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Volumn 89, Issue 2, 2013, Pages 350-371

Bypassing the need for subcellular localization of a polysaccharide export-anchor complex by overexpressing its protein subunits

Author keywords

[No Author keywords available]

Indexed keywords

LIPID TRANSFER PROTEIN; PROTEIN HFSA; PROTEIN HFSB; PROTEIN HFSD; PROTEIN PODJ; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84880133296     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12281     Document Type: Article
Times cited : (11)

References (64)
  • 1
    • 80051726238 scopus 로고    scopus 로고
    • Regulatory cohesion of cell cycle and cell differentiation through interlinked phosphorylation and second messenger networks
    • Abel, S., Chien, P., Wassmann, P., Schirmer, T., Kaever, V., Laub, M., etal. (2011) Regulatory cohesion of cell cycle and cell differentiation through interlinked phosphorylation and second messenger networks. Mol Cell 43: 550-560.
    • (2011) Mol Cell , vol.43 , pp. 550-560
    • Abel, S.1    Chien, P.2    Wassmann, P.3    Schirmer, T.4    Kaever, V.5    Laub, M.6
  • 2
    • 0026009504 scopus 로고
    • Genetic analysis of a temporally transcribed chemotaxis gene cluster in Caulobacter crescentus
    • Alley, M.R., Gomes, S.L., Alexander, W., and Shapiro, L. (1991) Genetic analysis of a temporally transcribed chemotaxis gene cluster in Caulobacter crescentus. Genetics 129: 333-341.
    • (1991) Genetics , vol.129 , pp. 333-341
    • Alley, M.R.1    Gomes, S.L.2    Alexander, W.3    Shapiro, L.4
  • 3
    • 0026628961 scopus 로고
    • Polar localization of a bacterial chemoreceptor
    • Alley, M.R., Maddock, J.R., and Shapiro, L. (1992) Polar localization of a bacterial chemoreceptor. Genes Dev 6: 825-836.
    • (1992) Genes Dev , vol.6 , pp. 825-836
    • Alley, M.R.1    Maddock, J.R.2    Shapiro, L.3
  • 4
    • 0021711731 scopus 로고
    • Simple, rapid, and quantitative release of periplasmic proteins by chloroform
    • Ames, G.F., Prody, C., and Kustu, S. (1984) Simple, rapid, and quantitative release of periplasmic proteins by chloroform. J Bacteriol 160: 1181-1183.
    • (1984) J Bacteriol , vol.160 , pp. 1181-1183
    • Ames, G.F.1    Prody, C.2    Kustu, S.3
  • 5
    • 0017723075 scopus 로고
    • Polysaccharide capsule of Escherichia coli: microscope study of its size, structure, and sites of synthesis
    • Bayer, M.E., and Thurow, H. (1977) Polysaccharide capsule of Escherichia coli: microscope study of its size, structure, and sites of synthesis. J Bacteriol 130: 911-936.
    • (1977) J Bacteriol , vol.130 , pp. 911-936
    • Bayer, M.E.1    Thurow, H.2
  • 6
    • 0041700114 scopus 로고    scopus 로고
    • A conserved oligomerization domain in Drosophila Bazooka/PAR-3 is important for apical localization and epithelial polarity
    • Benton, R., and Johnston, D.S. (2003) A conserved oligomerization domain in Drosophila Bazooka/PAR-3 is important for apical localization and epithelial polarity. Curr Biol 13: 1330-1334.
    • (2003) Curr Biol , vol.13 , pp. 1330-1334
    • Benton, R.1    Johnston, D.S.2
  • 7
    • 1342283002 scopus 로고    scopus 로고
    • Development of surface adhesion in Caulobacter crescentus
    • Bodenmiller, D., Toh, E., and Brun, Y.V. (2004) Development of surface adhesion in Caulobacter crescentus. J Bacteriol 186: 1438-1447.
    • (2004) J Bacteriol , vol.186 , pp. 1438-1447
    • Bodenmiller, D.1    Toh, E.2    Brun, Y.V.3
  • 8
    • 0027169049 scopus 로고
    • Expression of the capsular K5 polysaccharide of Escherichia coli: biochemical and electron microscopic analyses of mutants with defects in region 1 of the K5 gene cluster
    • Bronner, D., Sieberth, V., Pazzani, C., Roberts, I.S., Boulnois, G.J., Jann, B., and Jann, K. (1993) Expression of the capsular K5 polysaccharide of Escherichia coli: biochemical and electron microscopic analyses of mutants with defects in region 1 of the K5 gene cluster. J Bacteriol 175: 5984-5992.
    • (1993) J Bacteriol , vol.175 , pp. 5984-5992
    • Bronner, D.1    Sieberth, V.2    Pazzani, C.3    Roberts, I.S.4    Boulnois, G.J.5    Jann, B.6    Jann, K.7
  • 9
    • 52949102235 scopus 로고    scopus 로고
    • Complex regulatory pathways coordinate cell-cycle progression and development in Caulobacter crescentus
    • Poole, R.K. (ed.). London: Academic Press-Elsevier Science
    • 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. In Advances in Microbial Physiology, Vol. 54. Poole, R.K. (ed.). London: Academic Press-Elsevier Science, pp. 1-101.
    • (2009) Advances in Microbial Physiology , vol.54 , pp. 1-101
    • Brown, P.J.B.1    Hardy, G.G.2    Trimble, M.J.3    Brun, Y.V.4
  • 10
    • 84855935515 scopus 로고    scopus 로고
    • Improved enrichment and proteomic identification of outer membrane proteins from a Gram-negative bacterium: focus on Caulobacter crescentus
    • Cao, Y., Johnson, H.M., and Bazemore-Walker, C.R. (2012) Improved enrichment and proteomic identification of outer membrane proteins from a Gram-negative bacterium: focus on Caulobacter crescentus. Proteomics 12: 251-262.
    • (2012) Proteomics , vol.12 , pp. 251-262
    • Cao, Y.1    Johnson, H.M.2    Bazemore-Walker, C.R.3
  • 12
    • 0141677738 scopus 로고    scopus 로고
    • The HfaB and HfaD adhesion proteins of Caulobacter crescentus are localized in the stalk
    • Cole, J.L., Hardy, G.G., Bodenmiller, D., Toh, E., Hinz, A., and Brun, Y.V. (2003) The HfaB and HfaD adhesion proteins of Caulobacter crescentus are localized in the stalk. Mol Microbiol 49: 1671-1683.
    • (2003) Mol Microbiol , vol.49 , pp. 1671-1683
    • Cole, J.L.1    Hardy, G.G.2    Bodenmiller, D.3    Toh, E.4    Hinz, A.5    Brun, Y.V.6
  • 13
    • 33847779058 scopus 로고    scopus 로고
    • The 3D structure of a periplasm-spanning platform required for assembly of group 1 capsular polysaccharides in Escherichia coli
    • Collins, R.F., Beis, K., Dong, C., Botting, C.H., McDonnell, C., Ford, R.C., etal. (2007) The 3D structure of a periplasm-spanning platform required for assembly of group 1 capsular polysaccharides in Escherichia coli. Proc Natl Acad Sci USA 104: 2390-2395.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2390-2395
    • Collins, R.F.1    Beis, K.2    Dong, C.3    Botting, C.H.4    McDonnell, C.5    Ford, R.C.6
  • 14
    • 77749327485 scopus 로고    scopus 로고
    • Getting in the loop: regulation of development in Caulobacter crescentus
    • Curtis, P.D., and Brun, Y.V. (2010) Getting in the loop: regulation of development in Caulobacter crescentus. Microbiol Mol Biol Rev 74: 13-41.
    • (2010) Microbiol Mol Biol Rev , vol.74 , pp. 13-41
    • Curtis, P.D.1    Brun, Y.V.2
  • 15
    • 84860600234 scopus 로고    scopus 로고
    • The scaffolding and signaling 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 signaling 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
  • 16
    • 63849263023 scopus 로고    scopus 로고
    • Pivotal roles of the outer membrane polysaccharide export and polysaccharide copolymerase protein families in export of extracellular polysaccharides in Gram-negative bacteria
    • Cuthbertson, L., Mainprize, I.L., Naismith, J.H., and Whitfield, C. (2009) Pivotal roles of the outer membrane polysaccharide export and polysaccharide copolymerase protein families in export of extracellular polysaccharides in Gram-negative bacteria. Microbiol Mol Biol Rev 73: 155-177.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 155-177
    • Cuthbertson, L.1    Mainprize, I.L.2    Naismith, J.H.3    Whitfield, C.4
  • 17
    • 0034602835 scopus 로고    scopus 로고
    • Translocation of group 1 capsular polysaccharide to the surface of Escherichia coli requires a multimeric complex in the outer membrane
    • Drummelsmith, J., and Whitfield, C. (2000) Translocation of group 1 capsular polysaccharide to the surface of Escherichia coli requires a multimeric complex in the outer membrane. EMBO J 19: 57-66.
    • (2000) EMBO J , vol.19 , pp. 57-66
    • Drummelsmith, J.1    Whitfield, C.2
  • 18
    • 58149485506 scopus 로고    scopus 로고
    • Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression
    • Duerig, A., Abel, S., Folcher, M., Nicollier, M., Schwede, T., Amiot, N., etal. (2009) Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression. Genes Dev 23: 93-104.
    • (2009) Genes Dev , vol.23 , pp. 93-104
    • Duerig, A.1    Abel, S.2    Folcher, M.3    Nicollier, M.4    Schwede, T.5    Amiot, N.6
  • 19
    • 0017740506 scopus 로고
    • Envelope-associated nucleoid from Caulobacter crescentus stalked and swarmer cells
    • Evinger, M., and Agabian, N. (1977) Envelope-associated nucleoid from Caulobacter crescentus stalked and swarmer cells. J Bacteriol 132: 294-301.
    • (1977) J Bacteriol , vol.132 , pp. 294-301
    • Evinger, M.1    Agabian, N.2
  • 20
    • 84871974528 scopus 로고    scopus 로고
    • Xanthan chain length is modulated by increasing the availability of the polysaccharide copolymerase protein GumC and the outer membrane polysaccharide export protein GumB
    • Galván, E.M., Ielmini, M.V., Patel, Y.N., Bianco, M.I., Franceschini, E.A., Schneider, J.C., and Ielpi, L. (2013) Xanthan chain length is modulated by increasing the availability of the polysaccharide copolymerase protein GumC and the outer membrane polysaccharide export protein GumB. Glycobiology 23: 259-272.
    • (2013) Glycobiology , vol.23 , pp. 259-272
    • Galván, E.M.1    Ielmini, M.V.2    Patel, Y.N.3    Bianco, M.I.4    Franceschini, E.A.5    Schneider, J.C.6    Ielpi, L.7
  • 21
    • 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
  • 22
    • 79955770162 scopus 로고    scopus 로고
    • Scaffold proteins: hubs for controlling the flow of cellular information
    • Good, M.C., Zalatan, J.G., and Lim, W.A. (2011) Scaffold proteins: hubs for controlling the flow of cellular information. Science 332: 680-686.
    • (2011) Science , vol.332 , pp. 680-686
    • Good, M.C.1    Zalatan, J.G.2    Lim, W.A.3
  • 24
    • 80054001998 scopus 로고    scopus 로고
    • Synthesis of capsular polysaccharide at the division septum of Streptococcus pneumoniae is dependent on a bacterial tyrosine kinase
    • Henriques, M.X., Rodrigues, T., Carido, M., Ferreira, L., and Filipe, S.R. (2011) Synthesis of capsular polysaccharide at the division septum of Streptococcus pneumoniae is dependent on a bacterial tyrosine kinase. Mol Microbiol 82: 515-534.
    • (2011) Mol Microbiol , vol.82 , pp. 515-534
    • Henriques, M.X.1    Rodrigues, T.2    Carido, M.3    Ferreira, L.4    Filipe, S.R.5
  • 25
    • 0037329155 scopus 로고    scopus 로고
    • The Caulobacter crescentus polar organelle development protein PodJ is differentially localized and is required for polar targeting of the PleC development regulator
    • Hinz, A.J., Larson, D.E., Smith, C.S., and Brun, Y.V. (2003) The Caulobacter crescentus polar organelle development protein PodJ is differentially localized and is required for polar targeting of the PleC development regulator. Mol Microbiol 47: 929-941.
    • (2003) Mol Microbiol , vol.47 , pp. 929-941
    • Hinz, A.J.1    Larson, D.E.2    Smith, C.S.3    Brun, Y.V.4
  • 26
    • 0030752541 scopus 로고    scopus 로고
    • Transcriptional and mutational analyses of the rpoN operon in Caulobacter crescentus
    • Janakiraman, R.S., and Brun, Y.V. (1997) Transcriptional and mutational analyses of the rpoN operon in Caulobacter crescentus. J Bacteriol 179: 5138-5147.
    • (1997) J Bacteriol , vol.179 , pp. 5138-5147
    • Janakiraman, R.S.1    Brun, Y.V.2
  • 27
    • 0028125086 scopus 로고
    • Caulobacter flagellar function, but not assembly, requires FliL, a non-polarly localized membrane protein present in all cell types
    • Jenal, U., White, J., and Shapiro, L. (1994) Caulobacter flagellar function, but not assembly, requires FliL, a non-polarly localized membrane protein present in all cell types. J Mol Biol 243: 227-244.
    • (1994) J Mol Biol , vol.243 , pp. 227-244
    • Jenal, U.1    White, J.2    Shapiro, L.3
  • 28
    • 0017406740 scopus 로고
    • Isolation of spontaneously derived mutants of Caulobacter crescentus
    • Johnson, R.C., and Ely, B. (1977) Isolation of spontaneously derived mutants of Caulobacter crescentus. Genetics 86: 25-32.
    • (1977) Genetics , vol.86 , pp. 25-32
    • Johnson, R.C.1    Ely, B.2
  • 29
    • 80054892595 scopus 로고    scopus 로고
    • Poles apart: prokaryotic polar organelles and their spatial regulation
    • pii: a006809
    • Kirkpatrick, C.L., and Viollier, P.H. (2011) Poles apart: prokaryotic polar organelles and their spatial regulation. Cold Spring Harb Perspect Biol 3: pii: a006809.
    • (2011) Cold Spring Harb Perspect Biol , vol.3
    • Kirkpatrick, C.L.1    Viollier, P.H.2
  • 30
    • 0025353051 scopus 로고
    • Further electron microscopic studies on the expression of Escherichia coli group II capsules
    • Kroncke, K.D., Golecki, J.R., and Jann, K. (1990) Further electron microscopic studies on the expression of Escherichia coli group II capsules. J Bacteriol 172: 3469-3472.
    • (1990) J Bacteriol , vol.172 , pp. 3469-3472
    • Kroncke, K.D.1    Golecki, J.R.2    Jann, K.3
  • 31
    • 0036316102 scopus 로고    scopus 로고
    • Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains
    • Kuersten, S., Arts, G.-J., Walther, T.C., Englmeier, L., and Mattaj, I.W. (2002) Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains. Mol Cell Biol 22: 5708-5720.
    • (2002) Mol Cell Biol , vol.22 , pp. 5708-5720
    • Kuersten, S.1    Arts, G.-J.2    Walther, T.C.3    Englmeier, L.4    Mattaj, I.W.5
  • 32
    • 0026594850 scopus 로고
    • Analysis of a Caulobacter crescentus gene cluster involved in attachment of the holdfast to the cell
    • Kurtz, H.D., and Smith, J. (1992) Analysis of a Caulobacter crescentus gene cluster involved in attachment of the holdfast to the cell. J Bacteriol 174: 687-694.
    • (1992) J Bacteriol , vol.174 , pp. 687-694
    • Kurtz, H.D.1    Smith, J.2
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
  • 35
    • 33745898224 scopus 로고    scopus 로고
    • Holdfast formation in motile swarmer cells optimizes surface attachment during Caulobacter crescentus development
    • Levi, A., and Jenal, U. (2006) Holdfast formation in motile swarmer cells optimizes surface attachment during Caulobacter crescentus development. J Bacteriol 188: 5315-5318.
    • (2006) J Bacteriol , vol.188 , pp. 5315-5318
    • Levi, A.1    Jenal, U.2
  • 37
    • 33645052464 scopus 로고    scopus 로고
    • The cell surface expression of group 2 capsular polysaccharides in Escherichia coli: the role of KpsD, RhsA and a multi-protein complex at the pole of the cell
    • McNulty, C., Thompson, J., Barrett, B., Lord, L., Andersen, C., and Roberts, I.S. (2006) The cell surface expression of group 2 capsular polysaccharides in Escherichia coli: the role of KpsD, RhsA and a multi-protein complex at the pole of the cell. Mol Microbiol 59: 907-922.
    • (2006) Mol Microbiol , vol.59 , pp. 907-922
    • McNulty, C.1    Thompson, J.2    Barrett, B.3    Lord, L.4    Andersen, C.5    Roberts, I.S.6
  • 38
    • 0000698333 scopus 로고
    • Characterization of the adhesive holdfast of marine and freshwater Caulobacters
    • Merker, R.I., and Smit, J. (1988) Characterization of the adhesive holdfast of marine and freshwater Caulobacters. Appl Environ Microbiol 54: 2078-2085.
    • (1988) Appl Environ Microbiol , vol.54 , pp. 2078-2085
    • Merker, R.I.1    Smit, J.2
  • 39
    • 0042018901 scopus 로고
    • Phosphate-irrepressible alkaline phosphatase of Zymomonas mobilis
    • Michel, G.P.F., and Baratti, J.C. (1989) Phosphate-irrepressible alkaline phosphatase of Zymomonas mobilis. J Gen Microbiol 135: 453-460.
    • (1989) J Gen Microbiol , vol.135 , pp. 453-460
    • Michel, G.P.F.1    Baratti, J.C.2
  • 40
    • 0008065838 scopus 로고
    • Attachment and rosette formation by hyphomicrobia
    • Moore, R.L., and Marshall, K.C. (1981) Attachment and rosette formation by hyphomicrobia. Appl Environ Microbiol 42: 751-757.
    • (1981) Appl Environ Microbiol , vol.42 , pp. 751-757
    • Moore, R.L.1    Marshall, K.C.2
  • 41
    • 16344381001 scopus 로고    scopus 로고
    • The gellan gum biosynthetic genes gelC and gelE encode two separate polypeptides homologous to the activator and the kinase domains of tyrosine autokinases
    • Moreira, L.M., Hoffmann, K., Albano, H., Becker, A., Niehaus, K., and Sá-Correia, I. (2004) The gellan gum biosynthetic genes gelC and gelE encode two separate polypeptides homologous to the activator and the kinase domains of tyrosine autokinases. J Mol Microbiol Biotechnol 8: 43-57.
    • (2004) J Mol Microbiol Biotechnol , vol.8 , pp. 43-57
    • Moreira, L.M.1    Hoffmann, K.2    Albano, H.3    Becker, A.4    Niehaus, K.5    Sá-Correia, I.6
  • 42
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • Nooren, I.M.A., and Thornton, J.M. (2003) Diversity of protein-protein interactions. EMBO J 22: 3486-3492.
    • (2003) EMBO J , vol.22 , pp. 3486-3492
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 43
    • 0015720893 scopus 로고
    • Asticcacaulis biprosthecum sp. nov. Life cycle, morphology and cultural characteristics
    • Pate, J., Porter, J., and Jordan, T. (1973) Asticcacaulis biprosthecum sp. nov. Life cycle, morphology and cultural characteristics. Antonie Van Leeuwenhoek 39: 569-583.
    • (1973) Antonie Van Leeuwenhoek , vol.39 , pp. 569-583
    • Pate, J.1    Porter, J.2    Jordan, T.3
  • 44
    • 84861371522 scopus 로고    scopus 로고
    • Functional characterization of UDP-glucose: undecaprenyl-phosphate glucose-1-phosphate transferases of Escherichia coli and Caulobacter crescentus
    • Patel, K.B., Toh, E., Fernandez, X.B., Hanuszkiewicz, A., Hardy, G.G., Brun, Y.V., etal. (2012) Functional characterization of UDP-glucose: undecaprenyl-phosphate glucose-1-phosphate transferases of Escherichia coli and Caulobacter crescentus. J Bacteriol 194: 2646-2657.
    • (2012) J Bacteriol , vol.194 , pp. 2646-2657
    • Patel, K.B.1    Toh, E.2    Fernandez, X.B.3    Hanuszkiewicz, A.4    Hardy, G.G.5    Brun, Y.V.6
  • 45
    • 0030843523 scopus 로고    scopus 로고
    • Computer-based analyses of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria
    • Paulsen, I.T., Beness, A.M., and Saier, M.H., Jr (1997) Computer-based analyses of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria. Microbiology 143: 2685-2699.
    • (1997) Microbiology , vol.143 , pp. 2685-2699
    • Paulsen, I.T.1    Beness, A.M.2    Saier Jr., M.H.3
  • 46
    • 0000552888 scopus 로고
    • Biological properties and classification of Caulobacter group
    • Poindexter, J.S. (1964) Biological properties and classification of Caulobacter group. Bacteriol Rev 28: 231-295.
    • (1964) Bacteriol Rev , vol.28 , pp. 231-295
    • Poindexter, J.S.1
  • 47
    • 0024618580 scopus 로고
    • Cloning, sequencing, and characterization of the principal acid phosphatase, the phoC+ product, from Zymomonas mobilis
    • Pond, J.L., Eddy, C.K., Mackenzie, K.F., Conway, T., Borecky, D.J., and Ingram, L.O. (1989) Cloning, sequencing, and characterization of the principal acid phosphatase, the phoC+ product, from Zymomonas mobilis. J Bacteriol 171: 767-774.
    • (1989) J Bacteriol , vol.171 , pp. 767-774
    • Pond, J.L.1    Eddy, C.K.2    Mackenzie, K.F.3    Conway, T.4    Borecky, D.J.5    Ingram, L.O.6
  • 48
    • 0041935939 scopus 로고    scopus 로고
    • Bethesda, MD: US National Institutes of Health.
    • Rasband, W.S. (1997-2012) ImageJ. Bethesda, MD: US National Institutes of Health.
    • (1997) ImageJ
    • Rasband, W.S.1
  • 49
    • 0027184288 scopus 로고
    • Biosynthesis of succinoglycan, a symbiotically important exopolysaccharide of Rhizobium meliloti
    • Reuber, T.L., and Walker, G.C. (1993) Biosynthesis of succinoglycan, a symbiotically important exopolysaccharide of Rhizobium meliloti. Cell 74: 269-280.
    • (1993) Cell , vol.74 , pp. 269-280
    • Reuber, T.L.1    Walker, G.C.2
  • 51
    • 0023546657 scopus 로고
    • Translocation of capsular polysaccharides in pathogenic strains of Escherichia coli requires a 60-kilodalton periplasmic protein
    • Silver, R.P., Aaronson, W., and Vann, W.F. (1987) Translocation of capsular polysaccharides in pathogenic strains of Escherichia coli requires a 60-kilodalton periplasmic protein. J Bacteriol 169: 5489-5495.
    • (1987) J Bacteriol , vol.169 , pp. 5489-5495
    • Silver, R.P.1    Aaronson, W.2    Vann, W.F.3
  • 52
    • 79955024764 scopus 로고    scopus 로고
    • High-throughput, subpixel precision analysis of bacterial morphogenesis and intracellular spatio-temporal dynamics
    • Sliusarenko, O., Heinritz, J., Emonet, T., and Jacobs-Wagner, C. (2011) High-throughput, subpixel precision analysis of bacterial morphogenesis and intracellular spatio-temporal dynamics. Mol Microbiol 80: 612-627.
    • (2011) Mol Microbiol , vol.80 , pp. 612-627
    • Sliusarenko, O.1    Heinritz, J.2    Emonet, T.3    Jacobs-Wagner, C.4
  • 53
    • 0037317866 scopus 로고    scopus 로고
    • Identification of genes required for synthesis of the adhesive holdfast in Caulobacter crescentus
    • Smith, C.S., Hinz, A., Bodenmiller, D., Larson, D.E., and Brun, Y.V. (2003) Identification of genes required for synthesis of the adhesive holdfast in Caulobacter crescentus. J Bacteriol 185: 1432-1442.
    • (2003) J Bacteriol , vol.185 , pp. 1432-1442
    • Smith, C.S.1    Hinz, A.2    Bodenmiller, D.3    Larson, D.E.4    Brun, Y.V.5
  • 54
    • 33744913312 scopus 로고    scopus 로고
    • Staphylococcus aureus operates protein-tyrosine phosphorylation through a specific mechanism
    • Soulat, D., Jault, J.-M., Duclos, B., Geourjon, C., Cozzone, A.J., and Grangeasse, C. (2006) Staphylococcus aureus operates protein-tyrosine phosphorylation through a specific mechanism. J Biol Chem 281: 14048-14056.
    • (2006) J Biol Chem , vol.281 , pp. 14048-14056
    • Soulat, D.1    Jault, J.-M.2    Duclos, B.3    Geourjon, C.4    Cozzone, A.J.5    Grangeasse, C.6
  • 55
    • 52949120316 scopus 로고    scopus 로고
    • Characterization of the Caulobacter crescentus holdfast polysaccharide biosynthesis pathway reveals significant redundancy in the initiating glycosyltransferase and polymerase steps
    • Toh, E., Kurtz, H.D., Jr, and Brun, Y.V. (2008) Characterization of the Caulobacter crescentus holdfast polysaccharide biosynthesis pathway reveals significant redundancy in the initiating glycosyltransferase and polymerase steps. J Bacteriol 190: 7219-7231.
    • (2008) J Bacteriol , vol.190 , pp. 7219-7231
    • Toh, E.1    Kurtz Jr., H.D.2    Brun, Y.V.3
  • 56
    • 71549156538 scopus 로고    scopus 로고
    • Mechanisms and regulation of polar surface attachment in Agrobacterium tumefaciens
    • Tomlinson, A.D., and Fuqua, C. (2009) Mechanisms and regulation of polar surface attachment in Agrobacterium tumefaciens. Curr Opin Microbiol 12: 708-714.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 708-714
    • Tomlinson, A.D.1    Fuqua, C.2
  • 57
    • 0034884131 scopus 로고    scopus 로고
    • Proteolysis of the Caulobacter McpA chemoreceptor is cell cycle regulated by a ClpX-dependent pathway
    • Tsai, J.-W., and Alley, M.R.K. (2001) Proteolysis of the Caulobacter McpA chemoreceptor is cell cycle regulated by a ClpX-dependent pathway. J Bacteriol 183: 5001-5007.
    • (2001) J Bacteriol , vol.183 , pp. 5001-5007
    • Tsai, J.-W.1    Alley, M.R.K.2
  • 59
    • 0037108973 scopus 로고    scopus 로고
    • Identification of a localization factor for the polar positioning of bacterial structural and regulatory proteins
    • Viollier, P.H., Sternheim, N., and Shapiro, L. (2002) Identification of a localization factor for the polar positioning of bacterial structural and regulatory proteins. Proc Natl Acad Sci USA 99: 13831-13836.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13831-13836
    • Viollier, P.H.1    Sternheim, N.2    Shapiro, L.3
  • 60
    • 0031748633 scopus 로고    scopus 로고
    • Evidence for a role for the gumB and gumC gene products in the formation of xanthan from its pentasaccharide repeating unit by Xanthomonas campestris
    • Vojnov, A.A., Zorreguieta, A., Dow, J.M., Daniels, M.J., and Dankert, M.A. (1998) Evidence for a role for the gumB and gumC gene products in the formation of xanthan from its pentasaccharide repeating unit by Xanthomonas campestris. Microbiology 144: 1487-1493.
    • (1998) Microbiology , vol.144 , pp. 1487-1493
    • Vojnov, A.A.1    Zorreguieta, A.2    Dow, J.M.3    Daniels, M.J.4    Dankert, M.A.5
  • 61
    • 0027475809 scopus 로고
    • A histidine protein kinase is involved in polar organelle development in Caulobacter crescentus
    • Wang, S.P., Sharma, P.L., Schoenlein, P.V., and Ely, B. (1993) A histidine protein kinase is involved in polar organelle development in Caulobacter crescentus. Proc Natl Acad Sci USA 90: 630-634.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 630-634
    • Wang, S.P.1    Sharma, P.L.2    Schoenlein, P.V.3    Ely, B.4
  • 62
    • 33746356503 scopus 로고    scopus 로고
    • Biosynthesis and assembly of capsular polysaccharides in Escherichia coli
    • Whitfield, C. (2006) Biosynthesis and assembly of capsular polysaccharides in Escherichia coli. Annu Rev Biochem 75: 39-68.
    • (2006) Annu Rev Biochem , vol.75 , pp. 39-68
    • Whitfield, C.1
  • 63
    • 38849207749 scopus 로고    scopus 로고
    • Stop and go: regulation of chain length in the biosynthesis of bacterial polysaccharides
    • Whitfield, C., and Larue, K. (2008) Stop and go: regulation of chain length in the biosynthesis of bacterial polysaccharides. Nat Struct Mol Biol 15: 121-123.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 121-123
    • Whitfield, C.1    Larue, K.2
  • 64
    • 0035951884 scopus 로고    scopus 로고
    • Phosphorylation of Wzc, a tyrosine autokinase, is essential for assembly of group 1 capsular polysaccharides in Escherichia coli
    • Wugeditsch, T., Paiment, A., Hocking, J., Drummelsmith, J., Forrester, C., and Whitfield, C. (2001) Phosphorylation of Wzc, a tyrosine autokinase, is essential for assembly of group 1 capsular polysaccharides in Escherichia coli. J Biol Chem 276: 2361-2371.
    • (2001) J Biol Chem , vol.276 , pp. 2361-2371
    • Wugeditsch, T.1    Paiment, A.2    Hocking, J.3    Drummelsmith, J.4    Forrester, C.5    Whitfield, C.6


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