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Volumn 124, Issue 5, 2006, Pages 1025-1037

Bacterial birth scar proteins mark future flagellum assembly site

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYCLIC GMP PHOSPHODIESTERASE; PROTEIN TIPF; PROTEIN TIPN; UNCLASSIFIED DRUG;

EID: 33644764886     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2006.01.019     Document Type: Article
Times cited : (174)

References (48)
  • 1
    • 0026628961 scopus 로고
    • Polar localization of a bacterial chemoreceptor
    • M.R. Alley, J.R. Maddock, and L. Shapiro Polar localization of a bacterial chemoreceptor Genes Dev. 6 1992 825 836
    • (1992) Genes Dev. , vol.6 , pp. 825-836
    • Alley, M.R.1    Maddock, J.R.2    Shapiro, L.3
  • 2
    • 0037462540 scopus 로고    scopus 로고
    • RacA, a bacterial protein that anchors chromosomes to the cell poles
    • S. Ben-Yehuda, D.Z. Rudner, and R. Losick RacA, a bacterial protein that anchors chromosomes to the cell poles Science 299 2003 532 536
    • (2003) Science , vol.299 , pp. 532-536
    • Ben-Yehuda, S.1    Rudner, D.Z.2    Losick, R.3
  • 3
    • 20444385050 scopus 로고    scopus 로고
    • The phosphodiesterase activity of the HmsP EAL domain is required for negative regulation of biofilm formation in Yersinia pestis
    • A.G. Bobrov, O. Kirillina, and R.D. Perry The phosphodiesterase activity of the HmsP EAL domain is required for negative regulation of biofilm formation in Yersinia pestis FEMS Microbiol. Lett. 247 2005 123 130
    • (2005) FEMS Microbiol. Lett. , vol.247 , pp. 123-130
    • Bobrov, A.G.1    Kirillina, O.2    Perry, R.D.3
  • 4
    • 0035859884 scopus 로고    scopus 로고
    • Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and Vibrio
    • M. Charles, M. Perez, J.H. Kobil, and M.B. Goldberg Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and Vibrio Proc. Natl. Acad. Sci. USA 98 2001 9871 9876
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9871-9876
    • Charles, M.1    Perez, M.2    Kobil, J.H.3    Goldberg, M.B.4
  • 5
    • 14544270275 scopus 로고    scopus 로고
    • A membrane metalloprotease participates in the sequential degradation of a Caulobacter polarity determinant
    • J.C. Chen, P.H. Viollier, and L. Shapiro A membrane metalloprotease participates in the sequential degradation of a Caulobacter polarity determinant Mol. Microbiol. 55 2005 1085 1103
    • (2005) Mol. Microbiol. , vol.55 , pp. 1085-1103
    • Chen, J.C.1    Viollier, P.H.2    Shapiro, L.3
  • 6
    • 24744457756 scopus 로고    scopus 로고
    • Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP
    • M. Christen, B. Christen, M. Folcher, A. Schauerte, and U. Jenal Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP J. Biol. Chem. 280 2005 30829 30837
    • (2005) J. Biol. Chem. , vol.280 , pp. 30829-30837
    • Christen, M.1    Christen, B.2    Folcher, M.3    Schauerte, A.4    Jenal, U.5
  • 7
    • 0031780597 scopus 로고    scopus 로고
    • Dominant C-terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA
    • N. Din, E.M. Quardokus, M.J. Sackett, and Y.V. Brun Dominant C-terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA Mol. Microbiol. 27 1998 1051 1063
    • (1998) Mol. Microbiol. , vol.27 , pp. 1051-1063
    • Din, N.1    Quardokus, E.M.2    Sackett, M.J.3    Brun, Y.V.4
  • 8
    • 0034212381 scopus 로고    scopus 로고
    • Promiscuous targeting of Bacillus subtilis cell division protein DivIVA to division sites in Escherichia coli and fission yeast
    • D.H. Edwards, H.B. Thomaides, and J. Errington Promiscuous targeting of Bacillus subtilis cell division protein DivIVA to division sites in Escherichia coli and fission yeast EMBO J. 19 2000 2719 2727
    • (2000) EMBO J. , vol.19 , pp. 2719-2727
    • Edwards, D.H.1    Thomaides, H.B.2    Errington, J.3
  • 9
    • 0025888266 scopus 로고
    • Genetics of Caulobacter crescentus
    • B. Ely Genetics of Caulobacter crescentus Methods Enzymol. 204 1991 372 384
    • (1991) Methods Enzymol. , vol.204 , pp. 372-384
    • Ely, B.1
  • 10
    • 1842613501 scopus 로고    scopus 로고
    • Regulation of endospore formation in Bacillus subtilis
    • J. Errington Regulation of endospore formation in Bacillus subtilis Nat. Rev. Microbiol. 1 2003 117 126
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 117-126
    • Errington, J.1
  • 12
    • 0037341855 scopus 로고    scopus 로고
    • Productive interaction between the chromosome partitioning proteins, para and ParB, is required for the progression of the cell cycle in Caulobacter crescentus
    • R.M. Figge, J. Easter, and J.W. Gober Productive interaction between the chromosome partitioning proteins, ParA and ParB, is required for the progression of the cell cycle in Caulobacter crescentus Mol. Microbiol. 47 2003 1225 1237
    • (2003) Mol. Microbiol. , vol.47 , pp. 1225-1237
    • Figge, R.M.1    Easter, J.2    Gober, J.W.3
  • 13
    • 0028274712 scopus 로고
    • Isolation, characterization and structure of bacterial flagellar motors containing the switch complex
    • N.R. Francis, G.E. Sosinsky, D. Thomas, and D.J. DeRosier Isolation, characterization and structure of bacterial flagellar motors containing the switch complex J. Mol. Biol. 235 1994 1261 1270
    • (1994) J. Mol. Biol. , vol.235 , pp. 1261-1270
    • Francis, N.R.1    Sosinsky, G.E.2    Thomas, D.3    Derosier, D.J.4
  • 14
    • 0002225857 scopus 로고    scopus 로고
    • Regulation of flagellum biosynthesis and motility in Caulobacter
    • Y.V. Brun L.J. Shimkets American Society for Microbiology Washington DC
    • J.W. Gober, and J.C. England Regulation of flagellum biosynthesis and motility in Caulobacter Y.V. Brun L.J. Shimkets Prokaryotic Development 2000 American Society for Microbiology Washington DC 319 339
    • (2000) Prokaryotic Development , pp. 319-339
    • Gober, J.W.1    England, J.C.2
  • 15
    • 0037228462 scopus 로고    scopus 로고
    • Polar targeting of DivIVA in Bacillus subtilis is not directly dependent on FtsZ or PBP 2B
    • L.W. Hamoen, and J. Errington Polar targeting of DivIVA in Bacillus subtilis is not directly dependent on FtsZ or PBP 2B J. Bacteriol. 185 2003 693 697
    • (2003) J. Bacteriol. , vol.185 , pp. 693-697
    • Hamoen, L.W.1    Errington, J.2
  • 16
    • 2942616403 scopus 로고    scopus 로고
    • Compartmentalization of gene expression during Bacillus subtilis spore formation
    • D.W. Hilbert, and P.J. Piggot Compartmentalization of gene expression during Bacillus subtilis spore formation Microbiol. Mol. Biol. Rev. 68 2004 234 262
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 234-262
    • Hilbert, D.W.1    Piggot, P.J.2
  • 17
    • 0345735666 scopus 로고    scopus 로고
    • A mechanism for polar protein localization in bacteria
    • M. Howard A mechanism for polar protein localization in bacteria J. Mol. Biol. 335 2004 655 663
    • (2004) J. Mol. Biol. , vol.335 , pp. 655-663
    • Howard, M.1
  • 18
    • 0345097587 scopus 로고    scopus 로고
    • FimX, a multidomain protein connecting environmental signals to twitching motility in Pseudomonas aeruginosa
    • B. Huang, C.B. Whitchurch, and J.S. Mattick FimX, a multidomain protein connecting environmental signals to twitching motility in Pseudomonas aeruginosa J. Bacteriol. 185 2003 7068 7076
    • (2003) J. Bacteriol. , vol.185 , pp. 7068-7076
    • Huang, B.1    Whitchurch, C.B.2    Mattick, J.S.3
  • 19
    • 1842610464 scopus 로고    scopus 로고
    • Cyclic di-guanosine-monophosphate comes of age: A novel secondary messenger involved in modulating cell surface structures in bacteria?
    • U. Jenal Cyclic di-guanosine-monophosphate comes of age: a novel secondary messenger involved in modulating cell surface structures in bacteria? Curr. Opin. Microbiol. 7 2004 185 191
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 185-191
    • Jenal, U.1
  • 20
    • 0032521234 scopus 로고    scopus 로고
    • Cell cycle-dependent transcriptional and proteolytic regulation of FtsZ in Caulobacter
    • A.J. Kelly, M.J. Sackett, N. Din, E. Quardokus, and Y.V. Brun Cell cycle-dependent transcriptional and proteolytic regulation of FtsZ in Caulobacter Genes Dev. 12 1998 880 893
    • (1998) Genes Dev. , vol.12 , pp. 880-893
    • Kelly, A.J.1    Sackett, M.J.2    Din, N.3    Quardokus, E.4    Brun, Y.V.5
  • 21
    • 33644753905 scopus 로고    scopus 로고
    • A landmark protein essential for establishing and perpetuating the polarity of a bacterial cell
    • H. Lam, W.B. Schofield, and C. Jacobs-Wagner A landmark protein essential for establishing and perpetuating the polarity of a bacterial cell Cell 124 2006 1011 1023 this issue
    • (2006) Cell , vol.124 , pp. 1011-1023
    • Lam, H.1    Schofield, W.B.2    Jacobs-Wagner, C.3
  • 22
    • 0030884961 scopus 로고    scopus 로고
    • Localization of the sporulation protein SpoIIE in Bacillus subtilis is dependent upon the cell division protein FtsZ
    • P.A. Levin, R. Losick, P. Stragier, and F. Arigoni Localization of the sporulation protein SpoIIE in Bacillus subtilis is dependent upon the cell division protein FtsZ Mol. Microbiol. 25 1997 839 846
    • (1997) Mol. Microbiol. , vol.25 , pp. 839-846
    • Levin, P.A.1    Losick, R.2    Stragier, P.3    Arigoni, F.4
  • 23
    • 0033558144 scopus 로고    scopus 로고
    • Linking asymmetric division to cell fate: Teaching an old microbe new tricks
    • R. Losick, and J. Dworkin Linking asymmetric division to cell fate: teaching an old microbe new tricks Genes Dev. 13 1999 377 381
    • (1999) Genes Dev. , vol.13 , pp. 377-381
    • Losick, R.1    Dworkin, J.2
  • 24
    • 0034599494 scopus 로고    scopus 로고
    • Direct interaction between the cell division protein FtsZ and the cell differentiation protein SpoIIE
    • I. Lucet, A. Feucht, M.D. Yudkin, and J. Errington Direct interaction between the cell division protein FtsZ and the cell differentiation protein SpoIIE EMBO J. 19 2000 1467 1475
    • (2000) EMBO J. , vol.19 , pp. 1467-1475
    • Lucet, I.1    Feucht, A.2    Yudkin, M.D.3    Errington, J.4
  • 25
    • 0023281131 scopus 로고
    • Membrane-murein attachment at the leading edge of the division septum: A second membrane-murein structure associated with morphogenesis of the gram-negative bacterial division septum
    • T.J. MacAlister, W.R. Cook, R. Weigand, and L.I. Rothfield Membrane-murein attachment at the leading edge of the division septum: a second membrane-murein structure associated with morphogenesis of the gram-negative bacterial division septum J. Bacteriol. 169 1987 3945 3951
    • (1987) J. Bacteriol. , vol.169 , pp. 3945-3951
    • MacAlister, T.J.1    Cook, W.R.2    Weigand, R.3    Rothfield, L.I.4
  • 26
    • 0032213104 scopus 로고    scopus 로고
    • Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site
    • A.L. Marston, H.B. Thomaides, D.H. Edwards, M.E. Sharpe, and J. Errington Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site Genes Dev. 12 1998 3419 3430
    • (1998) Genes Dev. , vol.12 , pp. 3419-3430
    • Marston, A.L.1    Thomaides, H.B.2    Edwards, D.H.3    Sharpe, M.E.4    Errington, J.5
  • 27
    • 4444372637 scopus 로고    scopus 로고
    • Cytokinesis monitoring during development; Rapid pole-to-pole shuttling of a signaling protein by localized kinase and phosphatase in Caulobacter
    • J.Y. Matroule, H. Lam, D.T. Burnette, and C. Jacobs-Wagner Cytokinesis monitoring during development; rapid pole-to-pole shuttling of a signaling protein by localized kinase and phosphatase in Caulobacter Cell 118 2004 579 590
    • (2004) Cell , vol.118 , pp. 579-590
    • Matroule, J.Y.1    Lam, H.2    Burnette, D.T.3    Jacobs-Wagner, C.4
  • 28
    • 1842610460 scopus 로고    scopus 로고
    • Setting the pace: Mechanisms tying Caulobacter cell-cycle progression to macroscopic cellular events
    • P.T. McGrath, P. Viollier, and H.H. McAdams Setting the pace: mechanisms tying Caulobacter cell-cycle progression to macroscopic cellular events Curr. Opin. Microbiol. 7 2004 192 197
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 192-197
    • McGrath, P.T.1    Viollier, P.2    McAdams, H.H.3
  • 29
    • 1842451699 scopus 로고    scopus 로고
    • Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain
    • R. Paul, S. Weiser, N.C. Amiot, C. Chan, T. Schirmer, B. Giese, and U. Jenal Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain Genes Dev. 18 2004 715 727
    • (2004) Genes Dev. , vol.18 , pp. 715-727
    • Paul, R.1    Weiser, S.2    Amiot, N.C.3    Chan, C.4    Schirmer, T.5    Giese, B.6    Jenal, U.7
  • 30
    • 9644277150 scopus 로고    scopus 로고
    • Identification of a polar targeting determinant for Bacillus subtilis DivIVA
    • S.E. Perry, and D.H. Edwards Identification of a polar targeting determinant for Bacillus subtilis DivIVA Mol. Microbiol. 54 2004 1237 1249
    • (2004) Mol. Microbiol. , vol.54 , pp. 1237-1249
    • Perry, S.E.1    Edwards, D.H.2
  • 31
    • 0031018531 scopus 로고    scopus 로고
    • Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites
    • J. Pogliano, K. Pogliano, D.S. Weiss, R. Losick, and J. Beckwith Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites Proc. Natl. Acad. Sci. USA 94 1997 559 564
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 559-564
    • Pogliano, J.1    Pogliano, K.2    Weiss, D.S.3    Losick, R.4    Beckwith, J.5
  • 32
    • 24144471500 scopus 로고    scopus 로고
    • Bacterial shape and ActA distribution affect initiation of Listeria monocytogenes Actin-based motility
    • S.M. Rafelski, and J.A. Theriot Bacterial shape and ActA distribution affect initiation of Listeria monocytogenes Actin-based motility Biophys. J. 89 2005 2146 2158
    • (2005) Biophys. J. , vol.89 , pp. 2146-2158
    • Rafelski, S.M.1    Theriot, J.A.2
  • 33
    • 22644438480 scopus 로고    scopus 로고
    • C-di-GMP: The dawning of a novel bacterial signalling system
    • U. Romling, M. Gomelsky, and M.Y. Galperin C-di-GMP: the dawning of a novel bacterial signalling system Mol. Microbiol. 57 2005 629 639
    • (2005) Mol. Microbiol. , vol.57 , pp. 629-639
    • Romling, U.1    Gomelsky, M.2    Galperin, M.Y.3
  • 34
    • 21844451590 scopus 로고    scopus 로고
    • The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: Enzymatically active and inactive EAL domains
    • A.J. Schmidt, D.A. Ryjenkov, and M. Gomelsky The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains J. Bacteriol. 187 2005 4774 4781
    • (2005) J. Bacteriol. , vol.187 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 35
    • 0035923586 scopus 로고    scopus 로고
    • Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway
    • M.E. Scott, Z.Y. Dossani, and M. Sandkvist Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway Proc. Natl. Acad. Sci. USA 98 2001 13978 13983
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13978-13983
    • Scott, M.E.1    Dossani, Z.Y.2    Sandkvist, M.3
  • 36
    • 0037032826 scopus 로고    scopus 로고
    • Generating and exploiting polarity in bacteria
    • L. Shapiro, H.H. McAdams, and R. Losick Generating and exploiting polarity in bacteria Science 298 2002 1942 1946
    • (2002) Science , vol.298 , pp. 1942-1946
    • Shapiro, L.1    McAdams, H.H.2    Losick, R.3
  • 37
    • 0041853574 scopus 로고    scopus 로고
    • Bacterial chromosome dynamics
    • D.J. Sherratt Bacterial chromosome dynamics Science 301 2003 780 785
    • (2003) Science , vol.301 , pp. 780-785
    • Sherratt, D.J.1
  • 38
    • 4344688129 scopus 로고    scopus 로고
    • GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility
    • R. Simm, M. Morr, A. Kader, M. Nimtz, and U. Romling GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility Mol. Microbiol. 53 2004 1123 1134
    • (2004) Mol. Microbiol. , vol.53 , pp. 1123-1134
    • Simm, R.1    Morr, M.2    Kader, A.3    Nimtz, M.4    Romling, U.5
  • 39
    • 0034600835 scopus 로고    scopus 로고
    • Identification and cell cycle control of a novel pilus system in Caulobacter crescentus
    • J.M. Skerker, and L. Shapiro Identification and cell cycle control of a novel pilus system in Caulobacter crescentus EMBO J. 19 2000 3223 3234
    • (2000) EMBO J. , vol.19 , pp. 3223-3234
    • Skerker, J.M.1    Shapiro, L.2
  • 40
    • 2142647271 scopus 로고    scopus 로고
    • Cell-cycle progression and the generation of asymmetry in Caulobacter crescentus
    • J.M. Skerker, and M.T. Laub Cell-cycle progression and the generation of asymmetry in Caulobacter crescentus Nat. Rev. Microbiol. 2 2004 325 337
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 325-337
    • Skerker, J.M.1    Laub, M.T.2
  • 41
    • 25144489145 scopus 로고    scopus 로고
    • The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase
    • R. Tamayo, A.D. Tischler, and A. Camilli The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase J. Biol. Chem. 280 2005 33324 33330
    • (2005) J. Biol. Chem. , vol.280 , pp. 33324-33330
    • Tamayo, R.1    Tischler, A.D.2    Camilli, A.3
  • 43
    • 0037487270 scopus 로고    scopus 로고
    • A lytic transglycosylase homologue, PleA, is required for the assembly of pili and the flagellum at the Caulobacter crescentus cell pole
    • P.H. Viollier, and L. Shapiro A lytic transglycosylase homologue, PleA, is required for the assembly of pili and the flagellum at the Caulobacter crescentus cell pole Mol. Microbiol. 49 2003 331 345
    • (2003) Mol. Microbiol. , vol.49 , pp. 331-345
    • Viollier, P.H.1    Shapiro, L.2
  • 44
    • 0037009444 scopus 로고    scopus 로고
    • A dynamically localized histidine kinase controls the asymmetric distribution of polar pili proteins
    • P.H. Viollier, N. Sternheim, and L. Shapiro A dynamically localized histidine kinase controls the asymmetric distribution of polar pili proteins EMBO J. 21 2002 4420 4428
    • (2002) EMBO J. , vol.21 , pp. 4420-4428
    • Viollier, P.H.1    Sternheim, N.2    Shapiro, L.3
  • 45
    • 0037108973 scopus 로고    scopus 로고
    • Identification of a localization factor for the polar positioning of bacterial structural and regulatory proteins
    • P.H. Viollier, N. Sternheim, and L. Shapiro Identification of a localization factor for the polar positioning of bacterial structural and regulatory proteins Proc. Natl. Acad. Sci. USA 99 2002 13831 13836
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13831-13836
    • Viollier, P.H.1    Sternheim, N.2    Shapiro, L.3
  • 46
    • 0036207168 scopus 로고    scopus 로고
    • Use of the Caulobacter crescentus genome sequence to develop a method for systematic genetic mapping
    • L. West, D. Yang, and C. Stephens Use of the Caulobacter crescentus genome sequence to develop a method for systematic genetic mapping J. Bacteriol. 184 2002 2155 2166
    • (2002) J. Bacteriol. , vol.184 , pp. 2155-2166
    • West, L.1    Yang, D.2    Stephens, C.3
  • 47
    • 0033231550 scopus 로고    scopus 로고
    • Differential localization of two histidine kinases controlling bacterial cell differentiation
    • R.T. Wheeler, and L. Shapiro Differential localization of two histidine kinases controlling bacterial cell differentiation Mol. Cell 4 1999 683 694
    • (1999) Mol. Cell , vol.4 , pp. 683-694
    • Wheeler, R.T.1    Shapiro, L.2
  • 48
    • 0141677790 scopus 로고    scopus 로고
    • RacA and the Soj-Spo0J system combine to effect polar chromosome segregation in sporulating Bacillus subtilis
    • L.J. Wu, and J. Errington RacA and the Soj-Spo0J system combine to effect polar chromosome segregation in sporulating Bacillus subtilis Mol. Microbiol. 49 2003 1463 1475
    • (2003) Mol. Microbiol. , vol.49 , pp. 1463-1475
    • Wu, L.J.1    Errington, J.2


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