메뉴 건너뛰기




Volumn 77, Issue 1, 2010, Pages 90-107

DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PEPTIDOGLYCAN; PROTEIN DIPM; UNCLASSIFIED DRUG; BACTERIAL DNA; CELL CYCLE PROTEIN; MEMBRANE PROTEIN; PERIPLASMIC PROTEIN; PROTEIN BINDING; PROTEINASE;

EID: 77953996215     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07224.x     Document Type: Article
Times cited : (76)

References (89)
  • 1
    • 34248364322 scopus 로고    scopus 로고
    • The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus
    • Aaron, M., Charbon, G., Lam, H., Schwarz, H., Vollmer, W. Jacobs-Wagner, C. (2007) The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus. Mol Microbiol 64 : 938 952.
    • (2007) Mol Microbiol , vol.64 , pp. 938-952
    • Aaron, M.1    Charbon, G.2    Lam, H.3    Schwarz, H.4    Vollmer, W.5    Jacobs-Wagner, C.6
  • 3
    • 0030856502 scopus 로고    scopus 로고
    • FtsN, a late recruit to the septum in Escherichia coli
    • Addinall, S.G., Cao, C. Lutkenhaus, J. (1997) FtsN, a late recruit to the septum in Escherichia coli. Mol Microbiol 25 : 303 309.
    • (1997) Mol Microbiol , vol.25 , pp. 303-309
    • Addinall, S.G.1    Cao, C.2    Lutkenhaus, J.3
  • 4
    • 73849120353 scopus 로고    scopus 로고
    • Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA
    • Arends, S.J., Williams, K., Scott, R.J., Rolong, S., Popham, D.L. Weiss, D.S. (2009) Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA. J Bacteriol 192 : 242 255.
    • (2009) J Bacteriol , vol.192 , pp. 242-255
    • Arends, S.J.1    Williams, K.2    Scott, R.J.3    Rolong, S.4    Popham, D.L.5    Weiss, D.S.6
  • 5
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)
    • Bateman, A. Bycroft, M. (2000) The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J Mol Biol 299 : 1113 1119.
    • (2000) J Mol Biol , vol.299 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 6
    • 0037783310 scopus 로고    scopus 로고
    • The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway
    • Bernhardt, T.G. de Boer, P.A. (2003) The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway. Mol Microbiol 48 : 1171 1182.
    • (2003) Mol Microbiol , vol.48 , pp. 1171-1182
    • Bernhardt, T.G.1    De Boer, P.A.2
  • 7
    • 2942538589 scopus 로고    scopus 로고
    • Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity
    • Bernhardt, T.G. de Boer, P.A. (2004) Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity. Mol Microbiol 52 : 1255 1269.
    • (2004) Mol Microbiol , vol.52 , pp. 1255-1269
    • Bernhardt, T.G.1    De Boer, P.A.2
  • 9
    • 0016671464 scopus 로고
    • Role of antirepressor in the bipartite control of repression and immunity by bacteriophage P22
    • Botstein, K., Lew, K.K., Jarvik, V. Swanson, C.A. (1975) Role of antirepressor in the bipartite control of repression and immunity by bacteriophage P22. J Mol Biol 91 : 439 462.
    • (1975) J Mol Biol , vol.91 , pp. 439-462
    • Botstein, K.1    Lew, K.K.2    Jarvik, V.3    Swanson, C.A.4
  • 10
    • 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., et al. (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
  • 11
    • 45149093047 scopus 로고    scopus 로고
    • Location and architecture of the Caulobacter crescentus chemoreceptor array
    • Briegel, A., Ding, H.J., Li, Z., Werner, J., Gitai, Z., Dias, D.P., et al. (2008) Location and architecture of the Caulobacter crescentus chemoreceptor array. Mol Microbiol 69 : 30 41.
    • (2008) Mol Microbiol , vol.69 , pp. 30-41
    • Briegel, A.1    Ding, H.J.2    Li, Z.3    Werner, J.4    Gitai, Z.5    Dias, D.P.6
  • 12
    • 52949102235 scopus 로고    scopus 로고
    • Complex regulatory pathways coordinate cell-cycle progression and development in Caulobacter crescentus
    • Brown, P.J., Hardy, G.G., Trimble, M.J. 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.1    Hardy, G.G.2    Trimble, M.J.3    Brun, Y.V.4
  • 13
    • 2942570076 scopus 로고    scopus 로고
    • A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region
    • Buddelmeijer, N. Beckwith, J. (2004) A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region. Mol Microbiol 52 : 1315 1327.
    • (2004) Mol Microbiol , vol.52 , pp. 1315-1327
    • Buddelmeijer, N.1    Beckwith, J.2
  • 14
    • 42549103340 scopus 로고    scopus 로고
    • LysM, a widely distributed protein motif for binding to (peptido)glycans
    • Buist, G., Steen, A., Kok, J. Kuipers, O.P. (2008) LysM, a widely distributed protein motif for binding to (peptido)glycans. Mol Microbiol 68 : 838 847.
    • (2008) Mol Microbiol , vol.68 , pp. 838-847
    • Buist, G.1    Steen, A.2    Kok, J.3    Kuipers, O.P.4
  • 16
    • 53849143253 scopus 로고    scopus 로고
    • Localization of PBP3 in Caulobacter crescentus is highly dynamic and largely relies on its functional transpeptidase domain
    • Costa, T., Priyadarshini, R. Jacobs-Wagner, C. (2008) Localization of PBP3 in Caulobacter crescentus is highly dynamic and largely relies on its functional transpeptidase domain. Mol Microbiol 70 : 634 651.
    • (2008) Mol Microbiol , vol.70 , pp. 634-651
    • Costa, T.1    Priyadarshini, R.2    Jacobs-Wagner, C.3
  • 17
    • 0026697767 scopus 로고
    • The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli
    • Dai, K. Lutkenhaus, J. (1992) The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli. J Bacteriol 174 : 6145 6151.
    • (1992) J Bacteriol , vol.174 , pp. 6145-6151
    • Dai, K.1    Lutkenhaus, J.2
  • 18
    • 0027167446 scopus 로고
    • Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsA12(Ts)
    • Dai, K., Xu, Y. Lutkenhaus, J. (1993) Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsA12(Ts). J Bacteriol 175 : 3790 3797.
    • (1993) J Bacteriol , vol.175 , pp. 3790-3797
    • Dai, K.1    Xu, Y.2    Lutkenhaus, J.3
  • 19
    • 39749105962 scopus 로고    scopus 로고
    • The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin binding protein 3, FtsW, and FtsN
    • Derouaux, A., Wolf, B., Fraipont, C., Breukink, E., Nguyen-Disteche, M. Terrak, M. (2008) The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin binding protein 3, FtsW, and FtsN. J Bacteriol 190 : 1831 1834.
    • (2008) J Bacteriol , vol.190 , pp. 1831-1834
    • Derouaux, A.1    Wolf, B.2    Fraipont, C.3    Breukink, E.4    Nguyen-Disteche, M.5    Terrak, M.6
  • 20
    • 0346252349 scopus 로고    scopus 로고
    • Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: Bacterial septosome differentiation
    • Di Lallo, G., Fagioli, M., Barionovi, D., Ghelardini, P. Paolozzi, L. (2003) Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation. Microbiology 149 : 3353 3359.
    • (2003) Microbiology , vol.149 , pp. 3353-3359
    • Di Lallo, G.1    Fagioli, M.2    Barionovi, D.3    Ghelardini, P.4    Paolozzi, L.5
  • 21
    • 0030747761 scopus 로고    scopus 로고
    • Cell type-specific phosphorylation and proteolysis of a transcriptional regulator controls the G1-to-S transition in a bacterial cell cycle
    • Domian, I.J., Quon, K.C. Shapiro, L. (1997) Cell type-specific phosphorylation and proteolysis of a transcriptional regulator controls the G1-to-S transition in a bacterial cell cycle. Cell 90 : 415 424.
    • (1997) Cell , vol.90 , pp. 415-424
    • Domian, I.J.1    Quon, K.C.2    Shapiro, L.3
  • 22
    • 0031720923 scopus 로고    scopus 로고
    • Only the N-terminal domain of FtsK functions in cell division
    • Draper, G.C., McLennan, N., Begg, K., Masters, M. Donachie, W.D. (1998) Only the N-terminal domain of FtsK functions in cell division. J Bacteriol 180 : 4621 4627.
    • (1998) J Bacteriol , vol.180 , pp. 4621-4627
    • Draper, G.C.1    McLennan, N.2    Begg, K.3    Masters, M.4    Donachie, W.D.5
  • 23
    • 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. 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
  • 24
    • 0025888266 scopus 로고
    • Genetics of Caulobacter crescentus
    • Ely, B. (1991) Genetics of Caulobacter crescentus. Methods Enzymol 204 : 372 384.
    • (1991) Methods Enzymol , vol.204 , pp. 372-384
    • Ely, B.1
  • 25
    • 0017753103 scopus 로고
    • Generalized transduction in Caulobacter crescentus
    • Ely, B. Johnson, R.C. (1977) Generalized transduction in Caulobacter crescentus. Genetics 87 : 391 399.
    • (1977) Genetics , vol.87 , pp. 391-399
    • Ely, B.1    Johnson, R.C.2
  • 26
    • 0017740506 scopus 로고
    • Envelope-associated nucleoid from Caulobacter crescentus stalked and swarmer cells
    • Evinger, M. 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
  • 27
    • 57749083521 scopus 로고    scopus 로고
    • Molecular organization of Gram-negative peptidoglycan
    • Gan, L., Chen, S. Jensen, G.J. (2008) Molecular organization of Gram-negative peptidoglycan. Proc Natl Acad Sci USA 105 : 18953 18957.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 18953-18957
    • Gan, L.1    Chen, S.2    Jensen, G.J.3
  • 28
    • 15844431346 scopus 로고    scopus 로고
    • PSORTb v.2.0: Expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
    • Gardy, J.L., Laird, M.R., Chen, F., Rey, S., Walsh, C.J., Ester, M. Brinkman, F.S. (2005) PSORTb v.2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics 21 : 617 623.
    • (2005) Bioinformatics , vol.21 , pp. 617-623
    • Gardy, J.L.1    Laird, M.R.2    Chen, F.3    Rey, S.4    Walsh, C.J.5    Ester, M.6    Brinkman, F.S.7
  • 29
    • 33846650968 scopus 로고    scopus 로고
    • The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli
    • Gerding, M.A., Ogata, Y., Pecora, N.D., Niki, H. de Boer, P.A. (2007) The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli. Mol Microbiol 63 : 1008 1025.
    • (2007) Mol Microbiol , vol.63 , pp. 1008-1025
    • Gerding, M.A.1    Ogata, Y.2    Pecora, N.D.3    Niki, H.4    De Boer, P.A.5
  • 30
    • 72449160318 scopus 로고    scopus 로고
    • Self-enhanced accumulation of FtsN at division sites, and roles for other proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell constriction
    • Gerding, M.A., Liu, B., Bendezu, F.O., Hale, C.A., Bernhardt, T.G. de Boer, P.A. (2009) Self-enhanced accumulation of FtsN at division sites, and roles for other proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell constriction. J Bacteriol 191 : 7383 7401.
    • (2009) J Bacteriol , vol.191 , pp. 7383-7401
    • Gerding, M.A.1    Liu, B.2    Bendezu, F.O.3    Hale, C.A.4    Bernhardt, T.G.5    De Boer, P.A.6
  • 31
    • 21844441637 scopus 로고    scopus 로고
    • Diverse paths to midcell: Assembly of the bacterial cell division machinery
    • Goehring, N.W. Beckwith, J. (2005) Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr Biol 15 : R514 R526.
    • (2005) Curr Biol , vol.15
    • Goehring, N.W.1    Beckwith, J.2
  • 32
    • 33846198296 scopus 로고    scopus 로고
    • Role for the nonessential N terminus of FtsN in divisome assembly
    • Goehring, N.W., Robichon, C. Beckwith, J. (2007) Role for the nonessential N terminus of FtsN in divisome assembly. J Bacteriol 189 : 646 649.
    • (2007) J Bacteriol , vol.189 , pp. 646-649
    • Goehring, N.W.1    Robichon, C.2    Beckwith, J.3
  • 33
    • 0036791675 scopus 로고    scopus 로고
    • A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ
    • Gueiros-Filho, F.J. Losick, R. (2002) A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ. Genes Dev 16 : 2544 2556.
    • (2002) Genes Dev , vol.16 , pp. 2544-2556
    • Gueiros-Filho, F.J.1    Losick, R.2
  • 34
    • 0031444158 scopus 로고    scopus 로고
    • Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli
    • Hale, C.A. de Boer, P.A. (1997) Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli. Cell 88 : 175 185.
    • (1997) Cell , vol.88 , pp. 175-185
    • Hale, C.A.1    De Boer, P.A.2
  • 35
    • 0034945221 scopus 로고    scopus 로고
    • Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli
    • Heidrich, C., Templin, M.F., Ursinus, A., Merdanovic, M., Berger, J., Schwarz, H., et al. (2001) Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli. Mol Microbiol 41 : 167 178.
    • (2001) Mol Microbiol , vol.41 , pp. 167-178
    • Heidrich, C.1    Templin, M.F.2    Ursinus, A.3    Merdanovic, M.4    Berger, J.5    Schwarz, H.6
  • 36
    • 0036843026 scopus 로고    scopus 로고
    • Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli
    • Heidrich, C., Ursinus, A., Berger, J., Schwarz, H. Holtje, J.V. (2002) Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli. J Bacteriol 184 : 6093 6099.
    • (2002) J Bacteriol , vol.184 , pp. 6093-6099
    • Heidrich, C.1    Ursinus, A.2    Berger, J.3    Schwarz, H.4    Holtje, J.V.5
  • 37
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Holtje, J.V. (1998) Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol Mol Biol Rev 62 : 181 203.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 181-203
    • Holtje, J.V.1
  • 38
    • 0037701542 scopus 로고    scopus 로고
    • Characterization of LytH, a differentiation-associated peptidoglycan hydrolase of Bacillus subtilis involved in endospore cortex maturation
    • Horsburgh, G.J., Atrih, A. Foster, S.J. (2003) Characterization of LytH, a differentiation-associated peptidoglycan hydrolase of Bacillus subtilis involved in endospore cortex maturation. J Bacteriol 185 : 3813 3820.
    • (2003) J Bacteriol , vol.185 , pp. 3813-3820
    • Horsburgh, G.J.1    Atrih, A.2    Foster, S.J.3
  • 41
    • 0015855914 scopus 로고
    • Studies on lysostaphin. Separation and characterization of three enzymes
    • Iversen, O.J. Grov, A. (1973) Studies on lysostaphin. Separation and characterization of three enzymes. Eur J Biochem 38 : 293 300.
    • (1973) Eur J Biochem , vol.38 , pp. 293-300
    • Iversen, O.J.1    Grov, A.2
  • 43
    • 26444490066 scopus 로고    scopus 로고
    • Distinct constrictive processes, separated in time and space, divide Caulobacter inner and outer membranes
    • Judd, E.M., Comolli, L.R., Chen, J.C., Downing, K.H., Moerner, W.E. McAdams, H.H. (2005) Distinct constrictive processes, separated in time and space, divide Caulobacter inner and outer membranes. J Bacteriol 187 : 6874 6882.
    • (2005) J Bacteriol , vol.187 , pp. 6874-6882
    • Judd, E.M.1    Comolli, L.R.2    Chen, J.C.3    Downing, K.H.4    Moerner, W.E.5    McAdams, H.H.6
  • 44
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • Karimova, G., Dautin, N. Ladant, D. (2005) Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J Bacteriol 187 : 2233 2243.
    • (2005) J Bacteriol , vol.187 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 45
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova, G., Pidoux, J., Ullmann, A. Ladant, D. (1998) A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc Natl Acad Sci USA 95 : 5752 5756.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 46
    • 0025966272 scopus 로고
    • Direct proof of a 'more-than-single-layered' peptidoglycan architecture of Escherichia coli W7: A neutron small-angle scattering study
    • Labischinski, H., Goodell, E.W., Goodell, A. Hochberg, M.L. (1991) Direct proof of a 'more-than-single-layered' peptidoglycan architecture of Escherichia coli W7: a neutron small-angle scattering study. J Bacteriol 173 : 751 756.
    • (1991) J Bacteriol , vol.173 , pp. 751-756
    • Labischinski, H.1    Goodell, E.W.2    Goodell, A.3    Hochberg, M.L.4
  • 47
    • 33644753905 scopus 로고    scopus 로고
    • A landmark protein essential for establishing and perpetuating the polarity of a bacterial cell
    • Lam, H., Schofield, W.B. Jacobs-Wagner, C. (2006) A landmark protein essential for establishing and perpetuating the polarity of a bacterial cell. Cell 124 : 1011 1023.
    • (2006) Cell , vol.124 , pp. 1011-1023
    • Lam, H.1    Schofield, W.B.2    Jacobs-Wagner, C.3
  • 48
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li, Z., Trimble, M.J., Brun, Y.V. Jensen, G.J. (2007) The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J 26 : 4694 4708.
    • (2007) EMBO J , vol.26 , pp. 4694-4708
    • Li, Z.1    Trimble, M.J.2    Brun, Y.V.3    Jensen, G.J.4
  • 49
    • 0031902183 scopus 로고    scopus 로고
    • FtsK is a bifunctional protein involved in cell division and chromosome localization in Escherichia coli
    • Liu, G., Draper, G.C. Donachie, W.D. (1998) FtsK is a bifunctional protein involved in cell division and chromosome localization in Escherichia coli. Mol Microbiol 29 : 893 903.
    • (1998) Mol Microbiol , vol.29 , pp. 893-903
    • Liu, G.1    Draper, G.C.2    Donachie, W.D.3
  • 50
    • 34548630230 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring
    • Lutkenhaus, J. (2007) Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring. Annu Rev Biochem 76 : 539 562.
    • (2007) Annu Rev Biochem , vol.76 , pp. 539-562
    • Lutkenhaus, J.1
  • 51
    • 69949158186 scopus 로고    scopus 로고
    • Sculpting the bacterial cell
    • Margolin, W. (2009) Sculpting the bacterial cell. Curr Biol 19 : R812 R822.
    • (2009) Curr Biol , vol.19
    • Margolin, W.1
  • 52
    • 0021053820 scopus 로고
    • Murein structure and lack of DD- and LD-carboxypeptidase activities in Caulobacter crescentus
    • Markiewicz, Z., Glauner, B. Schwarz, U. (1983) Murein structure and lack of DD- and LD-carboxypeptidase activities in Caulobacter crescentus. J Bacteriol 156 : 649 655.
    • (1983) J Bacteriol , vol.156 , pp. 649-655
    • Markiewicz, Z.1    Glauner, B.2    Schwarz, U.3
  • 53
    • 4744340613 scopus 로고    scopus 로고
    • Cell cycle-dependent abundance, stability and localization of FtsA and FtsQ in Caulobacter crescentus
    • Martin, M.E., Trimble, M.J. Brun, Y.V. (2004) Cell cycle-dependent abundance, stability and localization of FtsA and FtsQ in Caulobacter crescentus. Mol Microbiol 54 : 60 74.
    • (2004) Mol Microbiol , vol.54 , pp. 60-74
    • Martin, M.E.1    Trimble, M.J.2    Brun, Y.V.3
  • 54
    • 0031422417 scopus 로고    scopus 로고
    • Dual-axis tomography: An approach with alignment methods that preserve resolution
    • Mastronarde, D.N. (1997) Dual-axis tomography: an approach with alignment methods that preserve resolution. J Struct Biol 120 : 343 352.
    • (1997) J Struct Biol , vol.120 , pp. 343-352
    • Mastronarde, D.N.1
  • 55
    • 0031016796 scopus 로고    scopus 로고
    • Isolation and characterization of a xylose-dependent promoter from Caulobacter crescentus
    • Meisenzahl, A.C., Shapiro, L. Jenal, U. (1997) Isolation and characterization of a xylose-dependent promoter from Caulobacter crescentus. J Bacteriol 179 : 592 600.
    • (1997) J Bacteriol , vol.179 , pp. 592-600
    • Meisenzahl, A.C.1    Shapiro, L.2    Jenal, U.3
  • 57
    • 65549119201 scopus 로고    scopus 로고
    • FtsN-like proteins are conserved components of the cell division machinery in proteobacteria
    • Möll, A. Thanbichler, M. (2009) FtsN-like proteins are conserved components of the cell division machinery in proteobacteria. Mol Microbiol 72 : 1037 1053.
    • (2009) Mol Microbiol , vol.72 , pp. 1037-1053
    • Möll, A.1    Thanbichler, M.2
  • 58
    • 37548998632 scopus 로고    scopus 로고
    • The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli
    • Müller, P., Ewers, C., Bertsche, U., Anstett, M., Kallis, T., Breukink, E., et al. (2007) The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli. J Biol Chem 282 : 36394 36402.
    • (2007) J Biol Chem , vol.282 , pp. 36394-36402
    • Müller, P.1    Ewers, C.2    Bertsche, U.3    Anstett, M.4    Kallis, T.5    Breukink, E.6
  • 60
    • 41949097138 scopus 로고    scopus 로고
    • LysM domains from Pteris ryukyuensis chitinase-A: A stability study and characterization of the chitin binding site
    • Ohnuma, T., Onaga, S., Murata, K., Taira, T. Katoh, E. (2008) LysM domains from Pteris ryukyuensis chitinase-A: a stability study and characterization of the chitin binding site. J Biol Chem 283 : 5178 5187.
    • (2008) J Biol Chem , vol.283 , pp. 5178-5187
    • Ohnuma, T.1    Onaga, S.2    Murata, K.3    Taira, T.4    Katoh, E.5
  • 61
    • 44049091371 scopus 로고    scopus 로고
    • Reconstitution of contractile FtsZ rings in liposomes
    • Osawa, M., Anderson, D.E. Erickson, H.P. (2008) Reconstitution of contractile FtsZ rings in liposomes. Science 320 : 792 794.
    • (2008) Science , vol.320 , pp. 792-794
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 62
    • 70450224670 scopus 로고    scopus 로고
    • Curved FtsZ protofilaments generate bending forces on liposome membranes
    • Osawa, M., Anderson, D.E. Erickson, H.P. (2009) Curved FtsZ protofilaments generate bending forces on liposome membranes. EMBO J 28 : 3476 3484.
    • (2009) EMBO J , vol.28 , pp. 3476-3484
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 63
    • 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
  • 64
    • 34447515813 scopus 로고    scopus 로고
    • Role of peptidoglycan amidases in the development and morphology of the division septum in Escherichia coli
    • Priyadarshini, R., de Pedro, M.A. Young, K.D. (2007) Role of peptidoglycan amidases in the development and morphology of the division septum in Escherichia coli. J Bacteriol 189 : 5334 5347.
    • (2007) J Bacteriol , vol.189 , pp. 5334-5347
    • Priyadarshini, R.1    De Pedro, M.A.2    Young, K.D.3
  • 65
    • 0035113802 scopus 로고    scopus 로고
    • Cell cycle and positional constraints on FtsZ localization and the initiation of cell division in Caulobacter crescentus
    • Quardokus, E.M., Din, N. Brun, Y.V. (2001) Cell cycle and positional constraints on FtsZ localization and the initiation of cell division in Caulobacter crescentus. Mol Microbiol 39 : 949 959.
    • (2001) Mol Microbiol , vol.39 , pp. 949-959
    • Quardokus, E.M.1    Din, N.2    Brun, Y.V.3
  • 66
    • 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. 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
  • 67
    • 0032957487 scopus 로고    scopus 로고
    • Characterization of a chromosomally encoded glycylglycine endopeptidase of Staphylococcus aureus
    • Pt 4
    • Ramadurai, L., Lockwood, K.J., Nadakavukaren, M.J. Jayaswal, R.K. (1999) Characterization of a chromosomally encoded glycylglycine endopeptidase of Staphylococcus aureus. Microbiology 145 (Pt 4 801 808.
    • (1999) Microbiology , vol.145 , pp. 801-808
    • Ramadurai, L.1    Lockwood, K.J.2    Nadakavukaren, M.J.3    Jayaswal, R.K.4
  • 68
    • 0013883373 scopus 로고
    • The development of cellular stalks in bacteria
    • Schmidt, J.M. 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
  • 69
    • 0037930133 scopus 로고    scopus 로고
    • Cell wall attachment of a widely distributed peptidoglycan binding domain is hindered by cell wall constituents
    • Steen, A., Buist, G., Leenhouts, K.J., El Khattabi, M., Grijpstra, F., Zomer, A.L., et al. (2003) Cell wall attachment of a widely distributed peptidoglycan binding domain is hindered by cell wall constituents. J Biol Chem 278 : 23874 23881.
    • (2003) J Biol Chem , vol.278 , pp. 23874-23881
    • Steen, A.1    Buist, G.2    Leenhouts, K.J.3    El Khattabi, M.4    Grijpstra, F.5    Zomer, A.L.6
  • 70
    • 0030035042 scopus 로고    scopus 로고
    • A cell cycle-regulated bacterial DNA methyltransferase is essential for viability
    • Stephens, C., Reisenauer, A., Wright, R. Shapiro, L. (1996) A cell cycle-regulated bacterial DNA methyltransferase is essential for viability. Proc Natl Acad Sci USA 93 : 1210 1214.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1210-1214
    • Stephens, C.1    Reisenauer, A.2    Wright, R.3    Shapiro, L.4
  • 72
    • 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
  • 73
    • 33745699284 scopus 로고    scopus 로고
    • MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter
    • Thanbichler, M. 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
  • 74
    • 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. 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 , pp. 137
    • Thanbichler, M.1    Iniesta, A.A.2    Shapiro, L.3
  • 76
    • 0034884131 scopus 로고    scopus 로고
    • Proteolysis of the Caulobacter McpA chemoreceptor is cell cycle regulated by a ClpX-dependent pathway
    • Tsai, J.W. Alley, M.R. (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.2
  • 77
    • 44349107842 scopus 로고    scopus 로고
    • Growth of Escherichia coli: Significance of peptidoglycan degradation during elongation and septation
    • Uehara, T. Park, J.T. (2008) Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation. J Bacteriol 190 : 3914 3922.
    • (2008) J Bacteriol , vol.190 , pp. 3914-3922
    • Uehara, T.1    Park, J.T.2
  • 78
    • 67749117916 scopus 로고    scopus 로고
    • LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli
    • Uehara, T., Dinh, T. Bernhardt, T.G. (2009) LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli. J Bacteriol 191 : 5094 5107.
    • (2009) J Bacteriol , vol.191 , pp. 5094-5107
    • Uehara, T.1    Dinh, T.2    Bernhardt, T.G.3
  • 79
    • 77951470447 scopus 로고    scopus 로고
    • Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis
    • Uehara, T., Parzych, K.R., Dinh, T. Bernhardt, T.G. (2010) Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis. EMBO J 29 : 1412 1422.
    • (2010) EMBO J , vol.29 , pp. 1412-1422
    • Uehara, T.1    Parzych, K.R.2    Dinh, T.3    Bernhardt, T.G.4
  • 80
    • 4944223117 scopus 로고    scopus 로고
    • Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli
    • Ursinus, A., den Ent, F., Brechtel, S., de Pedro, M., Höltje, J.V., Löwe, J. Vollmer, W. (2004) Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli. J Bacteriol 186 : 6728 6737.
    • (2004) J Bacteriol , vol.186 , pp. 6728-6737
    • Ursinus, A.1    Den Ent, F.2    Brechtel, S.3    De Pedro, M.4    Höltje, J.V.5    Löwe, J.6    Vollmer, W.7
  • 83
    • 0032453738 scopus 로고    scopus 로고
    • FtsI and FtsW are localized to the septum in Escherichia coli
    • Wang, L., Khattar, M.K., Donachie, W.D. Lutkenhaus, J. (1998) FtsI and FtsW are localized to the septum in Escherichia coli. J Bacteriol 180 : 2810 2816.
    • (1998) J Bacteriol , vol.180 , pp. 2810-2816
    • Wang, L.1    Khattar, M.K.2    Donachie, W.D.3    Lutkenhaus, J.4
  • 84
    • 32444436111 scopus 로고    scopus 로고
    • The bifunctional FtsK protein mediates chromosome partitioning and cell division in Caulobacter
    • Wang, S.C., West, L. Shapiro, L. (2006) The bifunctional FtsK protein mediates chromosome partitioning and cell division in Caulobacter. J Bacteriol 188 : 1497 1508.
    • (2006) J Bacteriol , vol.188 , pp. 1497-1508
    • Wang, S.C.1    West, L.2    Shapiro, L.3
  • 85
    • 0030881627 scopus 로고    scopus 로고
    • Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole
    • Weiss, D.S., Pogliano, K., Carson, M., Guzman, L.M., Fraipont, C., Nguyen-Disteche, M., et al. (1997) Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole. Mol Microbiol 25 : 671 681.
    • (1997) Mol Microbiol , vol.25 , pp. 671-681
    • Weiss, D.S.1    Pogliano, K.2    Carson, M.3    Guzman, L.M.4    Fraipont, C.5    Nguyen-Disteche, M.6
  • 87
    • 0347915664 scopus 로고    scopus 로고
    • Genetic analysis of the cell division protein FtsI (PBP3): Amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN
    • Wissel, M.C. Weiss, D.S. (2004) Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN. J Bacteriol 186 : 490 502.
    • (2004) J Bacteriol , vol.186 , pp. 490-502
    • Wissel, M.C.1    Weiss, D.S.2
  • 88
    • 52649134462 scopus 로고    scopus 로고
    • The major and minor wall teichoic acids prevent the sidewall localization of vegetative DL-endopeptidase LytF in Bacillus subtilis
    • Yamamoto, H., Miyake, Y., Hisaoka, M., Kurosawa, S. Sekiguchi, J. (2008) The major and minor wall teichoic acids prevent the sidewall localization of vegetative DL-endopeptidase LytF in Bacillus subtilis. Mol Microbiol 70 : 297 310.
    • (2008) Mol Microbiol , vol.70 , pp. 297-310
    • Yamamoto, H.1    Miyake, Y.2    Hisaoka, M.3    Kurosawa, S.4    Sekiguchi, J.5
  • 89
    • 27744448526 scopus 로고    scopus 로고
    • Peptidoglycan degradation by specialized lytic transglycosylases associated with type III and type IV secretion systems
    • Zahrl, D., Wagner, M., Bischof, K., Bayer, M., Zavecz, B., Beranek, A., et al. (2005) Peptidoglycan degradation by specialized lytic transglycosylases associated with type III and type IV secretion systems. Microbiology 151 : 3455 3467.
    • (2005) Microbiology , vol.151 , pp. 3455-3467
    • Zahrl, D.1    Wagner, M.2    Bischof, K.3    Bayer, M.4    Zavecz, B.5    Beranek, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.