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Volumn 90, Issue 4, 2013, Pages 776-795

Oligomerization and higher-order assembly contribute to sub-cellular localization of a bacterial scaffold

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN POPZ; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84887403420     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12398     Document Type: Article
Times cited : (45)

References (41)
  • 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.T., 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.T.6
  • 2
    • 51549087758 scopus 로고    scopus 로고
    • A polymeric protein anchors the chromosomal origin/ParB complex at a bacterial cell pole
    • Bowman, G.R., Comolli, L.R., Zhu, J., Eckart, M., Koenig, M., Downing, K.H., etal. (2008) A polymeric protein anchors the chromosomal origin/ParB complex at a bacterial cell pole. Cell 134: 945-955.
    • (2008) Cell , vol.134 , pp. 945-955
    • Bowman, G.R.1    Comolli, L.R.2    Zhu, J.3    Eckart, M.4    Koenig, M.5    Downing, K.H.6
  • 3
    • 77950275435 scopus 로고    scopus 로고
    • Caulobacter PopZ forms a polar subdomain dictating sequential changes in pole composition and function
    • Bowman, G.R., Comolli, L.R., Gaietta, G.M., Fero, M., Hong, S.-H., Jones, Y., etal. (2010) Caulobacter PopZ forms a polar subdomain dictating sequential changes in pole composition and function. Mol Microbiol 76: 173-189.
    • (2010) Mol Microbiol , vol.76 , pp. 173-189
    • Bowman, G.R.1    Comolli, L.R.2    Gaietta, G.M.3    Fero, M.4    Hong, S.-H.5    Jones, Y.6
  • 5
    • 0001104441 scopus 로고
    • Information on polydispersity and branching from combined quasi-elastic and intergrated scattering
    • Burchard, W., Schmidt, M., and Stockmayer, W.H. (1980) Information on polydispersity and branching from combined quasi-elastic and intergrated scattering. Macromolecules 13: 1265-1272.
    • (1980) Macromolecules , vol.13 , pp. 1265-1272
    • Burchard, W.1    Schmidt, M.2    Stockmayer, W.H.3
  • 6
    • 84865311013 scopus 로고    scopus 로고
    • Circular dichroism techniques for the analysis of intrinsically disordered proteins and domains
    • Chemes, L.B., Alonso, L.G., Noval, M.G., and Prat-Gay, G. (2012) Circular dichroism techniques for the analysis of intrinsically disordered proteins and domains. Methods Mol Biol 895: 387-404.
    • (2012) Methods Mol Biol , vol.895 , pp. 387-404
    • Chemes, L.B.1    Alonso, L.G.2    Noval, M.G.3    Prat-Gay, G.4
  • 7
    • 0021759423 scopus 로고
    • Use of high-speed size-exclusion chromatography for the study of protein folding and stability
    • Corbett, R.J., and Roche, R.S. (1984) Use of high-speed size-exclusion chromatography for the study of protein folding and stability. Biochemistry 23: 1888-1894.
    • (1984) Biochemistry , vol.23 , pp. 1888-1894
    • Corbett, R.J.1    Roche, R.S.2
  • 8
    • 84858862680 scopus 로고    scopus 로고
    • A synthetic Escherichia coli system identifies a conserved origin tethering factor in Actinobacteria
    • Donovan, C., Sieger, B., Krämer, R., and Bramkamp, M. (2012) A synthetic Escherichia coli system identifies a conserved origin tethering factor in Actinobacteria. Mol Microbiol 84: 105-116.
    • (2012) Mol Microbiol , vol.84 , pp. 105-116
    • Donovan, C.1    Sieger, B.2    Krämer, R.3    Bramkamp, M.4
  • 9
    • 51549102573 scopus 로고    scopus 로고
    • A self-associating protein critical for chromosome attachment, division, and polar organization in Caulobacter
    • Ebersbach, G., Briegel, A., Jensen, G.J., and Jacobs-Wagner, C. (2008) A self-associating protein critical for chromosome attachment, division, and polar organization in Caulobacter. Cell 134: 956-968.
    • (2008) Cell , vol.134 , pp. 956-968
    • Ebersbach, G.1    Briegel, A.2    Jensen, G.J.3    Jacobs-Wagner, C.4
  • 10
    • 0034212381 scopus 로고    scopus 로고
    • Promiscuous targeting of Bacillus subtilis cell division protein DivIVA to division sites in Escherichia coli and fission yeast
    • Edwards, D.H., Thomaides, H.B., and Errington, J. (2000) Promiscuous targeting of Bacillus subtilis cell division protein DivIVA to division sites in Escherichia coli and fission yeast. EMBO J 19: 2719-2727.
    • (2000) EMBO J , vol.19 , pp. 2719-2727
    • Edwards, D.H.1    Thomaides, H.B.2    Errington, J.3
  • 11
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg, D., and Jucker, M. (2012) The amyloid state of proteins in human diseases. Cell 148: 1188-1203.
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 12
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink, A.L. (2005) Natively unfolded proteins. Curr Opin Struct Biol 15: 35-41.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 13
    • 4444243454 scopus 로고    scopus 로고
    • Determination of molecular masses of proteins in solution: implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory
    • Folta-Stogniew, E., and Williams, K.R. (1999) Determination of molecular masses of proteins in solution: implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory. J Biomol Tech 10: 51-63.
    • (1999) J Biomol Tech , vol.10 , pp. 51-63
    • Folta-Stogniew, E.1    Williams, K.R.2
  • 15
    • 84874966005 scopus 로고    scopus 로고
    • Quantitative multicolor subdiffraction imaging of bacterial protein ultrastructures in three dimensions
    • Gahlmann, A., Ptacin, J.L., Grover, G., Quirin, S., Diezmann, A.R.S., Lee, M.K., etal. (2013) Quantitative multicolor subdiffraction imaging of bacterial protein ultrastructures in three dimensions. Nano Lett 13: 987-993.
    • (2013) Nano Lett , vol.13 , pp. 987-993
    • Gahlmann, A.1    Ptacin, J.L.2    Grover, G.3    Quirin, S.4    Diezmann, A.R.S.5    Lee, M.K.6
  • 16
    • 41449110043 scopus 로고    scopus 로고
    • One-dimensional electrophoresis using nondenaturing conditions
    • Chapter 10, Unit 102B
    • Gallagher, S.R. (2001) One-dimensional electrophoresis using nondenaturing conditions. Curr Protoc Mol Biol Chapter 10: Unit 10.2B.
    • (2001) Curr Protoc Mol Biol
    • Gallagher, S.R.1
  • 17
    • 36849124197 scopus 로고
    • Sedimentation constants of broken chains and wormlike coils
    • Hearst, J., and Stockmayer, W. (1962) Sedimentation constants of broken chains and wormlike coils. J Chem Phys 37: 1425-1433.
    • (1962) J Chem Phys , vol.37 , pp. 1425-1433
    • Hearst, J.1    Stockmayer, W.2
  • 18
    • 84871309389 scopus 로고    scopus 로고
    • Architecturally the same, but playing a different game: the diverse species-specific roles of DivIVA proteins
    • Kaval, K.G., and Halbedel, S. (2012) Architecturally the same, but playing a different game: the diverse species-specific roles of DivIVA proteins. Virulence 3: 406-407.
    • (2012) Virulence , vol.3 , pp. 406-407
    • Kaval, K.G.1    Halbedel, S.2
  • 19
    • 84860777141 scopus 로고    scopus 로고
    • Localized dimerization and nucleoid binding drive gradient formation by the bacterial cell division inhibitor MipZ
    • Kiekebusch, D., Michie, K.A., Essen, L.-O., Löwe, J., and Thanbichler, M. (2012) Localized dimerization and nucleoid binding drive gradient formation by the bacterial cell division inhibitor MipZ. Mol Cell 46: 245-259.
    • (2012) Mol Cell , vol.46 , pp. 245-259
    • Kiekebusch, D.1    Michie, K.A.2    Essen, L.-O.3    Löwe, J.4    Thanbichler, M.5
  • 21
    • 36849103950 scopus 로고
    • Analysis of macromolecular polydispersity in intensity correlation spectroscopy: the method of cumulants
    • Koppel, D.E. (1972) Analysis of macromolecular polydispersity in intensity correlation spectroscopy: the method of cumulants. J Chem Phys 57: 4814-4820.
    • (1972) J Chem Phys , vol.57 , pp. 4814-4820
    • Koppel, D.E.1
  • 22
    • 84867347678 scopus 로고    scopus 로고
    • Asymmetric segregation of the double-stranded RNA binding protein Staufen2 during mammalian neural stem cell divisions promotes lineage progression
    • Kusek, G., Campbell, M., Doyle, F., Tenenbaum, S.A., Kiebler, M., and Temple, S. (2012) Asymmetric segregation of the double-stranded RNA binding protein Staufen2 during mammalian neural stem cell divisions promotes lineage progression. Cell Stem Cell 11: 505-516.
    • (2012) Cell Stem Cell , vol.11 , pp. 505-516
    • Kusek, G.1    Campbell, M.2    Doyle, F.3    Tenenbaum, S.A.4    Kiebler, M.5    Temple, S.6
  • 23
    • 84880018556 scopus 로고    scopus 로고
    • Spatiotemporal control of PopZ localization through cell cycle-coupled multimerization
    • Laloux, G., and Jacobs-Wagner, C. (2013) Spatiotemporal control of PopZ localization through cell cycle-coupled multimerization. J Cell Biol 201: 827-841.
    • (2013) J Cell Biol , vol.201 , pp. 827-841
    • Laloux, G.1    Jacobs-Wagner, C.2
  • 24
    • 68249141791 scopus 로고    scopus 로고
    • Localisation of DivIVA by targeting to negatively curved membranes
    • Lenarcic, R., Halbedel, S., Visser, L., Shaw, M., Wu, L.J., Errington, J., etal. (2009) Localisation of DivIVA by targeting to negatively curved membranes. EMBO J 28: 2272-2282.
    • (2009) EMBO J , vol.28 , pp. 2272-2282
    • Lenarcic, R.1    Halbedel, S.2    Visser, L.3    Shaw, M.4    Wu, L.J.5    Errington, J.6
  • 25
    • 77953613092 scopus 로고    scopus 로고
    • Features critical for membrane binding revealed by DivIVA crystal structure
    • Oliva, M.A., Halbedel, S., Freund, S.M., Dutow, P., Leonard, T.A., Veprintsev, D.B., etal. (2010) Features critical for membrane binding revealed by DivIVA crystal structure. EMBO J 29: 1988-2001.
    • (2010) EMBO J , vol.29 , pp. 1988-2001
    • Oliva, M.A.1    Halbedel, S.2    Freund, S.M.3    Dutow, P.4    Leonard, T.A.5    Veprintsev, D.B.6
  • 27
    • 38349059057 scopus 로고    scopus 로고
    • The dynamic interplay between a cell fate determinant and a lysozyme homolog drives the asymmetric division cycle of Caulobacter crescentus
    • Radhakrishnan, S.K., Thanbichler, M., and Viollier, P.H. (2008) The dynamic interplay between a cell fate determinant and a lysozyme homolog drives the asymmetric division cycle of Caulobacter crescentus. Genes Dev 22: 212-225.
    • (2008) Genes Dev , vol.22 , pp. 212-225
    • Radhakrishnan, S.K.1    Thanbichler, M.2    Viollier, P.H.3
  • 28
    • 69449106111 scopus 로고    scopus 로고
    • Negative membrane curvature as a cue for subcellular localization of a bacterial protein
    • Ramamurthi, K.S., and Losick, R. (2009) Negative membrane curvature as a cue for subcellular localization of a bacterial protein. Proc Natl Acad Sci USA 106: 13541-13545.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13541-13545
    • Ramamurthi, K.S.1    Losick, R.2
  • 29
    • 69549118308 scopus 로고    scopus 로고
    • E. coli transports aggregated proteins to the poles by a specific and energy-dependent process
    • Rokney, A., Shagan, M., Kessel, M., Smith, Y., Rosenshine, I., and Oppenheim, A.B. (2009) E. coli transports aggregated proteins to the poles by a specific and energy-dependent process. J Mol Biol 392: 589-601.
    • (2009) J Mol Biol , vol.392 , pp. 589-601
    • Rokney, A.1    Shagan, M.2    Kessel, M.3    Smith, Y.4    Rosenshine, I.5    Oppenheim, A.B.6
  • 30
    • 78649671515 scopus 로고    scopus 로고
    • Chromosome driven spatial patterning of proteins in bacteria
    • Saberi, S., and Emberly, E. (2010) Chromosome driven spatial patterning of proteins in bacteria. PLoS Comput Biol 6: e1000986.
    • (2010) PLoS Comput Biol , vol.6
    • Saberi, S.1    Emberly, E.2
  • 31
    • 77956801105 scopus 로고    scopus 로고
    • Cell cycle coordination and regulation of bacterial chromosome segregation dynamics by polarly localized proteins
    • Schofield, W.B., Lim, H.C., and Jacobs-Wagner, C. (2010) Cell cycle coordination and regulation of bacterial chromosome segregation dynamics by polarly localized proteins. EMBO J 29: 3068-3081.
    • (2010) EMBO J , vol.29 , pp. 3068-3081
    • Schofield, W.B.1    Lim, H.C.2    Jacobs-Wagner, C.3
  • 32
    • 84863788092 scopus 로고    scopus 로고
    • Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding
    • Shi, Y., Mowery, R.A., Ashley, J., Hentz, M., Ramirez, A.J., Bilgicer, B., etal. (2012) Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding. Protein Sci 21: 1197-1209.
    • (2012) Protein Sci , vol.21 , pp. 1197-1209
    • Shi, Y.1    Mowery, R.A.2    Ashley, J.3    Hentz, M.4    Ramirez, A.J.5    Bilgicer, B.6
  • 33
    • 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
  • 34
    • 2942630094 scopus 로고    scopus 로고
    • Oligomeric structure of the Bacillus subtilis cell division protein DivIVA determined by transmission electron microscopy
    • Stahlberg, H., Kutejová, E., Muchová, K., Gregorini, M., Lustig, A., Müller, S.A., etal. (2004) Oligomeric structure of the Bacillus subtilis cell division protein DivIVA determined by transmission electron microscopy. Mol Microbiol 52: 1281-1290.
    • (2004) Mol Microbiol , vol.52 , pp. 1281-1290
    • Stahlberg, H.1    Kutejová, E.2    Muchová, K.3    Gregorini, M.4    Lustig, A.5    Müller, S.A.6
  • 35
    • 71549140634 scopus 로고    scopus 로고
    • Spatial regulation in Caulobacter crescentus
    • Thanbichler, M. (2009) Spatial regulation in Caulobacter crescentus. Curr Opin Microbiol 12: 715-721.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 715-721
    • Thanbichler, M.1
  • 36
    • 33745699284 scopus 로고    scopus 로고
    • MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter
    • Thanbichler, M., and Shapiro, L. (2006) MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter. Cell 126: 147-162.
    • (2006) Cell , vol.126 , pp. 147-162
    • Thanbichler, M.1    Shapiro, L.2
  • 37
    • 36749049715 scopus 로고    scopus 로고
    • A comprehensive set of plasmids for vanillate- and xylose-inducible gene expression in Caulobacter crescentus
    • Thanbichler, M., Iniesta, A.A., and Shapiro, L. (2007) A comprehensive set of plasmids for vanillate- and xylose-inducible gene expression in Caulobacter crescentus. Nucleic Acids Res 35: e137.
    • (2007) Nucleic Acids Res , vol.35
    • Thanbichler, M.1    Iniesta, A.A.2    Shapiro, L.3
  • 38
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins, D.K., Grimshaw, S.B., Receveur, V., Dobson, C.M., Jones, J.A., and Smith, L.J. (1999) Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 38: 16424-16431.
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 39
    • 77649293067 scopus 로고    scopus 로고
    • Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing
    • Winkler, J., Seybert, A., König, L., Pruggnaller, S., Haselmann, U., Sourjik, V., etal. (2010) Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing. EMBO J 29: 910-923.
    • (2010) EMBO J , vol.29 , pp. 910-923
    • Winkler, J.1    Seybert, A.2    König, L.3    Pruggnaller, S.4    Haselmann, U.5    Sourjik, V.6
  • 40
    • 0027498262 scopus 로고
    • Light Scattering and the absolute characterization of macromolecules
    • Wyatt, P. (1993) Light Scattering and the absolute characterization of macromolecules. Chimica acta 272: 1-40.
    • (1993) Chimica acta , vol.272 , pp. 1-40
    • Wyatt, P.1
  • 41
    • 38749152406 scopus 로고    scopus 로고
    • Asymmetric centrosome behavior and the mechanisms of stem cell division
    • Yamashita, Y.M., and Fuller, M.T. (2008) Asymmetric centrosome behavior and the mechanisms of stem cell division. J Cell Biol 180: 261-266.
    • (2008) J Cell Biol , vol.180 , pp. 261-266
    • Yamashita, Y.M.1    Fuller, M.T.2


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