메뉴 건너뛰기




Volumn 90, Issue 6, 2013, Pages 1162-1177

Co-ordinate synthesis and protein localization in a bacterial organelle by the action of a penicillin-binding-protein

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; COPPER; PENICILLIN BINDING PROTEIN; STPX PROTEIN; UNCLASSIFIED DRUG; ZINC;

EID: 84890115756     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12422     Document Type: Article
Times cited : (26)

References (48)
  • 1
  • 2
    • 52949102235 scopus 로고    scopus 로고
    • Complex regulatory pathways coordinate cell-cycle progression and development in Caulobacter crescentus
    • Brown, P.J.B., Hardy, G.G., Trimble, M.J., and Brun, Y.V. (2009) Complex regulatory pathways coordinate cell-cycle progression and development in Caulobacter crescentus. Adv Microb Physiol 54: 1-101.
    • (2009) Adv Microb Physiol , vol.54 , pp. 1-101
    • Brown, P.J.B.1    Hardy, G.G.2    Trimble, M.J.3    Brun, Y.V.4
  • 3
    • 80052329732 scopus 로고    scopus 로고
    • Genome sequences of eight morphologically diverse alphaproteobacteria
    • Brown, P.J.B., Kysela, D.T., Buechlein, A., Hemmerich, C., and Brun, Y.V. (2011) Genome sequences of eight morphologically diverse alphaproteobacteria. J Bacteriol 193: 4567-4568.
    • (2011) J Bacteriol , vol.193 , pp. 4567-4568
    • Brown, P.J.B.1    Kysela, D.T.2    Buechlein, A.3    Hemmerich, C.4    Brun, Y.V.5
  • 5
    • 0035822583 scopus 로고    scopus 로고
    • Identification and characterization of a high-affinity zinc uptake system in Neisseria gonorrhoeae
    • Chen, C.Y., and Morse, S.A. (2001) Identification and characterization of a high-affinity zinc uptake system in Neisseria gonorrhoeae. FEMS Microbiol Lett 202: 67-71.
    • (2001) FEMS Microbiol Lett , vol.202 , pp. 67-71
    • Chen, C.Y.1    Morse, S.A.2
  • 6
    • 84860600234 scopus 로고    scopus 로고
    • The scaffolding and signalling functions of a localization factor impact polar development
    • Curtis, P.D., Quardokus, E.M., Lawler, M.L., Guo, X., Klein, D., Chen, J.C., etal. (2012) The scaffolding and signalling functions of a localization factor impact polar development. Mol Microbiol 84: 712-735.
    • (2012) Mol Microbiol , vol.84 , pp. 712-735
    • Curtis, P.D.1    Quardokus, E.M.2    Lawler, M.L.3    Guo, X.4    Klein, D.5    Chen, J.C.6
  • 7
    • 34548677525 scopus 로고    scopus 로고
    • The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes
    • Divakaruni, A.V., Baida, C., White, C.L., and Gober, J.W. (2007) The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes. Mol Microbiol 66: 174-188.
    • (2007) Mol Microbiol , vol.66 , pp. 174-188
    • Divakaruni, A.V.1    Baida, C.2    White, C.L.3    Gober, J.W.4
  • 8
    • 33748372299 scopus 로고    scopus 로고
    • Thermodynamic and kinetic aspects of metal binding to the histidine-rich protein, Hpn
    • Ge, R., Zhang, Y., Sun, X., Watt, R.M., He, Q.-Y., Huang, J.-D., etal. (2006) Thermodynamic and kinetic aspects of metal binding to the histidine-rich protein, Hpn. J Am Chem Soc 128: 11330-11331.
    • (2006) J Am Chem Soc , vol.128 , pp. 11330-11331
    • Ge, R.1    Zhang, Y.2    Sun, X.3    Watt, R.M.4    He, Q.-Y.5    Huang, J.-D.6
  • 9
    • 0029070195 scopus 로고
    • Protein Hpn: cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelae
    • Gilbert, J.V., Ramakrishna, J., Sunderman, F.W., Wright, A., and Plaut, A.G. (1995) Protein Hpn: cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelae. Infect Immun 63: 2682-2688.
    • (1995) Infect Immun , vol.63 , pp. 2682-2688
    • Gilbert, J.V.1    Ramakrishna, J.2    Sunderman, F.W.3    Wright, A.4    Plaut, A.G.5
  • 10
    • 0026716013 scopus 로고
    • Nucleotide sequence analysis of the gene encoding the Caulobacter crescentus paracrystalline surface layer protein
    • Gilchrist, A., Fisher, J.A., and Smit, J. (1992) Nucleotide sequence analysis of the gene encoding the Caulobacter crescentus paracrystalline surface layer protein. Can J Microbiol 38: 193-202.
    • (1992) Can J Microbiol , vol.38 , pp. 193-202
    • Gilchrist, A.1    Fisher, J.A.2    Smit, J.3
  • 11
    • 14844304655 scopus 로고    scopus 로고
    • The new bacterial cell biology: moving parts and subcellular architecture
    • Gitai, Z. (2005) The new bacterial cell biology: moving parts and subcellular architecture. Cell 120: 577-586.
    • (2005) Cell , vol.120 , pp. 577-586
    • Gitai, Z.1
  • 12
    • 0033988998 scopus 로고    scopus 로고
    • Regulation of stalk elongation by phosphate in Caulobacter crescentus
    • Gonin, M., Quardokus, E.M., O'Donnol, D., Maddock, J., and Brun, Y.V. (2000) Regulation of stalk elongation by phosphate in Caulobacter crescentus. J Bacteriol 182: 337-347.
    • (2000) J Bacteriol , vol.182 , pp. 337-347
    • Gonin, M.1    Quardokus, E.M.2    O'Donnol, D.3    Maddock, J.4    Brun, Y.V.5
  • 14
    • 0036037333 scopus 로고    scopus 로고
    • Proteomic analysis of the Caulobacter crescentus stalk indicates competence for nutrient uptake
    • Ireland, M.M.E., Karty, J.A., Quardokus, E.M., Reilly, J.P., and Brun, Y.V. (2002) Proteomic analysis of the Caulobacter crescentus stalk indicates competence for nutrient uptake. Mol Microbiol 45: 1029-1041.
    • (2002) Mol Microbiol , vol.45 , pp. 1029-1041
    • Ireland, M.M.E.1    Karty, J.A.2    Quardokus, E.M.3    Reilly, J.P.4    Brun, Y.V.5
  • 15
    • 78651311318 scopus 로고    scopus 로고
    • Interplay between manganese and zinc homeostasis in the human pathogen Streptococcus pneumoniae
    • Jacobsen, F.E., Kazmierczak, K.M., Lisher, J.P., Winkler, M.E., and Giedroc, D.P. (2011) Interplay between manganese and zinc homeostasis in the human pathogen Streptococcus pneumoniae. Metallomics 3: 38-41.
    • (2011) Metallomics , vol.3 , pp. 38-41
    • Jacobsen, F.E.1    Kazmierczak, K.M.2    Lisher, J.P.3    Winkler, M.E.4    Giedroc, D.P.5
  • 17
    • 60749102331 scopus 로고    scopus 로고
    • Membrane protein architects: the role of the BAM complex in outer membrane protein assembly
    • Knowles, T.J., Scott-Tucker, A., Overduin, M., and Henderson, I.R. (2009) Membrane protein architects: the role of the BAM complex in outer membrane protein assembly. Nat Rev Microbiol 7: 206-214.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 206-214
    • Knowles, T.J.1    Scott-Tucker, A.2    Overduin, M.3    Henderson, I.R.4
  • 18
    • 77950282521 scopus 로고    scopus 로고
    • The proline-rich domain of TonB possesses an extended polyproline II-like conformation of sufficient length to span the periplasm of Gram-negative bacteria
    • Köhler, S.D., Weber, A., Howard, S.P., Welte, W., and Drescher, M. (2010) The proline-rich domain of TonB possesses an extended polyproline II-like conformation of sufficient length to span the periplasm of Gram-negative bacteria. Protein Sci 19: 625-630.
    • (2010) Protein Sci , vol.19 , pp. 625-630
    • Köhler, S.D.1    Weber, A.2    Howard, S.P.3    Welte, W.4    Drescher, M.5
  • 19
    • 30844471175 scopus 로고    scopus 로고
    • Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK
    • Komeili, A., Li, Z., Newman, D.K., and Jensen, G.J. (2006) Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK. Science 311: 242-245.
    • (2006) Science , vol.311 , pp. 242-245
    • Komeili, A.1    Li, Z.2    Newman, D.K.3    Jensen, G.J.4
  • 20
    • 75049083437 scopus 로고    scopus 로고
    • Bactofilins, a ubiquitous class of cytoskeletal proteins mediating polar localization of a cell wall synthase in Caulobacter crescentus
    • Kühn, J., Briegel, A., Mörschel, E., Kahnt, J., Leser, K., Wick, S., etal. (2009) Bactofilins, a ubiquitous class of cytoskeletal proteins mediating polar localization of a cell wall synthase in Caulobacter crescentus. EMBO J 29: 327-339.
    • (2009) EMBO J , vol.29 , pp. 327-339
    • Kühn, J.1    Briegel, A.2    Mörschel, E.3    Kahnt, J.4    Leser, K.5    Wick, S.6
  • 21
    • 0020403342 scopus 로고
    • Induction and control of the autolytic system of Escherichia coli
    • Leduc, M., Kasra, R., and van Heijenoort, J. (1982) Induction and control of the autolytic system of Escherichia coli. J Bacteriol 152: 26-34.
    • (1982) J Bacteriol , vol.152 , pp. 26-34
    • Leduc, M.1    Kasra, R.2    van Heijenoort, J.3
  • 22
    • 13444257369 scopus 로고    scopus 로고
    • Mapping transposon insertion sites by touchdown PCR and hybrid degenerate primers
    • Levano-Garcia, J., Verjovski-Almeida, S., and Da Silva, A.C.R. (2005) Mapping transposon insertion sites by touchdown PCR and hybrid degenerate primers. BioTechniques 38: 225-229.
    • (2005) BioTechniques , vol.38 , pp. 225-229
    • Levano-Garcia, J.1    Verjovski-Almeida, S.2    Da Silva, A.C.R.3
  • 25
    • 80053936743 scopus 로고    scopus 로고
    • Reactions of the fluorescent sensor, Zinquin, with the zinc-proteome: adduct formation and ligand substitution
    • Nowakowski, A.B., and Petering, D.H. (2011) Reactions of the fluorescent sensor, Zinquin, with the zinc-proteome: adduct formation and ligand substitution. Inorg Chem 50: 10124-10133.
    • (2011) Inorg Chem , vol.50 , pp. 10124-10133
    • Nowakowski, A.B.1    Petering, D.H.2
  • 26
    • 78650497005 scopus 로고    scopus 로고
    • Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases
    • Paradis-Bleau, C., Markovski, M., Uehara, T., Lupoli, T.J., Walker, S., Kahne, D.E., and Bernhardt, T.G. (2010) Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases. Cell 143: 1110-1120.
    • (2010) Cell , vol.143 , pp. 1110-1120
    • Paradis-Bleau, C.1    Markovski, M.2    Uehara, T.3    Lupoli, T.J.4    Walker, S.5    Kahne, D.E.6    Bernhardt, T.G.7
  • 27
    • 0031798662 scopus 로고    scopus 로고
    • The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli
    • Patzer, S.I., and Hantke, K. (1998) The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol Microbiol 28: 1199-1210.
    • (1998) Mol Microbiol , vol.28 , pp. 1199-1210
    • Patzer, S.I.1    Hantke, K.2
  • 28
    • 39049114368 scopus 로고    scopus 로고
    • Dimorphic prosthecate bacteria: the genera Caulobacter, Asticcacaulis, Hyphomicrobium, Pedomicrobium, Hyphomonas and Thiodendron
    • Poindexter, J. (2006) Dimorphic prosthecate bacteria: the genera Caulobacter, Asticcacaulis, Hyphomicrobium, Pedomicrobium, Hyphomonas and Thiodendron. Prokaryotes 5: 72-90.
    • (2006) Prokaryotes , vol.5 , pp. 72-90
    • Poindexter, J.1
  • 29
    • 0000552888 scopus 로고
    • Biological properties and classification of the Caulobacter group
    • Poindexter, J.S. (1964) Biological properties and classification of the Caulobacter group. Bacteriol Rev 28: 231-295.
    • (1964) Bacteriol Rev , vol.28 , pp. 231-295
    • Poindexter, J.S.1
  • 30
    • 0018087772 scopus 로고
    • Selection for nonbuoyant morphological mutants of Caulobacter crescentus
    • Poindexter, J.S. (1978) Selection for nonbuoyant morphological mutants of Caulobacter crescentus. J Bacteriol 135: 1141-1145.
    • (1978) J Bacteriol , vol.135 , pp. 1141-1145
    • Poindexter, J.S.1
  • 31
    • 0001489722 scopus 로고
    • The fine structure of stalked bacteria belonging to the family Caulobacteraceae
    • Poindexter, J.S., and Cohen-Bazire, G. (1964) The fine structure of stalked bacteria belonging to the family Caulobacteraceae. J Cell Biol 23: 587-607.
    • (1964) J Cell Biol , vol.23 , pp. 587-607
    • Poindexter, J.S.1    Cohen-Bazire, G.2
  • 32
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A., and Zhang, Y. (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protocols 5: 725-738.
    • (2010) Nat Protocols , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 33
    • 77749296015 scopus 로고    scopus 로고
    • The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane beta-barrel proteins in Caulobacter crescentus
    • Ryan, K.R., Taylor, J.A., and Bowers, L.M. (2010) The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane beta-barrel proteins in Caulobacter crescentus. Microbiology 156: 742-756.
    • (2010) Microbiology , vol.156 , pp. 742-756
    • Ryan, K.R.1    Taylor, J.A.2    Bowers, L.M.3
  • 34
    • 0018817672 scopus 로고
    • Effects of acidification on mobilization of heavy metals and radionuclides from the sediments of a freshwater lake
    • Schindler, D.W., Hesslein, R.H., Wagemann, R., and Broecker, W.S. (1980) Effects of acidification on mobilization of heavy metals and radionuclides from the sediments of a freshwater lake. Can J Fish Aquat Sci 37: 373-377.
    • (1980) Can J Fish Aquat Sci , vol.37 , pp. 373-377
    • Schindler, D.W.1    Hesslein, R.H.2    Wagemann, R.3    Broecker, W.S.4
  • 35
    • 84870871957 scopus 로고    scopus 로고
    • General protein diffusion barriers create compartments within bacterial cells
    • Schlimpert, S., Klein, E.A., Briegel, A., Hughes, V., Kahnt, J., Bolte, K., etal. (2012) General protein diffusion barriers create compartments within bacterial cells. Cell 151: 1270-1282.
    • (2012) Cell , vol.151 , pp. 1270-1282
    • Schlimpert, S.1    Klein, E.A.2    Briegel, A.3    Hughes, V.4    Kahnt, J.5    Bolte, K.6
  • 36
    • 0013883373 scopus 로고
    • The development of cellular stalks in bacteria
    • Schmidt, J.M., and Stanier, R.Y. (1966) The development of cellular stalks in bacteria. J Cell Biol 28: 423-436.
    • (1966) J Cell Biol , vol.28 , pp. 423-436
    • Schmidt, J.M.1    Stanier, R.Y.2
  • 37
    • 34249820257 scopus 로고    scopus 로고
    • Roles of His-rich Hpn and Hpn-like proteins in Helicobacter pylori nickel physiology
    • Seshadri, S., Benoit, S.L., and Maier, R.J. (2007) Roles of His-rich Hpn and Hpn-like proteins in Helicobacter pylori nickel physiology. J Bacteriol 189: 4120-4126.
    • (2007) J Bacteriol , vol.189 , pp. 4120-4126
    • Seshadri, S.1    Benoit, S.L.2    Maier, R.J.3
  • 38
    • 0019400973 scopus 로고
    • Periodic surface array in Caulobacter crescentus: fine structure and chemical analysis
    • Smit, J., Grano, D.A., Glaeser, R.M., and Agabian, N. (1981) Periodic surface array in Caulobacter crescentus: fine structure and chemical analysis. J Bacteriol 146: 1135-1150.
    • (1981) J Bacteriol , vol.146 , pp. 1135-1150
    • Smit, J.1    Grano, D.A.2    Glaeser, R.M.3    Agabian, N.4
  • 39
    • 0026778803 scopus 로고
    • The S-layer of Caulobacter crescentus: three-dimensional image reconstruction and structure analysis by electron microscopy
    • Smit, J., Engelhardt, H., Volker, S., Smith, S.H., and Baumeister, W. (1992) The S-layer of Caulobacter crescentus: three-dimensional image reconstruction and structure analysis by electron microscopy. J Bacteriol 174: 6527-6538.
    • (1992) J Bacteriol , vol.174 , pp. 6527-6538
    • Smit, J.1    Engelhardt, H.2    Volker, S.3    Smith, S.H.4    Baumeister, W.5
  • 40
    • 0032874101 scopus 로고    scopus 로고
    • The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli
    • Terrak, M., Ghosh, T.K., Van Heijenoort, J., Van Beeumen, J., Lampilas, M., Aszodi, J., etal. (1999) The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli. Mol Microbiol 34: 350-364.
    • (1999) Mol Microbiol , vol.34 , pp. 350-364
    • Terrak, M.1    Ghosh, T.K.2    Van Heijenoort, J.3    Van Beeumen, J.4    Lampilas, M.5    Aszodi, J.6
  • 42
    • 11844281590 scopus 로고    scopus 로고
    • Caulobacter crescentus requires RodA and MreB for stalk synthesis and prevention of ectopic pole formation
    • Wagner, J.K., Galvani, C.D., and Brun, Y.V. (2005) Caulobacter crescentus requires RodA and MreB for stalk synthesis and prevention of ectopic pole formation. J Bacteriol 187: 544-553.
    • (2005) J Bacteriol , vol.187 , pp. 544-553
    • Wagner, J.K.1    Galvani, C.D.2    Brun, Y.V.3
  • 44
    • 0028004268 scopus 로고
    • Characterization of mutants of Caulobacter crescentus defective in surface attachment of the paracrystalline surface layer
    • Walker, S.G., Karunaratne, D.N., Ravenscroft, N., and Smit, J. (1994) Characterization of mutants of Caulobacter crescentus defective in surface attachment of the paracrystalline surface layer. J Bacteriol 176: 6312-6323.
    • (1994) J Bacteriol , vol.176 , pp. 6312-6323
    • Walker, S.G.1    Karunaratne, D.N.2    Ravenscroft, N.3    Smit, J.4
  • 45
    • 34250291740 scopus 로고
    • Sublethal effects of heavy metal contaminated sediment on midge larvae (Chironomus tentans)
    • Wentsel, R., McIntosh, A., and Atchison, G. (1977) Sublethal effects of heavy metal contaminated sediment on midge larvae (Chironomus tentans). Hydrobiologia 56: 153-156.
    • (1977) Hydrobiologia , vol.56 , pp. 153-156
    • Wentsel, R.1    McIntosh, A.2    Atchison, G.3
  • 47
    • 49649111573 scopus 로고    scopus 로고
    • Protein-based organelles in bacteria: carboxysomes and related microcompartments
    • Yeates, T.O., Kerfeld, C.A., Heinhorst, S., Cannon, G.C., and Shively, J.M. (2008) Protein-based organelles in bacteria: carboxysomes and related microcompartments. Nat Rev Microbiol 6: 681-691.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 681-691
    • Yeates, T.O.1    Kerfeld, C.A.2    Heinhorst, S.3    Cannon, G.C.4    Shively, J.M.5
  • 48
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y. (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9: 40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.