메뉴 건너뛰기




Volumn 289, Issue 43, 2014, Pages 30090-30100

Duplication of genes in an ATP-binding cassette transport system increases dynamic range while maintaining ligand specificity

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BINDING ENERGY; BIOMOLECULES; DICHROISM; FOOD SUPPLY; LIGANDS; MERGERS AND ACQUISITIONS; METABOLITES; NUTRIENTS; PROTEINS; TRANSPORTATION;

EID: 84908428460     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.590992     Document Type: Article
Times cited : (15)

References (36)
  • 1
    • 0020696807 scopus 로고
    • Physiological responses to nutrient limitation
    • Harder, W., and Dijkhuizen, L. (1983) Physiological responses to nutrient limitation. Annu. Rev. Microbiol. 37, 1-23
    • (1983) Annu. Rev. Microbiol. , vol.37 , pp. 1-23
    • Harder, W.1    Dijkhuizen, L.2
  • 3
    • 0031887807 scopus 로고    scopus 로고
    • Maltose/maltodextrin system of Escherichia coli: Transport, metabolism, and regulation
    • Boos, W., and Shuman, H. (1998) 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.2
  • 4
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R., and Saier, M. H., Jr. (1993) Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57, 320-346
    • (1993) Microbiol. Rev. , vol.57 , pp. 320-346
    • Tam, R.1    Saier, M.H.2
  • 5
    • 84887294881 scopus 로고    scopus 로고
    • Structural basis for substrate specificity in the Escherichia coli maltose transport system
    • Oldham, M. L., Chen, S., and Chen, J. (2013) Structural basis for substrate specificity in the Escherichia coli maltose transport system. Proc. Natl. Acad. Sci. U.S.A. 110, 18132-18137
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 18132-18137
    • Oldham, M.L.1    Chen, S.2    Chen, J.3
  • 7
    • 0031810816 scopus 로고    scopus 로고
    • ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains
    • Schneider, E., and Hunke, S. (1998) ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains. FEMS Microbiol. Rev. 22, 1-20
    • (1998) FEMS Microbiol. Rev. , vol.22 , pp. 1-20
    • Schneider, E.1    Hunke, S.2
  • 8
    • 75549087305 scopus 로고    scopus 로고
    • The evolution of gene duplications: Classifying and distinguishing between models
    • Innan, H., and Kondrashov, F. (2010) The evolution of gene duplications: classifying and distinguishing between models. Nat. Rev. Genet. 11, 97-108
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 97-108
    • Innan, H.1    Kondrashov, F.2
  • 9
    • 75149153513 scopus 로고    scopus 로고
    • The low-affinity phosphate transporter PitA is dispensable for in vitro growth of Mycobacterium smegmatis
    • Gebhard, S., Ekanayaka, N., and Cook, G. M. (2009) The low-affinity phosphate transporter PitA is dispensable for in vitro growth of Mycobacterium smegmatis. BMC Microbiol. 9, 254
    • (2009) BMC Microbiol. , vol.9 , pp. 254
    • Gebhard, S.1    Ekanayaka, N.2    Cook, G.M.3
  • 10
    • 8244238391 scopus 로고    scopus 로고
    • Three different putative phosphate transport receptors are encoded by the Mycobacterium tuberculosis genome and are present at the surface of Mycobacterium bovis BCG
    • Lefèvre, P., Braibant, M., de Wit, L., Kalai, M., Röeper, D., Grötzinger, J., Delville, J.-P., Peirs, P., Ooms, J., Huygen, K., and Content, J. (1997) Three different putative phosphate transport receptors are encoded by the Mycobacterium tuberculosis genome and are present at the surface of Mycobacterium bovis BCG. J. Bacteriol. 179, 2900-2906
    • (1997) J. Bacteriol. , vol.179 , pp. 2900-2906
    • Lefèvre, P.1    Braibant, M.2    De Wit, L.3    Kalai, M.4    Röeper, D.5    Grötzinger, J.6    Delville, J.-P.7    Peirs, P.8    Ooms, J.9    Huygen, K.10    Content, J.11
  • 11
    • 0033987682 scopus 로고    scopus 로고
    • Characterization of two inducible phosphate transport systems in Rhizobium tropici
    • Botero, L. M., Al-Niemi, T. S., and McDermott, T. R. (2000) Characterization of two inducible phosphate transport systems in Rhizobium tropici. Appl. Environ. Microbiol. 66, 15-22
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 15-22
    • Botero, L.M.1    Al-Niemi, T.S.2    McDermott, T.R.3
  • 12
    • 0035479142 scopus 로고    scopus 로고
    • Deletional bias and the evolution of bacterial genomes
    • Mira, A., Ochman, H., and Moran, N. A. (2001) Deletional bias and the evolution of bacterial genomes. Trends Genet. 17, 589-596
    • (2001) Trends Genet. , vol.17 , pp. 589-596
    • Mira, A.1    Ochman, H.2    Moran, N.A.3
  • 14
    • 27144509128 scopus 로고    scopus 로고
    • An expression-driven approach to the prediction of carbohydrate transport and utilization regulons in the hyperthermophilic bacterium Thermotoga maritima
    • Conners, S. B., Montero, C. I., Comfort, D. A., Shockley, K. R., Johnson, M. R., Chhabra, S. R., and Kelly, R. M. (2005) An expression-driven approach to the prediction of carbohydrate transport and utilization regulons in the hyperthermophilic bacterium Thermotoga maritima. J. Bacteriol. 187, 7267-7282
    • (2005) J. Bacteriol. , vol.187 , pp. 7267-7282
    • Conners, S.B.1    Montero, C.I.2    Comfort, D.A.3    Shockley, K.R.4    Johnson, M.R.5    Chhabra, S.R.6    Kelly, R.M.7
  • 15
    • 33144472334 scopus 로고    scopus 로고
    • Several archaeal homologs of putative oligopeptide-binding proteins encoded by Thermotoga maritima bind sugars
    • Nanavati, D. M., Thirangoon, K., and Noll, K. M. (2006) Several archaeal homologs of putative oligopeptide-binding proteins encoded by Thermotoga maritima bind sugars. Appl. Environ. Microbiol. 72, 1336-1345
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1336-1345
    • Nanavati, D.M.1    Thirangoon, K.2    Noll, K.M.3
  • 16
    • 0028067178 scopus 로고
    • The bacterial periplasmic histidine-binding protein. Structure/function analysis of the ligand-binding site and comparison with related proteins
    • Oh, B.-H., Kang, C.-H., De Bondt, H., Kim, S.-H., Nikaido, K., Joshi, A. K., and Ames, G. F. (1994) The bacterial periplasmic histidine-binding protein. Structure/function analysis of the ligand-binding site and comparison with related proteins. J. Biol. Chem. 269, 4135-4143
    • (1994) J. Biol. Chem. , vol.269 , pp. 4135-4143
    • Oh, B.-H.1    Kang, C.-H.2    De Bondt, H.3    Kim, S.-H.4    Nikaido, K.5    Joshi, A.K.6    Ames, G.F.7
  • 18
    • 0027935843 scopus 로고
    • Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature
    • Cohen, D. S., and Pielak, G. J. (1994) Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature. Protein Sci. 3, 1253-1260
    • (1994) Protein Sci. , vol.3 , pp. 1253-1260
    • Cohen, D.S.1    Pielak, G.J.2
  • 19
    • 27244462844 scopus 로고
    • Isothermal titration calorimetry
    • Freire, E., Mayorga, O. L., and Straume, M. (1990) Isothermal titration calorimetry. Anal. Chem. 62, 950A-959A
    • (1990) Anal. Chem. , vol.62 , pp. 950A-959A
    • Freire, E.1    Mayorga, O.L.2    Straume, M.3
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 21
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 22
  • 24
    • 3242886389 scopus 로고    scopus 로고
    • MOLPROBITY: Structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis, I. W., Murray, L. W., Richardson, J. S., and Richardson, D. C. (2004) MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Res. 32, W615-W619
    • (2004) Nucleic Acids Res. , vol.32 , pp. W615-W619
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 27
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF
    • Hvorup, R. N., Goetz, B. A., Niederer, M., Hollenstein, K., Perozo, E., and Locher, K. P. (2007) Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF. Science 317, 1387-1390
    • (2007) Science , vol.317 , pp. 1387-1390
    • Hvorup, R.N.1    Goetz, B.A.2    Niederer, M.3    Hollenstein, K.4    Perozo, E.5    Locher, K.P.6
  • 28
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham, M. L., Khare, D., Quiocho, F. A., Davidson, A. L., and Chen, J. (2007) Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450, 515-521
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 29
    • 70450285142 scopus 로고    scopus 로고
    • Structural analysis of semi-specific oligosaccharide recognition by a cellulose-binding protein of Thermotoga maritima reveals adaptations for functional diversification of the oligopeptide periplasmic binding protein fold
    • Cuneo, M. J., Beese, L. S., and Hellinga, H. W. (2009) Structural analysis of semi-specific oligosaccharide recognition by a cellulose-binding protein of Thermotoga maritima reveals adaptations for functional diversification of the oligopeptide periplasmic binding protein fold. J. Biol. Chem. 284, 33217-33223
    • (2009) J. Biol. Chem. , vol.284 , pp. 33217-33223
    • Cuneo, M.J.1    Beese, L.S.2    Hellinga, H.W.3
  • 31
    • 5144226338 scopus 로고    scopus 로고
    • The DxDxDG motif for calcium binding: Multiple structural contexts and implications for evolution
    • Rigden, D. J., and Galperin, M. Y. (2004) The DxDxDG motif for calcium binding: multiple structural contexts and implications for evolution. J. Mol. Biol. 343, 971-984
    • (2004) J. Mol. Biol. , vol.343 , pp. 971-984
    • Rigden, D.J.1    Galperin, M.Y.2
  • 32
    • 0035094475 scopus 로고    scopus 로고
    • Geometry of metal-ligand interactions in proteins
    • Harding, M. M. (2001) Geometry of metal-ligand interactions in proteins. Acta Crystallogr. D Biol. Crystallogr. 57, 401-411
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 401-411
    • Harding, M.M.1
  • 34
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 35
    • 0011729692 scopus 로고
    • Two periplasmic transport proteins which interact with a common membrane receptor show extensive homology: Complete nucleotide sequences
    • Higgins, C. F., and Ames, G. (1981) Two periplasmic transport proteins which interact with a common membrane receptor show extensive homology: complete nucleotide sequences. Proc. Natl. Acad. Sci. U.S.A. 78, 6038-6042
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 6038-6042
    • Higgins, C.F.1    Ames, G.2
  • 36
    • 0037470149 scopus 로고    scopus 로고
    • Carbohydrate-induced differential gene expression patterns in the hyperthermophilic bacterium Thermotoga maritima
    • Chhabra, S. R., Shockley, K. R., Conners, S. B., Scott, K. L., Wolfinger, R. D., and Kelly, R. M. (2003) Carbohydrate-induced differential gene expression patterns in the hyperthermophilic bacterium Thermotoga maritima. J. Biol. Chem. 278, 7540-7552
    • (2003) J. Biol. Chem. , vol.278 , pp. 7540-7552
    • Chhabra, S.R.1    Shockley, K.R.2    Conners, S.B.3    Scott, K.L.4    Wolfinger, R.D.5    Kelly, R.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.