메뉴 건너뛰기




Volumn 112, Issue 37, 2015, Pages 11666-11671

PopZ identifies the new pole, and PodJ identifies the old pole during polar growth in Agrobacterium tumefaciens

Author keywords

Agrobacterium cell cycle; Bacterial cell division; PodJ; Polar growth; PopZ

Indexed keywords

BACTERIAL PROTEIN; CELL MEMBRANE PROTEIN; FTSA PROTEIN; FTSZ PROTEIN; POLAR ORGANELLE DEVELOPMENT PROTEIN; POLE ORGANIZING PROTEIN; UNCLASSIFIED DRUG; CYTOSKELETON PROTEIN; GREEN FLUORESCENT PROTEIN; PEPTIDOGLYCAN; PEPTIDYLTRANSFERASE;

EID: 84941712465     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1515544112     Document Type: Article
Times cited : (42)

References (42)
  • 1
    • 0033907671 scopus 로고    scopus 로고
    • The transfer of DNA from agro-bacterium tumefaciens into plants: A feast of fundamental insights
    • Zupan J, Muth TR, Draper O, Zambryski P (2000) The transfer of DNA from agro-bacterium tumefaciens into plants: A feast of fundamental insights. Plant J 23(1): 11-28.
    • (2000) Plant J , vol.23 , Issue.1 , pp. 11-28
    • Zupan, J.1    Muth, T.R.2    Draper, O.3    Zambryski, P.4
  • 4
    • 81955161171 scopus 로고    scopus 로고
    • Polarity and the diversity of growth mechanisms in bacteria
    • Brown PJB, Kysela DT, Brun YV (2011) Polarity and the diversity of growth mechanisms in bacteria. Semin Cell Dev Biol 22(8):790-798.
    • (2011) Semin Cell Dev Biol , vol.22 , Issue.8 , pp. 790-798
    • Brown, P.J.B.1    Kysela, D.T.2    Brun, Y.V.3
  • 5
    • 84863116870 scopus 로고    scopus 로고
    • Polar growth in the Alphaproteobacterial order Rhizobiales
    • Brown PJB, et al. (2012) Polar growth in the Alphaproteobacterial order Rhizobiales. Proc Natl Acad Sci USA 109(5):1697-1701.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.5 , pp. 1697-1701
    • Brown, P.J.B.1
  • 6
    • 34047274095 scopus 로고    scopus 로고
    • Unusual features of the cell cycle in mycobacteria: Polar-restricted growth and the snapping-model of cell division
    • Thanky NR, Young DB, Robertson BD (2007) Unusual features of the cell cycle in mycobacteria: Polar-restricted growth and the snapping-model of cell division. Tuberculosis (Edinb) 87(3):231-236.
    • (2007) Tuberculosis (Edinb) , vol.87 , Issue.3 , pp. 231-236
    • Thanky, N.R.1    Young, D.B.2    Robertson, B.D.3
  • 7
    • 84905650444 scopus 로고    scopus 로고
    • Subpolar addition of new cell wall is directed by DivIVA in mycobacteria
    • Meniche X, et al. (2014) Subpolar addition of new cell wall is directed by DivIVA in mycobacteria. Proc Natl Acad Sci USA 111(31):E3243-E3251.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.31 , pp. E3243-E3251
    • Meniche, X.1
  • 8
    • 0020033783 scopus 로고
    • Mode of cell wall growth of Strepto-myces antibioticus
    • Braña AF, Manzanal M-B, Hardisson C (1982) Mode of cell wall growth of Strepto-myces antibioticus. FEMS Microbiol Lett 13(3):231-235.
    • (1982) FEMS Microbiol Lett , vol.13 , Issue.3 , pp. 231-235
    • Braña, A.F.1    Manzanal, M.-B.2    Hardisson, C.3
  • 10
    • 84878467761 scopus 로고    scopus 로고
    • Dynamic FtsA and FtsZ localization and outer membrane alterations during polar growth and cell division in Agrobacterium tumefaciens
    • Zupan JR, Cameron TA, Anderson-Furgeson J, Zambryski PC (2013) Dynamic FtsA and FtsZ localization and outer membrane alterations during polar growth and cell division in Agrobacterium tumefaciens. Proc Natl Acad Sci USA 110(22):9060-9065.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.22 , pp. 9060-9065
    • Zupan, J.R.1    Cameron, T.A.2    Anderson-Furgeson, J.3    Zambryski, P.C.4
  • 11
    • 84903954219 scopus 로고    scopus 로고
    • Peptido-glycan synthesis machinery in Agrobacterium tumefaciens during unipolar growth and cell division
    • Cameron TA, Anderson-Furgeson J, Zupan JR, Zik JJ, Zambryski PC (2014) Peptido-glycan synthesis machinery in Agrobacterium tumefaciens during unipolar growth and cell division. MBio 5(3):e01219-14.
    • (2014) MBio , vol.5 , Issue.3 , pp. e01219-e01314
    • Cameron, T.A.1    Anderson-Furgeson, J.2    Zupan, J.R.3    Zik, J.J.4    Zambryski, P.C.5
  • 12
    • 80052431295 scopus 로고    scopus 로고
    • The bacterial actin MreB rotates, and rotation depends on cell-wall assembly
    • van Teeffelen S, et al. (2011) The bacterial actin MreB rotates, and rotation depends on cell-wall assembly. Proc Natl Acad Sci USA 108(38):15822-15827.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.38 , pp. 15822-15827
    • Van Teeffelen, S.1
  • 13
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B subtilis
    • Garner EC, et al. (2011) Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis. Science 333(6039):222-225.
    • (2011) Science , vol.333 , Issue.6039 , pp. 222-225
    • Garner, E.C.1
  • 14
    • 79960083390 scopus 로고    scopus 로고
    • Processive movement of MreB-associated cell wall biosynthetic complexes in bacteria
    • Domínguez-Escobar J, et al. (2011) Processive movement of MreB-associated cell wall biosynthetic complexes in bacteria. Science 333(6039):225-228.
    • (2011) Science , vol.333 , Issue.6039 , pp. 225-228
    • Domínguez-Escobar, J.1
  • 15
    • 84891509603 scopus 로고    scopus 로고
    • How do bacteria localize proteins to the cell pole?
    • Laloux G, Jacobs-Wagner C (2014) How do bacteria localize proteins to the cell pole? J Cell Sci 127(1):11-19.
    • (2014) J Cell Sci , vol.127 , Issue.1 , pp. 11-19
    • Laloux, G.1    Jacobs-Wagner, C.2
  • 16
    • 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 AJ, Larson DE, Smith CS, Brun YV (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(4):929-941.
    • (2003) Mol Microbiol , vol.47 , Issue.4 , pp. 929-941
    • Hinz, A.J.1    Larson, D.E.2    Smith, C.S.3    Brun, Y.V.4
  • 17
    • 0037108973 scopus 로고    scopus 로고
    • Identification of a localization factor for the polar positioning of bacterial structural and regulatory proteins
    • Viollier PH, Sternheim N, Shapiro L (2002) Identification of a localization factor for the polar positioning of bacterial structural and regulatory proteins. Proc Natl Acad Sci USA 99(21):13831-13836.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.21 , pp. 13831-13836
    • Viollier, P.H.1    Sternheim, N.2    Shapiro, L.3
  • 18
    • 31444436935 scopus 로고    scopus 로고
    • Cytokinesis signals truncation of the PodJ polarity factor by a cell cycle-regulated protease
    • Chen JC, et al. (2006) Cytokinesis signals truncation of the PodJ polarity factor by a cell cycle-regulated protease. EMBO J 25(2):377-386.
    • (2006) EMBO J , vol.25 , Issue.2 , pp. 377-386
    • Chen, J.C.1
  • 19
    • 51549087758 scopus 로고    scopus 로고
    • A polymeric protein anchors the chromosomal origin/ParB complex at a bacterial cell pole
    • Bowman GR, et al. (2008) A polymeric protein anchors the chromosomal origin/ParB complex at a bacterial cell pole. Cell 134(6):945-955.
    • (2008) Cell , vol.134 , Issue.6 , pp. 945-955
    • Bowman, G.R.1
  • 20
    • 51549102573 scopus 로고    scopus 로고
    • A self-associating protein critical for chromosome attachment, division, and polar organization in caulobacter
    • Ebersbach G, Briegel A, Jensen GJ, Jacobs-Wagner C (2008) A self-associating protein critical for chromosome attachment, division, and polar organization in caulobacter. Cell 134(6):956-968.
    • (2008) Cell , vol.134 , Issue.6 , pp. 956-968
    • Ebersbach, G.1    Briegel, A.2    Jensen, G.J.3    Jacobs-Wagner, C.4
  • 21
    • 84900510259 scopus 로고    scopus 로고
    • Bacterial scaffold directs pole-specific centromere segregation
    • Ptacin JL, et al. (2014) Bacterial scaffold directs pole-specific centromere segregation. Proc Natl Acad Sci USA 111(19):E2046-E2055.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.19 , pp. E2046-E2055
    • Ptacin, J.L.1
  • 22
    • 84880018556 scopus 로고    scopus 로고
    • Spatiotemporal control of PopZ localization through cell cycle-coupled multimerization
    • Laloux G, Jacobs-Wagner C (2013) Spatiotemporal control of PopZ localization through cell cycle-coupled multimerization. J Cell Biol 201(6):827-841.
    • (2013) J Cell Biol , vol.201 , Issue.6 , pp. 827-841
    • Laloux, G.1    Jacobs-Wagner, C.2
  • 23
    • 85027947841 scopus 로고    scopus 로고
    • The conserved polarity factor podJ1 impacts multiple cell envelope-associated functions in Sinorhizobium meliloti
    • Fields AT, et al. (2012) The conserved polarity factor podJ1 impacts multiple cell envelope-associated functions in Sinorhizobium meliloti. Mol Microbiol 84(5):892-920.
    • (2012) Mol Microbiol , vol.84 , Issue.5 , pp. 892-920
    • Fields, A.T.1
  • 24
    • 0030681278 scopus 로고    scopus 로고
    • Interactions between heterologous FtsA and FtsZ proteins at the FtsZ ring
    • Ma X, et al. (1997) Interactions between heterologous FtsA and FtsZ proteins at the FtsZ ring. J Bacteriol 179(21):6788-6797.
    • (1997) J Bacteriol , vol.179 , Issue.21 , pp. 6788-6797
    • Ma, X.1
  • 25
    • 77958525927 scopus 로고    scopus 로고
    • In vivo structure of the E coli FtsZ-ring revealed by photoactivated localization microscopy (PALM)
    • Fu G, et al. (2010) In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM). PLoS One 5(9):e12682.
    • (2010) PLoS One , vol.5 , Issue.9 , pp. e12682
    • Fu, G.1
  • 26
    • 0027475809 scopus 로고
    • A histidine protein kinase is involved in polar organelle development in Caulobacter crescentus
    • Wang SP, Sharma PL, Schoenlein PV, Ely B (1993) A histidine protein kinase is involved in polar organelle development in Caulobacter crescentus. Proc Natl Acad Sci USA 90(2):630-634.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.2 , pp. 630-634
    • Wang, S.P.1    Sharma, P.L.2    Schoenlein, P.V.3    Ely, B.4
  • 27
    • 0037317866 scopus 로고    scopus 로고
    • Identification of genes required for synthesis of the adhesive holdfast in Caulobacter crescentus
    • Smith CS, Hinz A, Bodenmiller D, Larson DE, Brun YV (2003) Identification of genes required for synthesis of the adhesive holdfast in Caulobacter crescentus. J Bacteriol 185(4):1432-1442.
    • (2003) J Bacteriol , vol.185 , Issue.4 , pp. 1432-1442
    • Smith, C.S.1    Hinz, A.2    Bodenmiller, D.3    Larson, D.E.4    Brun, Y.V.5
  • 28
    • 31444440985 scopus 로고    scopus 로고
    • Dissection of functional domains of the polar localization factor PodJ in Caulobacter crescentus
    • Lawler ML, Larson DE, Hinz AJ, Klein D, Brun YV (2006) Dissection of functional domains of the polar localization factor PodJ in Caulobacter crescentus. Mol Microbiol 59(1):301-316.
    • (2006) Mol Microbiol , vol.59 , Issue.1 , pp. 301-316
    • Lawler, M.L.1    Larson, D.E.2    Hinz, A.J.3    Klein, D.4    Brun, Y.V.5
  • 29
    • 84860600234 scopus 로고    scopus 로고
    • The scaffolding and signalling functions of a localization factor impact polar development
    • Curtis PD, et al. (2012) The scaffolding and signalling functions of a localization factor impact polar development. Mol Microbiol 84(4):712-735.
    • (2012) Mol Microbiol , vol.84 , Issue.4 , pp. 712-735
    • Curtis, P.D.1
  • 30
    • 46049085808 scopus 로고    scopus 로고
    • Identification of the L, D-transpeptidases for peptidoglycan cross-linking in Escherichia coli
    • Magnet S, Dubost L, Marie A, Arthur M, Gutmann L (2008) Identification of the L, D-transpeptidases for peptidoglycan cross-linking in Escherichia coli. J Bacteriol 190(13):4782-4785.
    • (2008) J Bacteriol , vol.190 , Issue.13 , pp. 4782-4785
    • Magnet, S.1    Dubost, L.2    Marie, A.3    Arthur, M.4    Gutmann, L.5
  • 31
    • 0023677844 scopus 로고
    • The composition of the murein of Escherichia coli
    • Glauner B, Höltje JV, Schwarz U (1988) The composition of the murein of Escherichia coli. J Biol Chem 263(21):10088-10095.
    • (1988) J Biol Chem , vol.263 , Issue.21 , pp. 10088-10095
    • Glauner, B.1    Höltje, J.V.2    Schwarz, U.3
  • 32
    • 0038191051 scopus 로고    scopus 로고
    • Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycle
    • Rueda S, Vicente M, Mingorance J (2003) Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycle. J Bacteriol 185(11):3344-3351.
    • (2003) J Bacteriol , vol.185 , Issue.11 , pp. 3344-3351
    • Rueda, S.1    Vicente, M.2    Mingorance, J.3
  • 33
    • 15944362608 scopus 로고    scopus 로고
    • Maturation of the Escherichia coli divisome occurs in two steps
    • Aarsman MEG, et al. (2005) Maturation of the Escherichia coli divisome occurs in two steps. Mol Microbiol 55(6):1631-1645.
    • (2005) Mol Microbiol , vol.55 , Issue.6 , pp. 1631-1645
    • Aarsman, M.E.G.1
  • 34
    • 24944469539 scopus 로고    scopus 로고
    • Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly
    • Jensen SO, Thompson LS, Harry EJ (2005) Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly. J Bacteriol 187(18):6536-6544.
    • (2005) J Bacteriol , vol.187 , Issue.18 , pp. 6536-6544
    • Jensen, S.O.1    Thompson, L.S.2    Harry, E.J.3
  • 35
    • 79958782165 scopus 로고    scopus 로고
    • Assembly of the Caulobacter cell division machine
    • Goley ED, et al. (2011) Assembly of the Caulobacter cell division machine. Mol Microbiol 80(6):1680-1698.
    • (2011) Mol Microbiol , vol.80 , Issue.6 , pp. 1680-1698
    • Goley, E.D.1
  • 36
    • 84904615375 scopus 로고    scopus 로고
    • Regulation of cell polarity in bacteria
    • Treuner-Lange A, Søgaard-Andersen L (2014) Regulation of cell polarity in bacteria. J Cell Biol 206(1):7-17.
    • (2014) J Cell Biol , vol.206 , Issue.1 , pp. 7-17
    • Treuner-Lange, A.1    Søgaard-Andersen, L.2
  • 37
    • 84930925768 scopus 로고    scopus 로고
    • The essential features and modes of bacterial polar growth
    • Cameron TA, Zupan JR, Zambryski PC (2015) The essential features and modes of bacterial polar growth. Trends Microbiol 23(6):347-353.
    • (2015) Trends Microbiol , vol.23 , Issue.6 , pp. 347-353
    • Cameron, T.A.1    Zupan, J.R.2    Zambryski, P.C.3
  • 38
    • 0037515724 scopus 로고    scopus 로고
    • Polar localization of replicon origins in the multipartite genomes of Agrobacterium tumefaciens and Sinorhizobium meliloti
    • Kahng LS, Shapiro L (2003) Polar localization of replicon origins in the multipartite genomes of Agrobacterium tumefaciens and Sinorhizobium meliloti. J Bacteriol 185(11):3384-3391.
    • (2003) J Bacteriol , vol.185 , Issue.11 , pp. 3384-3391
    • Kahng, L.S.1    Shapiro, L.2
  • 39
    • 59649113418 scopus 로고    scopus 로고
    • RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E coli
    • Bendezú FO, Hale CA, Bernhardt TG, de Boer PAJ (2009) RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli. EMBO J 28(3):193-204.
    • (2009) EMBO J , vol.28 , Issue.3 , pp. 193-204
    • Bendezú, F.O.1    Hale, C.A.2    Bernhardt, T.G.3    De Boer, P.A.J.4
  • 40
    • 50049086448 scopus 로고    scopus 로고
    • Broad-host-range expression vectors with tightly regulated promoters and their use to examine the influence of TraR and TraM expression on Ti plasmid quorum sensing
    • Khan SR, Gaines J, Roop RM, 2nd, Farrand SK (2008) Broad-host-range expression vectors with tightly regulated promoters and their use to examine the influence of TraR and TraM expression on Ti plasmid quorum sensing. Appl Environ Microbiol 74(16):5053-5062.
    • (2008) Appl Environ Microbiol , vol.74 , Issue.16 , pp. 5053-5062
    • Khan, S.R.1    Gaines, J.2    Roop, R.M.3    Farrand, S.K.4
  • 41
    • 34548587089 scopus 로고    scopus 로고
    • VirB1∗promotes T-pilus formation in the vir-Type IV secretion system of Agrobacterium tumefaciens
    • Zupan J, Hackworth CA, Aguilar J, Ward D, Zambryski P (2007) VirB1∗ promotes T-pilus formation in the vir-Type IV secretion system of Agrobacterium tumefaciens. J Bacteriol 189(18):6551-6563.
    • (2007) J Bacteriol , vol.189 , Issue.18 , pp. 6551-6563
    • Zupan, J.1    Hackworth, C.A.2    Aguilar, J.3    Ward, D.4    Zambryski, P.5
  • 42
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, Van Dyke M, Stock J (1991) Predicting coiled coils from protein sequences. Science 252(5009):1162-1164.
    • (1991) Science , vol.252 , Issue.5009 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.