메뉴 건너뛰기




Volumn 194, Issue 19, 2012, Pages 5334-5342

ZipA is required for FtsZ-dependent preseptal peptidoglycan synthesis prior to invagination during cell division

Author keywords

[No Author keywords available]

Indexed keywords

FTSZ PROTEIN; PEPTIDOGLYCAN; PROTEIN ZIPA; UNCLASSIFIED DRUG;

EID: 84868326175     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00859-12     Document Type: Article
Times cited : (56)

References (73)
  • 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, et al. 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
  • 2
    • 15944362608 scopus 로고    scopus 로고
    • Maturation of the Escherichia coli divisome occurs in two steps
    • Aarsman ME, et al. 2005. Maturation of the Escherichia coli divisome occurs in two steps. Mol. Microbiol. 55:1631-1645.
    • (2005) Mol. Microbiol. , vol.55 , pp. 1631-1645
    • Aarsman, M.E.1
  • 3
    • 0030837787 scopus 로고    scopus 로고
    • Temperature shift experiments with an ftsZ84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated
    • Addinall SG, Cao C, Lutkenhaus J. 1997. Temperature shift experiments with an ftsZ84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated. J. Bacteriol. 179: 4277-4284.
    • (1997) J. Bacteriol. , vol.179 , pp. 4277-4284
    • Addinall, S.G.1    Cao, C.2    Lutkenhaus, J.3
  • 4
    • 0034529940 scopus 로고    scopus 로고
    • Antibacterial activity of synthetic analogues based on the disaccharide structure of moenomycin, an inhibitor of bacterial transglycosylase
    • Baizman ER, et al. 2000. Antibacterial activity of synthetic analogues based on the disaccharide structure of moenomycin, an inhibitor of bacterial transglycosylase. Microbiology 146:3129-3140.
    • (2000) Microbiology , vol.146 , pp. 3129-3140
    • Baizman, E.R.1
  • 5
    • 0031977950 scopus 로고    scopus 로고
    • Division planes alternate in spherical cells of Escherichia coli
    • Begg KJ, Donachie WD. 1998. Division planes alternate in spherical cells of Escherichia coli. J. Bacteriol. 180:2564-2567.
    • (1998) J. Bacteriol. , vol.180 , pp. 2564-2567
    • Begg, K.J.1    Donachie, W.D.2
  • 6
    • 39749142159 scopus 로고    scopus 로고
    • Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli
    • Bendezú FO, de Boer PA. 2008. Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli. J. Bacteriol. 190:1792-1811.
    • (2008) J. Bacteriol. , vol.190 , pp. 1792-1811
    • Bendezú, F.O.1    de Boer, P.A.2
  • 7
    • 34249811807 scopus 로고    scopus 로고
    • An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coli
    • Bernard CS, Sadasivam M, Shiomi D, Margolin W. 2007. An altered FtsA can compensate for the loss of essential cell division protein FtsN in Escherichia coli. Mol. Microbiol. 64:1289-1305.
    • (2007) Mol. Microbiol. , vol.64 , pp. 1289-1305
    • Bernard, C.S.1    Sadasivam, M.2    Shiomi, D.3    Margolin, W.4
  • 8
    • 0037783310 scopus 로고    scopus 로고
    • The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway
    • Bernhardt TG, de Boer PA. 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
  • 9
    • 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 TG, de Boer PA. 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
  • 10
    • 33748333182 scopus 로고    scopus 로고
    • Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli
    • Bertsche U, et al. 2006. Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli. Mol. Microbiol. 61:675-690.
    • (2006) Mol. Microbiol. , vol.61 , pp. 675-690
    • Bertsche, U.1
  • 11
    • 0020554044 scopus 로고
    • Evidence for diffuse growth of the cylindrical portion of the Escherichia coli murein sacculus
    • Burman LG, Raichler J, Park JT. 1983. Evidence for diffuse growth of the cylindrical portion of the Escherichia coli murein sacculus. J. Bacteriol. 155:983-988.
    • (1983) J. Bacteriol. , vol.155 , pp. 983-988
    • Burman, L.G.1    Raichler, J.2    Park, J.T.3
  • 12
    • 0030742717 scopus 로고    scopus 로고
    • Cell elongation and septation are two mutually exclusive processes in Escherichia coli
    • Canepari P, Signoretto C, Boaretti M, Lleo MM. 1997. Cell elongation and septation are two mutually exclusive processes in Escherichia coli. Arch. Microbiol. 168:152-159.
    • (1997) Arch. Microbiol. , vol.168 , pp. 152-159
    • Canepari, P.1    Signoretto, C.2    Boaretti, M.3    Lleo, M.M.4
  • 14
    • 33646420904 scopus 로고    scopus 로고
    • Orchestrating bacterial cell morphogenesis
    • Carballido-Lopez R. 2006. Orchestrating bacterial cell morphogenesis. Mol. Microbiol. 60:815-819.
    • (2006) Mol. Microbiol. , vol.60 , pp. 815-819
    • Carballido-Lopez, R.1
  • 15
    • 34247859209 scopus 로고    scopus 로고
    • Interaction between cell division proteins FtsE and FtsZ
    • Corbin BD, Wang Y, Beuria TK, Margolin W. 2007. Interaction between cell division proteins FtsE and FtsZ. J. Bacteriol. 189:3026-3035.
    • (2007) J. Bacteriol. , vol.189 , pp. 3026-3035
    • Corbin, B.D.1    Wang, Y.2    Beuria, T.K.3    Margolin, W.4
  • 16
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria. Two distinct ways to make a rod-shaped cell
    • Daniel RA, Errington J. 2003. Control of cell morphogenesis in bacteria. Two distinct ways to make a rod-shaped cell. Cell 113:767-776.
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 17
    • 78649646536 scopus 로고    scopus 로고
    • Advances in understanding E. coli cell fission
    • de Boer PAJ. 2010. Advances in understanding E. coli cell fission. Curr. Opin. Microbiol. 13:730-737.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 730-737
    • de Boer, P.A.J.1
  • 18
    • 0037244586 scopus 로고    scopus 로고
    • Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole
    • den Blaauwen T, Aarsman ME, Vischer NO, Nanninga N. 2003. Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole. Mol. Microbiol. 47:539-547.
    • (2003) Mol. Microbiol. , vol.47 , pp. 539-547
    • den Blaauwen, T.1    Aarsman, M.E.2    Vischer, N.O.3    Nanninga, N.4
  • 20
    • 0032985224 scopus 로고    scopus 로고
    • Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis
    • Denome SA, Elf PK, Henderson TA, Nelson DE, Young KD. 1999. Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis. J. Bacteriol. 181:3981-3993.
    • (1999) J. Bacteriol. , vol.181 , pp. 3981-3993
    • Denome, S.A.1    Elf, P.K.2    Henderson, T.A.3    Nelson, D.E.4    Young, K.D.5
  • 21
    • 0036146905 scopus 로고    scopus 로고
    • Fast lysis of Escherichia coli filament cells requires differentiation of potential division sites
    • de Pedro MA, Holtje JV, Schwarz H. 2002. Fast lysis of Escherichia coli filament cells requires differentiation of potential division sites. Microbiol. 148:79-86.
    • (2002) Microbiol , vol.148 , pp. 79-86
    • de Pedro, M.A.1    Holtje, J.V.2    Schwarz, H.3
  • 23
    • 0037312770 scopus 로고    scopus 로고
    • Branching of Escherichia coli cells arises from multiple sites of inert peptidoglycan
    • de Pedro MA, Young KD, Höltje JV, Schwarz H. 2003. Branching of Escherichia coli cells arises from multiple sites of inert peptidoglycan. J. Bacteriol. 185:1147-1152.
    • (2003) J. Bacteriol. , vol.185 , pp. 1147-1152
    • de Pedro, M.A.1    Young, K.D.2    Höltje, J.V.3    Schwarz, H.4
  • 24
    • 39749105962 scopus 로고    scopus 로고
    • The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillinbinding protein 3, FtsW, and FtsN
    • Derouaux A, et al. 2008. The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillinbinding protein 3, FtsW, and FtsN. J. Bacteriol. 190:1831-1834.
    • (2008) J. Bacteriol. , vol.190 , pp. 1831-1834
    • Derouaux, A.1
  • 25
    • 0030603148 scopus 로고    scopus 로고
    • The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan-synthesising enzymes
    • Di Berardino M, Dijkstra A, Stüber D, Keck W, Gubler M. 1996. The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan-synthesising enzymes. FEBS Lett. 392:184-188.
    • (1996) FEBS Lett , vol.392 , pp. 184-188
    • Di Berardino, M.1    Dijkstra, A.2    Stüber, D.3    Keck, W.4    Gubler, M.5
  • 26
    • 34548677525 scopus 로고    scopus 로고
    • The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes
    • Divakaruni AV, Baida C, White CL, Gober JW. 2007. The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes. Mol. Microbiol. 66:174-188.
    • (2007) Mol. Microbiol. , vol.66 , pp. 174-188
    • Divakaruni, A.V.1    Baida, C.2    White, C.L.3    Gober, J.W.4
  • 27
    • 79960083390 scopus 로고    scopus 로고
    • Processive movement of MreBassociated cell wall biosynthetic complexes in bacteria
    • Dominguez-Escobar J, et al. 2011. Processive movement of MreBassociated cell wall biosynthetic complexes in bacteria. Science 333:225-228.
    • (2011) Science , vol.333 , pp. 225-228
    • Dominguez-Escobar, J.1
  • 28
    • 0037377853 scopus 로고    scopus 로고
    • Identification of ZipA, a signal recognition particle-dependent protein from Neisseria gonorrhoeae
    • Du Y, Arvidson CG. 2003. Identification of ZipA, a signal recognition particle-dependent protein from Neisseria gonorrhoeae. J. Bacteriol. 185: 2122-2130.
    • (2003) J. Bacteriol. , vol.185 , pp. 2122-2130
    • Du, Y.1    Arvidson, C.G.2
  • 29
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shapedetermining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus
    • Figge RM, Divakaruni AV, Gober JW. 2004. MreB, the cell shapedetermining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus. Mol. Microbiol. 51:1321-1332.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1321-1332
    • Figge, R.M.1    Divakaruni, A.V.2    Gober, J.W.3
  • 30
    • 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 333:222-225.
    • (2011) Science , vol.333 , pp. 222-225
    • Garner, E.C.1
  • 31
    • 0037386678 scopus 로고    scopus 로고
    • A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli
    • Geissler B, Elraheb D, Margolin W. 2003. A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 100:4197-4202.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4197-4202
    • Geissler, B.1    Elraheb, D.2    Margolin, W.3
  • 32
    • 26944444295 scopus 로고    scopus 로고
    • Evidence for functional overlap among multiple bacterial cell division proteins: compensating for the loss of FtsK
    • Geissler B, Margolin W. 2005. Evidence for functional overlap among multiple bacterial cell division proteins: compensating for the loss of FtsK. Mol. Microbiol. 58:596-612.
    • (2005) Mol. Microbiol. , vol.58 , pp. 596-612
    • Geissler, B.1    Margolin, W.2
  • 33
    • 33947393232 scopus 로고    scopus 로고
    • The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring
    • Geissler B, Shiomi D, Margolin W. 2007. The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring. Microbiology 153:814-825.
    • (2007) Microbiology , vol.153 , pp. 814-825
    • Geissler, B.1    Shiomi, D.2    Margolin, W.3
  • 34
    • 21844441637 scopus 로고    scopus 로고
    • Diverse paths to midcell: assembly of the bacterial cell division machinery
    • Goehring NW, 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
  • 35
    • 0031736387 scopus 로고    scopus 로고
    • Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs
    • Goffin C, Ghuysen J-M. 1998. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62:1079-1093.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1079-1093
    • Goffin, C.1    Ghuysen, J.-M.2
  • 36
    • 79551614816 scopus 로고    scopus 로고
    • Large ring polymers align FtsZ polymers for normal septum formation
    • Gundogdu ME, et al. 2011. Large ring polymers align FtsZ polymers for normal septum formation. EMBO J. 30:617-626.
    • (2011) EMBO J , vol.30 , pp. 617-626
    • Gundogdu, M.E.1
  • 37
    • 0036229552 scopus 로고    scopus 로고
    • ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli
    • Hale CA, de Boer PA. 2002. ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli. J. Bacteriol. 184:2552-2556.
    • (2002) J. Bacteriol. , vol.184 , pp. 2552-2556
    • Hale, C.A.1    de Boer, P.A.2
  • 38
    • 0033810918 scopus 로고    scopus 로고
    • ZipA-induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains
    • Hale CA, Rhee AC, de Boer PA. 2000. ZipA-induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains. J. Bacteriol. 182:5153-5166.
    • (2000) J. Bacteriol. , vol.182 , pp. 5153-5166
    • Hale, C.A.1    Rhee, A.C.2    de Boer, P.A.3
  • 39
    • 0034945221 scopus 로고    scopus 로고
    • Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli
    • Heidrich C, 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
  • 40
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Höltje 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
    • Höltje, J.-V.1
  • 41
    • 0027251266 scopus 로고
    • The Escherichia coli K-12 "wild types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels
    • Jensen KF. 1993. The Escherichia coli K-12 "wild types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels. J. Bacteriol. 175:3401-3407.
    • (1993) J. Bacteriol. , vol.175 , pp. 3401-3407
    • Jensen, K.F.1
  • 42
    • 1842506701 scopus 로고    scopus 로고
    • ZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coli
    • Johnson JE, Lackner LL, Hale CA, de Boer PA. 2004. ZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coli. J. Bacteriol. 186:2418-2429.
    • (2004) J. Bacteriol. , vol.186 , pp. 2418-2429
    • Johnson, J.E.1    Lackner, L.L.2    Hale, C.A.3    de Boer, P.A.4
  • 43
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse T, Bork-Jensen J, Gerdes K. 2005. The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol. Microbiol. 55:78-89.
    • (2005) Mol. Microbiol. , vol.55 , pp. 78-89
    • Kruse, T.1    Bork-Jensen, J.2    Gerdes, K.3
  • 46
    • 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
  • 47
    • 0033823009 scopus 로고    scopus 로고
    • Themes and variations in prokaryotic cell division
    • Margolin W. 2000. Themes and variations in prokaryotic cell division. FEMS Microbiol. Rev. 24:531-548.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 531-548
    • Margolin, W.1
  • 48
    • 0025775118 scopus 로고
    • Cell division and peptidoglycan assembly in Escherichia coli
    • Nanninga N. 1991. Cell division and peptidoglycan assembly in Escherichia coli. Mol. Microbiol. 5:791-795.
    • (1991) Mol. Microbiol. , vol.5 , pp. 791-795
    • Nanninga, N.1
  • 50
    • 0037084109 scopus 로고    scopus 로고
    • Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli
    • Pichoff S, Lutkenhaus J. 2002. Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli. EMBO J. 21:685-693.
    • (2002) EMBO J , vol.21 , pp. 685-693
    • Pichoff, S.1    Lutkenhaus, J.2
  • 51
    • 84155167132 scopus 로고    scopus 로고
    • FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins
    • Pichoff S, Shen B, Sullivan B, Lutkenhaus J. 2012. FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins. Mol. Microbiol. 83:151-167.
    • (2012) Mol. Microbiol. , vol.83 , pp. 151-167
    • Pichoff, S.1    Shen, B.2    Sullivan, B.3    Lutkenhaus, J.4
  • 52
    • 77954375639 scopus 로고    scopus 로고
    • Septal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment
    • Potluri L, et al. 2010. Septal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment. Mol. Microbiol. 77:300-323.
    • (2010) Mol. Microbiol. , vol.77 , pp. 300-323
    • Potluri, L.1
  • 53
    • 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 MA, Young KD. 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
  • 54
    • 33746649568 scopus 로고    scopus 로고
    • Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli
    • Priyadarshini R, Popham DL, Young KD. 2006. Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli. J. Bacteriol. 188:5345-5355.
    • (2006) J. Bacteriol. , vol.188 , pp. 5345-5355
    • Priyadarshini, R.1    Popham, D.L.2    Young, K.D.3
  • 55
    • 0028324126 scopus 로고
    • The two-competing site (TCS) model for cell shape regulation in bacteria: the envelope as an integration point for the regulatory circuits of essential physiological events
    • Satta G, Fontana R, Canepari P. 1994. The two-competing site (TCS) model for cell shape regulation in bacteria: the envelope as an integration point for the regulatory circuits of essential physiological events. Adv. Microb. Physiol. 36:181-245.
    • (1994) Adv. Microb. Physiol. , vol.36 , pp. 181-245
    • Satta, G.1    Fontana, R.2    Canepari, P.3
  • 56
    • 0040205694 scopus 로고    scopus 로고
    • Cloning and characterization of PBP 1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli
    • Schiffer G, Höltje J-V. 1999. Cloning and characterization of PBP 1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli. J. Biol. Chem. 274:32031-32039.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32031-32039
    • Schiffer, G.1    Höltje, J.-V.2
  • 57
    • 0014674516 scopus 로고
    • Autolytic enzymes and cell division of Escherichia coli
    • Schwarz U, Asmus A, Frank H. 1969. Autolytic enzymes and cell division of Escherichia coli. J. Mol. Biol. 41:419-429.
    • (1969) J. Mol. Biol. , vol.41 , pp. 419-429
    • Schwarz, U.1    Asmus, A.2    Frank, H.3
  • 58
    • 57649165574 scopus 로고    scopus 로고
    • SepF increases the assembly and bundling of FtsZ polymers and stabilizes FtsZ protofilaments by binding along its length
    • Singh JK, Makde RD, Kumar V, Panda D. 2008. SepF increases the assembly and bundling of FtsZ polymers and stabilizes FtsZ protofilaments by binding along its length. J. Biol. Chem. 283:31116-31124.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31116-31124
    • Singh, J.K.1    Makde, R.D.2    Kumar, V.3    Panda, D.4
  • 59
    • 33745285330 scopus 로고    scopus 로고
    • Identification of cell cycle regulators in Mycobacterium tuberculosis by inhibition of septum formation and global transcriptional analysis
    • Slayden RA, Knudson DL, Belisle JT. 2006. Identification of cell cycle regulators in Mycobacterium tuberculosis by inhibition of septum formation and global transcriptional analysis. Microbiology 152:1789-1797.
    • (2006) Microbiology , vol.152 , pp. 1789-1797
    • Slayden, R.A.1    Knudson, D.L.2    Belisle, J.T.3
  • 60
    • 0017803849 scopus 로고
    • On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins
    • Suzuki H, Nishimura Y, Hirota Y. 1978. On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins. Proc. Natl. Acad. Sci. U. S. A. 75:664-668.
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 664-668
    • Suzuki, H.1    Nishimura, Y.2    Hirota, Y.3
  • 61
    • 84855889658 scopus 로고    scopus 로고
    • From the regulation of peptidoglycan synthesis to bacterial growth and morphology
    • Typas A, Banzhaf M, Gross CA, Vollmer W. 2012. From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat. Rev. Microbiol. 10:123-136.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 123-136
    • Typas, A.1    Banzhaf, M.2    Gross, C.A.3    Vollmer, W.4
  • 62
    • 77951470447 scopus 로고    scopus 로고
    • Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis
    • Uehara T, Parzych KR, Dinh T, Bernhardt TG. 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
  • 63
    • 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. U. S. A. 108:15822-15827.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 15822-15827
    • van Teeffelen, S.1
  • 64
    • 34547618469 scopus 로고    scopus 로고
    • FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli
    • Varma A, de Pedro MA, Young KD. 2007. FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli. J. Bacteriol. 189:5692-5704.
    • (2007) J. Bacteriol. , vol.189 , pp. 5692-5704
    • Varma, A.1    de Pedro, M.A.2    Young, K.D.3
  • 65
    • 4944246437 scopus 로고    scopus 로고
    • FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli
    • Varma A, Young KD. 2004. FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli. J. Bacteriol. 186:6768-6774.
    • (2004) J. Bacteriol. , vol.186 , pp. 6768-6774
    • Varma, A.1    Young, K.D.2
  • 66
    • 66149136478 scopus 로고    scopus 로고
    • In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2
    • Varma A, Young KD. 2009. In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2. J. Bacteriol. 191:3526-3533.
    • (2009) J. Bacteriol. , vol.191 , pp. 3526-3533
    • Varma, A.1    Young, K.D.2
  • 67
    • 36749016781 scopus 로고    scopus 로고
    • Duplication and segregation of the actin (MreB) cytoskeleton during the prokaryotic cell cycle
    • Vats P, Rothfield L. 2007. Duplication and segregation of the actin (MreB) cytoskeleton during the prokaryotic cell cycle. Proc. Natl. Acad. Sci. U. S. A. 104:17795-17800.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 17795-17800
    • Vats, P.1    Rothfield, L.2
  • 68
    • 62949149564 scopus 로고    scopus 로고
    • Assembly of the MreB-associated cytoskeletal ring of E. coli
    • Vats P, Shih YL, Rothfield L. 2009. Assembly of the MreB-associated cytoskeletal ring of E. coli. Mol. Microbiol. 72:170-182.
    • (2009) Mol. Microbiol. , vol.72 , pp. 170-182
    • Vats, P.1    Shih, Y.L.2    Rothfield, L.3
  • 69
    • 50049104157 scopus 로고    scopus 로고
    • Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
    • Vollmer W, Bertsche U. 2008. Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli. Biochim. Biophys. Acta 1778: 1714-1734.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1714-1734
    • Vollmer, W.1    Bertsche, U.2
  • 70
    • 0025941965 scopus 로고
    • A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli
    • Wang XD, de Boer PA, Rothfield LI. 1991. A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli. EMBO J. 10:3363-3372.
    • (1991) EMBO J , vol.10 , pp. 3363-3372
    • Wang, X.D.1    de Boer, P.A.2    Rothfield, L.I.3
  • 71
    • 7644219685 scopus 로고    scopus 로고
    • Bacterial cell division and the septal ring
    • Weiss DS. 2004. Bacterial cell division and the septal ring. Mol. Microbiol. 54:588-597.
    • (2004) Mol. Microbiol. , vol.54 , pp. 588-597
    • Weiss, D.S.1
  • 72
    • 0024381715 scopus 로고
    • Rate and topography of peptidoglycan synthesis during cell division in Escherichia coli: concept of a leading edge
    • Wientjes FB, Nanninga N. 1989. Rate and topography of peptidoglycan synthesis during cell division in Escherichia coli: concept of a leading edge. J. Bacteriol. 171:3412-3419.
    • (1989) J. Bacteriol. , vol.171 , pp. 3412-3419
    • Wientjes, F.B.1    Nanninga, N.2
  • 73
    • 0023134582 scopus 로고
    • Topography of peptidoglycan synthesis during elongation and polar cap formation in a cell division mutant of Escherichia coli MC4100
    • Woldringh C, Huls P, Pas E, Brakenhoff GJ, Nanninga N. 1987. Topography of peptidoglycan synthesis during elongation and polar cap formation in a cell division mutant of Escherichia coli MC4100. J. Gen. Microbiol. 133:575-586.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 575-586
    • Woldringh, C.1    Huls, P.2    Pas, E.3    Brakenhoff, G.J.4    Nanninga, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.