R, Koch A, Bolek P, Sewitz S, Kolbus T, Boos W. Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity. J Bacteriol 1997;179(24):7679-7686.
    • (1997) J Bacteriol , vol.179 , Issue.24 , pp. 7679-7686
    • Peist, R.1    Koch, A.2    Bolek, P.3    Sewitz, S.4    Kolbus, T.5    Boos, W.6
  • 24
    • 0037053363 scopus 로고    scopus 로고
    • The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon
    • Joly N, Danot O, Schlegel A, Boos W, Richet E. The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon. J Biol Chem 2002;277(19):16606-16613.
    • (2002) J Biol Chem , vol.277 , Issue.19 , pp. 16606-16613
    • Joly, N.1    Danot, O.2    Schlegel, A.3    Boos, W.4    Richet, E.5
  • 25
    • 2242442625 scopus 로고    scopus 로고
    • The Aes protein and the monomeric α-galactosidase from Escherichia coli form a non-covalent complex. Implications for the regulation of carbohydrate metabolism
    • Mandrich L, Caputo E, Martin BM, Rossi M, Manco G. The Aes protein and the monomeric α-galactosidase from Escherichia coli form a non-covalent complex. Implications for the regulation of carbohydrate metabolism. J Biol Chem 2002;277(50):48241-48247.
    • (2002) J Biol Chem , vol.277 , Issue.50 , pp. 48241-48247
    • Mandrich, L.1    Caputo, E.2    Martin, B.M.3    Rossi, M.4    Manco, G.5
  • 26
    • 0032524205 scopus 로고    scopus 로고
    • An esterase from Escherichia coli with a sequence similarity to hormone-sensitive lipase
    • Kanaya S, Koyanagi T, Kanaya E. An esterase from Escherichia coli with a sequence similarity to hormone-sensitive lipase. Biochem J 1998;332(Pt 1):75-80.
    • (1998) Biochem J , vol.332 , Issue.PART 1 , pp. 75-80
    • Kanaya, S.1    Koyanagi, T.2    Kanaya, E.3
  • 27
    • 0032974477 scopus 로고    scopus 로고
    • Identification of catalytically essential residues in Escherichia coli esterase by site-directed mutagenesis
    • Haruki M, Oohashi Y, Mizuguchi S, Matsuo Y, Morikawa M, Kanaya S. Identification of catalytically essential residues in Escherichia coli esterase by site-directed mutagenesis. FEBS Lett 1999;454(3):262-266.
    • (1999) FEBS Lett , vol.454 , Issue.3 , pp. 262-266
    • Haruki, M.1    Oohashi, Y.2    Mizuguchi, S.3    Matsuo, Y.4    Morikawa, M.5    Kanaya, S.6
  • 35
    • 0021866359 scopus 로고
    • Transposable λ placMu bacteriophages for creating lacZ operon fusions and kanamycin resistance insertions in Escherichia coli
    • Bremer E, Silhavy TJ, Weinstock GM. Transposable λ placMu bacteriophages for creating lacZ operon fusions and kanamycin resistance insertions in Escherichia coli. J Bacteriol 1985;162(3):1092-1099.
    • (1985) J Bacteriol , vol.162 , Issue.3 , pp. 1092-1099
    • Bremer, E.1    Silhavy, T.J.2    Weinstock, G.M.3
  • 36
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller JH. Experiments in molecular genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press; 1972.
    • (1972) Experiments in molecular genetics
    • Miller, J.H.1
  • 38
    • 84865274509 scopus 로고    scopus 로고
    • Structure and stability of a thermostable carboxylesterase from the thermoacidophilic archaeon Sulfolobus tokodaii
    • Angkawidjaja C, Koga Y, Takano K, Kanaya S. Structure and stability of a thermostable carboxylesterase from the thermoacidophilic archaeon Sulfolobus tokodaii. FEBS J 2012;279(17):3071-3084.
    • (2012) FEBS J , vol.279 , Issue.17 , pp. 3071-3084
    • Angkawidjaja, C.1    Koga, Y.2    Takano, K.3    Kanaya, S.4
  • 39
    • 34547643363 scopus 로고    scopus 로고
    • Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties
    • Byun JS, Rhee JK, Kim ND, Yoon J, Kim DU, Koh E, Oh JW, Cho HS. Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties. BMC Struct Biol 2007;7:47.
    • (2007) BMC Struct Biol , vol.7 , pp. 47
    • Byun, J.S.1    Rhee, J.K.2    Kim, N.D.3    Yoon, J.4    Kim, D.U.5    Koh, E.6    Oh, J.W.7    Cho, H.S.8
  • 40
    • 0034634338 scopus 로고    scopus 로고
    • A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase
    • De Simone G, Galdiero S, Manco G, Lang D, Rossi M, Pedone C. A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase. J Mol Biol 2000;303(5):761-771.
    • (2000) J Mol Biol , vol.303 , Issue.5 , pp. 761-771
    • De Simone, G.1    Galdiero, S.2    Manco, G.3    Lang, D.4    Rossi, M.5    Pedone, C.6
  • 41
    • 0035976710 scopus 로고    scopus 로고
    • The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus
    • De Simone G, Menchise V, Manco G, Mandrich L, Sorrentino N, Lang D, Rossi M, Pedone C. The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus. J Mol Biol 2001;314(3):507-518.
    • (2001) J Mol Biol , vol.314 , Issue.3 , pp. 507-518
    • De Simone, G.1    Menchise, V.2    Manco, G.3    Mandrich, L.4    Sorrentino, N.5    Lang, D.6    Rossi, M.7    Pedone, C.8
  • 42
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 2007;372(3):774-797.
    • (2007) J Mol Biol , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 43
    • 28844492475 scopus 로고    scopus 로고
    • The maltodextrin system of Escherichia coli: glycogen-derived endogenous induction and osmoregulation
    • Dippel R, Bergmiller T, Böhm A, Boos W. The maltodextrin system of Escherichia coli: glycogen-derived endogenous induction and osmoregulation. J Bacteriol 2005;187(24):8332-8339.
    • (2005) J Bacteriol , vol.187 , Issue.24 , pp. 8332-8339
    • Dippel, R.1    Bergmiller, T.2    Böhm, A.3    Boos, W.4
  • 44
    • 43549119514 scopus 로고    scopus 로고
    • A proteomic approach to study Escherichia coli. Acetyl esterase interactors unveil a sequence motif involved in protein-protein interaction
    • D'Ambrosio C, Mandrich L, Rossi M, Scaloni A, Manco G. A proteomic approach to study Escherichia coli. Acetyl esterase interactors unveil a sequence motif involved in protein-protein interaction. Protein Pept Lett 2008;15(4):333-340.
    • (2008) Protein Pept Lett , vol.15 , Issue.4 , pp. 333-340
    • D'Ambrosio, C.1    Mandrich, L.2    Rossi, M.3    Scaloni, A.4    Manco, G.5
  • 45
    • 4944262604 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose
    • Lunin VV, Li Y, Schrag JD, Iannuzzi P, Cygler M, Matte A. Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose. J Bacteriol 2004;186(20):6915-6927.
    • (2004) J Bacteriol , vol.186 , Issue.20 , pp. 6915-6927
    • Lunin, V.V.1    Li, Y.2    Schrag, J.D.3    Iannuzzi, P.4    Cygler, M.5    Matte, A.6
  • 46
    • 63449119985 scopus 로고    scopus 로고
    • Glucose- and glucokinase-controlled mal gene expression in Escherichia coli
    • Lengsfeld C, Schönert S, Dippel R, Boos W. Glucose- and glucokinase-controlled mal gene expression in Escherichia coli. J Bacteriol 2009;191(3):701-712.
    • (2009) J Bacteriol , vol.191 , Issue.3 , pp. 701-712
    • Lengsfeld, C.1    Schönert, S.2    Dippel, R.3    Boos, W.4
  • 47
    • 0001334088 scopus 로고    scopus 로고
    • Calculating partition coefficients of peptides by the addition method
    • Tao P, Wang R, Lai L. Calculating partition coefficients of peptides by the addition method. J Mol Model 1999;5:189-195.
    • (1999) J Mol Model , vol.5 , pp. 189-195
    • Tao, P.1    Wang, R.2    Lai, L.3
  • 48
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 2004;60(Pt 12 Pt 1):2256-2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PART 1 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.