메뉴 건너뛰기




Volumn 85, Issue 5, 2012, Pages 846-861

Interaction of the Escherichia coli transporter DctA with the sensor kinase DcuS: Presence of functional DctA/DcuS sensor units

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; COTRANSPORTER; DCTA PROTEIN; DCUS PROTEIN; PROTEIN KINASE; SODIUM GLUTAMATE SYMPORTER; UNCLASSIFIED DRUG;

EID: 84865565446     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.08143.x     Document Type: Article
Times cited : (39)

References (48)
  • 1
    • 79959780095 scopus 로고    scopus 로고
    • Topology and accessibility of the transmembrane helices and the sensory site in the bifunctional transporter DcuB of Escherichia coli
    • Bauer, J., Fritsch, M.J., Palmer, T., and Unden, G. (2011) Topology and accessibility of the transmembrane helices and the sensory site in the bifunctional transporter DcuB of Escherichia coli. Biochemistry 50: 5925-5938.
    • (2011) Biochemistry , vol.50 , pp. 5925-5938
    • Bauer, J.1    Fritsch, M.J.2    Palmer, T.3    Unden, G.4
  • 2
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • Boudker, O., Ryan, R.M., Yernool, D., Shimamoto, K., and Gouaux, E. (2007) Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature 445: 387-393.
    • (2007) Nature , vol.445 , pp. 387-393
    • Boudker, O.1    Ryan, R.M.2    Yernool, D.3    Shimamoto, K.4    Gouaux, E.5
  • 3
    • 0025330038 scopus 로고
    • Lac permease of Escherichia coli: topology and sequence elements promoting membrane insertion
    • Calamia, J., and Manoil, C. (1990) Lac permease of Escherichia coli: topology and sequence elements promoting membrane insertion. Proc Natl Acad Sci USA 87: 4937-4941.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4937-4941
    • Calamia, J.1    Manoil, C.2
  • 4
    • 57649219430 scopus 로고    scopus 로고
    • 4-dicarboxylate ligand complexes with sensor domains of histidine kinases DcuS and DctB
    • 4-dicarboxylate ligand complexes with sensor domains of histidine kinases DcuS and DctB. J Biol Chem 283: 30256-30265.
    • (2008) J Biol Chem , vol.283 , pp. 30256-30265
    • Cheung, J.1    Hendrickson, W.A.2
  • 6
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electroporation
    • Dower, W.J., Miller, J.F., and Ragsdale, C.W. (1988) High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res 16: 6127-6145.
    • (1988) Nucleic Acids Res , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 7
    • 53549125239 scopus 로고    scopus 로고
    • Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS
    • Etzkorn, M., Kneuper, H., Dünnwald, P., Vijayan, V., Krämer, J., Griesinger, C., etal. (2008) Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS. Nat Struct Mol Biol 15: 1031-1039.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1031-1039
    • Etzkorn, M.1    Kneuper, H.2    Dünnwald, P.3    Vijayan, V.4    Krämer, J.5    Griesinger, C.6
  • 8
    • 79960702462 scopus 로고    scopus 로고
    • Antimicrobial peptide sensing and detoxification modules: unravelling the regulatory circuitry of Staphylococcus aureus
    • Gebhard, S., and Mascher, T. (2011) Antimicrobial peptide sensing and detoxification modules: unravelling the regulatory circuitry of Staphylococcus aureus. Mol Microbiol 81: 581-587.
    • (2011) Mol Microbiol , vol.81 , pp. 581-587
    • Gebhard, S.1    Mascher, T.2
  • 12
    • 77952566391 scopus 로고    scopus 로고
    • Biochemical characterization of the C4-dicarboxylatetransporter DctA from Bacillus subtilis
    • Groeneveld, M., Weme, R.G.J.D.O., Duurkens, R.H., and Slotboom, D.J. (2010) Biochemical characterization of the C4-dicarboxylatetransporter DctA from Bacillus subtilis. J Bacteriol 192: 2900-2907.
    • (2010) J Bacteriol , vol.192 , pp. 2900-2907
    • Groeneveld, M.1    Weme, R.G.J.D.O.2    Duurkens, R.H.3    Slotboom, D.J.4
  • 13
    • 0034891560 scopus 로고    scopus 로고
    • DctA- and Dcu-independent transport of succinate in Escherichia coli: contribution of diffusion and of alternative carriers
    • Janausch, I.G., Kim, O.B., and Unden, G. (2001) DctA- and Dcu-independent transport of succinate in Escherichia coli: contribution of diffusion and of alternative carriers. Arch Microbiol 176: 224-230.
    • (2001) Arch Microbiol , vol.176 , pp. 224-230
    • Janausch, I.G.1    Kim, O.B.2    Unden, G.3
  • 15
    • 0028092856 scopus 로고
    • A transmembrane signalling complex controls transcription of the Uhp sugar phosphate transport system
    • Kadner, R.J., Island, M.D., Dahl, J.I., and Webber, C.A. (1994) A transmembrane signalling complex controls transcription of the Uhp sugar phosphate transport system. Res Microbiol 145: 381-387.
    • (1994) Res Microbiol , vol.145 , pp. 381-387
    • Kadner, R.J.1    Island, M.D.2    Dahl, J.I.3    Webber, C.A.4
  • 16
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transducing pathway
    • Karimova, G., Pidoux, J., Ullmann, A., and Ladant, D. (1998) A bacterial two-hybrid system based on a reconstituted signal transducing pathway. Proc Natl Acad Sci USA 95: 5752-5756.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 17
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • Karimova, G., Dautin, N., and Ladant, D. (2005) Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J Bactorial 187: 2233-2243.
    • (2005) J Bactorial , vol.187 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 18
    • 0014984409 scopus 로고
    • 4-dicarboxylic acids by Escherichia coli
    • 4-dicarboxylic acids by Escherichia coli. Eur J Biochem 18: 274-281.
    • (1971) Eur J Biochem , vol.18 , pp. 274-281
    • Kay, W.W.1    Kornberg, H.L.2
  • 19
    • 33748486238 scopus 로고    scopus 로고
    • Determinants of chemoreceptor cluster formation in Escherichia coli
    • Kentner, D., Thiem, S., Hildenbeutel, M., and Sourjik, V. (2006) Determinants of chemoreceptor cluster formation in Escherichia coli. Mol Microbiol 61: 407-417.
    • (2006) Mol Microbiol , vol.61 , pp. 407-417
    • Kentner, D.1    Thiem, S.2    Hildenbeutel, M.3    Sourjik, V.4
  • 20
    • 58849136357 scopus 로고    scopus 로고
    • The fumarate/succinate antiporter DcuB of Escherichia coli is a bifunctional protein with sites for regulation of DcuS-dependent gene expression
    • Kleefeld, A., Ackermann, B., Bauer, J., Krämer, J., and Unden, G. (2009) The fumarate/succinate antiporter DcuB of Escherichia coli is a bifunctional protein with sites for regulation of DcuS-dependent gene expression. J Biol Chem 284: 265-275.
    • (2009) J Biol Chem , vol.284 , pp. 265-275
    • Kleefeld, A.1    Ackermann, B.2    Bauer, J.3    Krämer, J.4    Unden, G.5
  • 21
    • 20144380866 scopus 로고    scopus 로고
    • The nature of the stimulus and the fumarate binding site of the fumarate sensor DcuS of Escherichia coli
    • Kneuper, H., Janausch, I.G., Vijayan, V., Zweckstetter, M., Bock, V., Griesinger, C., etal. (2005) The nature of the stimulus and the fumarate binding site of the fumarate sensor DcuS of Escherichia coli. J Biol Chem 280: 20596-20603.
    • (2005) J Biol Chem , vol.280 , pp. 20596-20603
    • Kneuper, H.1    Janausch, I.G.2    Vijayan, V.3    Zweckstetter, M.4    Bock, V.5    Griesinger, C.6
  • 23
    • 0024064872 scopus 로고
    • Molecular genetic analysis of membrane protein topology
    • Manoil, C., Boyd, D., and Beckwith, J. (1988) Molecular genetic analysis of membrane protein topology. Trends Genet 4: 223-226.
    • (1988) Trends Genet , vol.4 , pp. 223-226
    • Manoil, C.1    Boyd, D.2    Beckwith, J.3
  • 24
    • 33845640610 scopus 로고    scopus 로고
    • Stimulus perception in bacterial signal transducing histidine kinases
    • Mascher, T., Helmann, J.D., and Unden, G. (2006) Stimulus perception in bacterial signal transducing histidine kinases. Microbiol Mol Biol Rev 70: 910-938.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 910-938
    • Mascher, T.1    Helmann, J.D.2    Unden, G.3
  • 25
    • 56249148844 scopus 로고    scopus 로고
    • Regulatory properties and interaction of the C- and N-terinal domains of BetP, an osmoregulated betaine transporter from Corynebacterium glutamicum
    • Ott, V., Koch, J., Späte, K., Morbach, S., and Krämer, R. (2008) Regulatory properties and interaction of the C- and N-terinal domains of BetP, an osmoregulated betaine transporter from Corynebacterium glutamicum. Biochemistry 47: 12208-12218.
    • (2008) Biochemistry , vol.47 , pp. 12208-12218
    • Ott, V.1    Koch, J.2    Späte, K.3    Morbach, S.4    Krämer, R.5
  • 26
    • 0141531993 scopus 로고    scopus 로고
    • The NMR structure of the sensory domain of the membraneous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli
    • Pappalardo, L., Janausch, I.G., Vijayan, V., Zientz, E., Junker, J., Peti, W., etal. (2003) The NMR structure of the sensory domain of the membraneous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli. J Biol Chem 278: 39185-39188.
    • (2003) J Biol Chem , vol.278 , pp. 39185-39188
    • Pappalardo, L.1    Janausch, I.G.2    Vijayan, V.3    Zientz, E.4    Junker, J.5    Peti, W.6
  • 27
    • 84872600963 scopus 로고    scopus 로고
    • Transport database
    • Paulsen, I.T. (1998) Transport database [WWW document]. URL http://www.membranetransport.org/.
    • (1998)
    • Paulsen, I.T.1
  • 28
    • 0031896855 scopus 로고    scopus 로고
    • Roles of DctA and DctB in signal detection by the dicarboxylic acid transport system of Rhizobium leguminosarum
    • Reid, C.J., and Poole, P.S. (1998) Roles of DctA and DctB in signal detection by the dicarboxylic acid transport system of Rhizobium leguminosarum. J Bacteriol 180: 2660-2669.
    • (1998) J Bacteriol , vol.180 , pp. 2660-2669
    • Reid, C.J.1    Poole, P.S.2
  • 29
    • 72449164409 scopus 로고    scopus 로고
    • Transport mechanism of a bacterial homologue of glutamate transporters
    • Reyes, N., Ginter, C., and Boudker, O. (2009) Transport mechanism of a bacterial homologue of glutamate transporters. Nature 462: 880-885.
    • (2009) Nature , vol.462 , pp. 880-885
    • Reyes, N.1    Ginter, C.2    Boudker, O.3
  • 31
    • 34248679167 scopus 로고    scopus 로고
    • Tricine SDS PAGE
    • Schägger, H. (2006) Tricine SDS PAGE. Nat Protoc 1: 16-22.
    • (2006) Nat Protoc , vol.1 , pp. 16-22
    • Schägger, H.1
  • 32
    • 51149089479 scopus 로고    scopus 로고
    • Polar accumulation of the metabolic sensory histidine kinases DcuS and CitA in Escherichia coli
    • Scheu, P., Sdorra, S., Liao, Y.F., Wegner, M., Basché, T., Unden, G., etal. (2008) Polar accumulation of the metabolic sensory histidine kinases DcuS and CitA in Escherichia coli. Microbiology 154: 2463-2472.
    • (2008) Microbiology , vol.154 , pp. 2463-2472
    • Scheu, P.1    Sdorra, S.2    Liao, Y.F.3    Wegner, M.4    Basché, T.5    Unden, G.6
  • 33
    • 77957559402 scopus 로고    scopus 로고
    • Sensing by the membrane-bound sensor kinase DcuS: exogenous versus endogenous sensing of C4-dicarboxylates in bacteria
    • Scheu, P.D., Kim, O.B., Griesinger, C., and Unden, G. (2010a) Sensing by the membrane-bound sensor kinase DcuS: exogenous versus endogenous sensing of C4-dicarboxylates in bacteria. Future Microbiol 5: 1383-1402.
    • (2010) Future Microbiol , vol.5 , pp. 1383-1402
    • Scheu, P.D.1    Kim, O.B.2    Griesinger, C.3    Unden, G.4
  • 34
    • 77954378944 scopus 로고    scopus 로고
    • Oligomeric sensor kinase DcuS in the membrane of Escherichia coli and in proteoliposomes: chemical cross-linking and FRET spectroscopy
    • Scheu, P.D., Liao, Y.F., Bauer, J., Kneuper, H., Basché, T., Unden, G., etal. (2010b) Oligomeric sensor kinase DcuS in the membrane of Escherichia coli and in proteoliposomes: chemical cross-linking and FRET spectroscopy. J Bacteriol 192: 3474-3483.
    • (2010) J Bacteriol , vol.192 , pp. 3474-3483
    • Scheu, P.D.1    Liao, Y.F.2    Bauer, J.3    Kneuper, H.4    Basché, T.5    Unden, G.6
  • 35
    • 84855934674 scopus 로고    scopus 로고
    • The CitA/CitB two-component system regulating citrate fermentation in Escherichia coli and its relation to the DcuS/DcuR system in vivo
    • Scheu, P.D., Witan, J., Rauschmeier, M., Graf, S., Liao, Y.F., Ebert-Jung, A., etal. (2011) The CitA/CitB two-component system regulating citrate fermentation in Escherichia coli and its relation to the DcuS/DcuR system in vivo. J Bacteriol 194: 636-645.
    • (2011) J Bacteriol , vol.194 , pp. 636-645
    • Scheu, P.D.1    Witan, J.2    Rauschmeier, M.3    Graf, S.4    Liao, Y.F.5    Ebert-Jung, A.6
  • 36
    • 0344837749 scopus 로고    scopus 로고
    • Connection of transport and sensing by UhpC, the sensor for external glucose-6-phosphate in Escherichia coli
    • Schwöppe, C., Winkler, H.H., and Neuhaus, H.E. (2003) Connection of transport and sensing by UhpC, the sensor for external glucose-6-phosphate in Escherichia coli. Eur J Biochem 270: 1450-1457.
    • (2003) Eur J Biochem , vol.270 , pp. 1450-1457
    • Schwöppe, C.1    Winkler, H.H.2    Neuhaus, H.E.3
  • 37
  • 38
  • 39
    • 0035448934 scopus 로고    scopus 로고
    • Glutamate transporters combine transporter- and channel-like features
    • Slotboom, D.J., Konings, W.N., and Lolkema, J.S. (2001) Glutamate transporters combine transporter- and channel-like features. Trends Biochem Sci 26: 534-539.
    • (2001) Trends Biochem Sci , vol.26 , pp. 534-539
    • Slotboom, D.J.1    Konings, W.N.2    Lolkema, J.S.3
  • 40
    • 70350173721 scopus 로고    scopus 로고
    • The regulatory interplay between membrane-integrated sensors and transport proreins in bacteria
    • Tetsch, L., and Jung, K. (2009) The regulatory interplay between membrane-integrated sensors and transport proreins in bacteria. Mol Microbiol 73: 982-991.
    • (2009) Mol Microbiol , vol.73 , pp. 982-991
    • Tetsch, L.1    Jung, K.2
  • 41
    • 37749014565 scopus 로고    scopus 로고
    • The membrane-integrated transcriptional activator CadC of Escherichia coli senses lysine indirectly via the interaction with the lysine permease LysP
    • Tetsch, L., Koller, C., Haneburger, I., and Jung, K. (2008) The membrane-integrated transcriptional activator CadC of Escherichia coli senses lysine indirectly via the interaction with the lysine permease LysP. Mol Microbiol 67: 570-583.
    • (2008) Mol Microbiol , vol.67 , pp. 570-583
    • Tetsch, L.1    Koller, C.2    Haneburger, I.3    Jung, K.4
  • 42
    • 0022259474 scopus 로고
    • Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system
    • Treptow, N.A., and Schuman, H.A. (1985) Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system. J Bacteriol 163: 654-660.
    • (1985) J Bacteriol , vol.163 , pp. 654-660
    • Treptow, N.A.1    Schuman, H.A.2
  • 43
    • 38049069378 scopus 로고    scopus 로고
    • Core residue replacement cause coiled-coil orientation switching in vitro and in vivo: Structure-function correlations for osmosensory transporter ProP
    • Tsatskis, Y., Kwok, S.C., Becker, E., Gill, C., Smith, M.N., Keates, R.A.B., etal. (2008) Core residue replacement cause coiled-coil orientation switching in vitro and in vivo: Structure-function correlations for osmosensory transporter ProP. Biochemistry 47: 60-72.
    • (2008) Biochemistry , vol.47 , pp. 60-72
    • Tsatskis, Y.1    Kwok, S.C.2    Becker, E.3    Gill, C.4    Smith, M.N.5    Keates, R.A.B.6
  • 44
    • 36849015970 scopus 로고    scopus 로고
    • 4-Dicarboxylate degradation in aerobic and anaerobic growth
    • Module 3.4.5. Curtiss, R. III (Editor in Chief). Washington, DC: ASM Press (Online)
    • 4-Dicarboxylate degradation in aerobic and anaerobic growth. Module 3.4.5. In EcoSal -Escherichia coli and Salmonella: Cellular and Molecular Biology. Curtiss, R. III (Editor in Chief). Washington, DC: ASM Press (Online). http://www.ecosal.org
    • (2004) EcoSal -Escherichia coli and Salmonella: Cellular and Molecular Biology
    • Unden, G.1    Kleefeld, A.2
  • 45
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J., and Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33: 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 46
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool, D., Boudker, O., Jin, Y., and Gouaux, E. (2004) Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431: 811-818.
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 47
    • 77957234040 scopus 로고    scopus 로고
    • The BCCT family of carriers: from physiology to crystal structure
    • Ziegler, C., Bremer, E., and Krämer, R. (2010) The BCCT family of carriers: from physiology to crystal structure. Mol Microbiol 78: 13-34.
    • (2010) Mol Microbiol , vol.78 , pp. 13-34
    • Ziegler, C.1    Bremer, E.2    Krämer, R.3
  • 48
    • 0031661593 scopus 로고    scopus 로고
    • Fumarate regulation of gene expression in Escherichia coli by the DcuSR (dcuSR genes) two-component regulatory system
    • Zientz, E., Bongaerts, J., and Unden, G. (1998) Fumarate regulation of gene expression in Escherichia coli by the DcuSR (dcuSR genes) two-component regulatory system. J Bacteriol 180: 5421-5425.
    • (1998) J Bacteriol , vol.180 , pp. 5421-5425
    • Zientz, E.1    Bongaerts, J.2    Unden, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.