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Volumn 56, Issue 6, 2011, Pages 514-520

Alternative split sites for fragment complementation, and glyphosate function as extra ligand and stabilizer for the AroA enzyme complexes

Author keywords

AroA; complex stability; extra ligand; fragment complementation; glyphosate

Indexed keywords

ESCHERICHIA COLI;

EID: 79952067131     PISSN: 10016538     EISSN: 18619541     Source Type: Journal    
DOI: 10.1007/s11434-010-4323-9     Document Type: Article
Times cited : (2)

References (25)
  • 1
    • 0000356227 scopus 로고
    • On the enzymic activity of subtilisin-modified ribonuclease
    • Richards F M. On the enzymic activity of subtilisin-modified ribonuclease. Proc Natl Acad Sci USA, 1958, 44: 162-166.
    • (1958) Proc Natl Acad Sci USA , vol.44 , pp. 162-166
    • Richards, F.M.1
  • 2
    • 0014126182 scopus 로고
    • Nuclease-T: An active derivative of staphylococcal nuclease composed of two noncovalently bonded peptide fragments
    • Taniuchi H, Anfinsen C B, Sodja A. Nuclease-T: An active derivative of staphylococcal nuclease composed of two noncovalently bonded peptide fragments. Proc Natl Acad Sci USA, 1967, 58: 1235-1242.
    • (1967) Proc Natl Acad Sci USA , vol.58 , pp. 1235-1242
    • Taniuchi, H.1    Anfinsen, C.B.2    Sodja, A.3
  • 3
    • 0025310534 scopus 로고
    • In vivo expression of the lacY gene in two segments leads to functional lac permease
    • Bibi E, Kaback H R. In vivo expression of the lacY gene in two segments leads to functional lac permease. Proc Natl Acad Sci USA, 1990, 87: 4325-4329.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4325-4329
    • Bibi, E.1    Kaback, H.R.2
  • 4
    • 0026592651 scopus 로고
    • Functional assembly of a randomly cleaved protein
    • Shiba K, Schimmel P. Functional assembly of a randomly cleaved protein. Proc Natl Acad Sci USA, 1992, 89: 1880-1884.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1880-1884
    • Shiba, K.1    Schimmel, P.2
  • 5
    • 0034486018 scopus 로고    scopus 로고
    • Fragment complementation of calbindin D28k
    • Berggard T, Thulin E, Akerfeldt K S, et al. Fragment complementation of calbindin D28k. Protein Sci, 2000, 9: 2094-2108.
    • (2000) Protein Sci , vol.9 , pp. 2094-2108
    • Berggard, T.1    Thulin, E.2    Akerfeldt, K.S.3
  • 6
    • 0042838110 scopus 로고    scopus 로고
    • In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12
    • Braun M, Endriss F, Killmann H, et al. In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12. J Bacteriol, 2003, 185: 5508-5518.
    • (2003) J Bacteriol , vol.185 , pp. 5508-5518
    • Braun, M.1    Endriss, F.2    Killmann, H.3
  • 7
    • 0036890333 scopus 로고    scopus 로고
    • Protein reconstitution and 3D domain swapping
    • Hakansson M, Linse S. Protein reconstitution and 3D domain swapping. Curr Protein Pept Sci, 2002, 3: 629-642.
    • (2002) Curr Protein Pept Sci , vol.3 , pp. 629-642
    • Hakansson, M.1    Linse, S.2
  • 8
    • 0030838729 scopus 로고    scopus 로고
    • Reconstitution of functional volt-age-gated chloride channels from complementary fragments of CLC-1
    • Schmidt-Rose T, Jentsch T J. Reconstitution of functional volt-age-gated chloride channels from complementary fragments of CLC-1. J Biol Chem, 1997, 272: 20515-20521.
    • (1997) J Biol Chem , vol.272 , pp. 20515-20521
    • Schmidt-Rose, T.1    Jentsch, T.J.2
  • 9
    • 0018932939 scopus 로고
    • The herbicide glyphosate is a potent inhibitor of 5-enolpyruvyl-shikimic acid-3-phosphate synthase
    • Steinrucken H C, Amrhein N. The herbicide glyphosate is a potent inhibitor of 5-enolpyruvyl-shikimic acid-3-phosphate synthase. Biochem Biophys Res Commun, 1980, 94: 1207-1212.
    • (1980) Biochem Biophys Res Commun , vol.94 , pp. 1207-1212
    • Steinrucken, H.C.1    Amrhein, N.2
  • 10
    • 0025581736 scopus 로고
    • The shikimate pathway-A metabolic tree with many branches
    • Bentley R. The shikimate pathway-A metabolic tree with many branches. Crit Rev Biochem Mol Biol, 1990, 25: 307-384.
    • (1990) Crit Rev Biochem Mol Biol , vol.25 , pp. 307-384
    • Bentley, R.1
  • 11
    • 0035852781 scopus 로고    scopus 로고
    • Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvyl-shikimate 3-phosphate synthase in atomic detail
    • Schonbrunn E, Eschenburg S, Shuttleworth W A, et al. Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvyl-shikimate 3-phosphate synthase in atomic detail. Proc Natl Acad Sci USA, 2001, 98: 1376-1380.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1376-1380
    • Schonbrunn, E.1    Eschenburg, S.2    Shuttleworth, W.A.3
  • 12
    • 0025837325 scopus 로고
    • Site-directed mutagenesis of a conserved region of the 5-enolpyruvylshikimate-3-phosphate synthase active site
    • Padgette S R, Re D B, Gasser C S, et al. Site-directed mutagenesis of a conserved region of the 5-enolpyruvylshikimate-3-phosphate synthase active site. J Biol Chem, 1991, 266: 22364-22369.
    • (1991) J Biol Chem , vol.266 , pp. 22364-22369
    • Padgette, S.R.1    Re, D.B.2    Gasser, C.S.3
  • 13
    • 0036833740 scopus 로고    scopus 로고
    • How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli
    • Eschenburg S, Healy M L, Priestman M A, et al. How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli. Planta, 2002, 216: 129-135.
    • (2002) Planta , vol.216 , pp. 129-135
    • Eschenburg, S.1    Healy, M.L.2    Priestman, M.A.3
  • 14
    • 0025754179 scopus 로고
    • Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: A distinctive protein fold
    • Stallings W C, Abdel-Meguid S S, Lim L W, et al. Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: A distinctive protein fold. Proc Natl Acad Sci USA, 1991, 88: 5046-5050.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5046-5050
    • Stallings, W.C.1    Abdel-Meguid, S.S.2    Lim, L.W.3
  • 15
    • 0033551439 scopus 로고    scopus 로고
    • Substrate and inhibitor-induced conformational changes in the structurally related enzymes UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate 3-phosphate synthase (EPSPS)
    • Krekel F, Oecking C, Amrhein N, et al. Substrate and inhibitor-induced conformational changes in the structurally related enzymes UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate 3-phosphate synthase (EPSPS). Biochemistry, 1999, 38: 8864-8878.
    • (1999) Biochemistry , vol.38 , pp. 8864-8878
    • Krekel, F.1    Oecking, C.2    Amrhein, N.3
  • 16
    • 32344440872 scopus 로고    scopus 로고
    • Reconstitution of the enzyme AroA and its glyphosate tolerance by fragment complementation
    • Sun Y C, Li Y, Zhang H, et al. Reconstitution of the enzyme AroA and its glyphosate tolerance by fragment complementation. FEBS Lett, 2006, 580: 1521-1527.
    • (2006) FEBS Lett , vol.580 , pp. 1521-1527
    • Sun, Y.C.1    Li, Y.2    Zhang, H.3
  • 17
    • 23744445780 scopus 로고    scopus 로고
    • Novel AroA with high tolerance to glyphosate, encoded by a gene of Pseudomonas putida 4G-1 isolated from an extremely polluted environment in China
    • Sun Y C, Chen Y C, Tian Z X, et al. Novel AroA with high tolerance to glyphosate, encoded by a gene of Pseudomonas putida 4G-1 isolated from an extremely polluted environment in China. Appl Environ Microbiol, 2005, 71: 4771-4776.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 4771-4776
    • Sun, Y.C.1    Chen, Y.C.2    Tian, Z.X.3
  • 18
    • 0030796260 scopus 로고    scopus 로고
    • Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization
    • Link A J, Phillips D, Church G M. Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization. J Bacteriol, 1997, 179: 6228-6237.
    • (1997) J Bacteriol , vol.179 , pp. 6228-6237
    • Link, A.J.1    Phillips, D.2    Church, G.M.3
  • 19
    • 0000605871 scopus 로고    scopus 로고
    • TyrR protein of Escherichia coli and its role as repressor and activator
    • 2nd edth edn., F. C. Neidhardt, R. CurtissIII, and J. L. Ingraham (Eds.), Washington DC: American Society for Microbiology
    • Pittard A J. TyrR protein of Escherichia coli and its role as repressor and activator. In: Neidhardt F C, Curtiss R III, Ingraham J L, et al., eds. Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd ed. Washington DC: American Society for Microbiology, 1996. 458-484.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 458-484
    • Pittard, A.J.1
  • 20
    • 0344824655 scopus 로고    scopus 로고
    • Proteolysis in bacterial regulatory circuits
    • Gottesman S. Proteolysis in bacterial regulatory circuits. Annu Rev Cell Dev Biol, 2003, 19: 565-587.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 565-587
    • Gottesman, S.1
  • 21
    • 0035814792 scopus 로고    scopus 로고
    • Fragment complementation studies of protein stabilization by hydrophobic core residues
    • Berggard T, Julenius K, Ogard A, et al. Fragment complementation studies of protein stabilization by hydrophobic core residues. Biochemistry, 2001, 40: 1257-1264.
    • (2001) Biochemistry , vol.40 , pp. 1257-1264
    • Berggard, T.1    Julenius, K.2    Ogard, A.3
  • 22
    • 33646091307 scopus 로고    scopus 로고
    • Intraversus intermolecular interactions in monellin: Contribution of surface charges to protein assembly
    • Xue W F, Szczepankiewicz O, Bauer M C, et al. Intraversus intermolecular interactions in monellin: Contribution of surface charges to protein assembly. J Mol Biol, 2006, 358: 1244-1255.
    • (2006) J Mol Biol , vol.358 , pp. 1244-1255
    • Xue, W.F.1    Szczepankiewicz, O.2    Bauer, M.C.3
  • 23
    • 21244433239 scopus 로고    scopus 로고
    • Electrostatic contributions to the kinetics and thermodynamics of protein assembly
    • Dell'Orco D, Xue W F, Thulin E, et al. Electrostatic contributions to the kinetics and thermodynamics of protein assembly. Biophys J, 2005, 88: 1991-2002.
    • (2005) Biophys J , vol.88 , pp. 1991-2002
    • Dell'Orco, D.1    Xue, W.F.2    Thulin, E.3
  • 24
    • 0347298770 scopus 로고    scopus 로고
    • Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects
    • Schwehm J M, Fitch C A, Dang B N, et al. Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. Biochemistry, 2003, 42: 1118-1128.
    • (2003) Biochemistry , vol.42 , pp. 1118-1128
    • Schwehm, J.M.1    Fitch, C.A.2    Dang, B.N.3
  • 25
    • 0037215318 scopus 로고    scopus 로고
    • Electrostatic interactions in the reconstitution of an SH2 domain from constituent peptide fragments
    • Ojennus D D, Lehto S E, Wuttke D S. Electrostatic interactions in the reconstitution of an SH2 domain from constituent peptide fragments. Protein Sci, 2003, 12: 44-55.
    • (2003) Protein Sci , vol.12 , pp. 44-55
    • Ojennus, D.D.1    Lehto, S.E.2    Wuttke, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.