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Volumn 108, Issue 45, 2011, Pages

An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring

Author keywords

Cell division; Cell envelope; Morphogenesis; Peptidoglycan

Indexed keywords

ABC TRANSPORTER; AMIDASE; PROTEIN FTSEX; UNCLASSIFIED DRUG;

EID: 81055145336     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1107780108     Document Type: Article
Times cited : (174)

References (46)
  • 1
    • 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
  • 2
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi EF, Lutkenhaus J (1991) FtsZ ring structure associated with division in Escherichia coli. Nature 354:161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.F.1    Lutkenhaus, J.2
  • 4
    • 0037084109 scopus 로고    scopus 로고
    • Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli
    • DOI 10.1093/emboj/21.4.685
    • 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. (Pubitemid 34174049)
    • (2002) EMBO Journal , vol.21 , Issue.4 , pp. 685-693
    • Pichoff, S.1    Lutkenhaus, J.2
  • 5
    • 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
    • DOI 10.1016/S0092-8674(00)81838-3
    • Hale CA, de Boer PA (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. (Pubitemid 28015866)
    • (1997) Cell , vol.88 , Issue.2 , pp. 175-185
    • Hale, C.A.1    De Boer, P.A.J.2
  • 6
    • 79952401787 scopus 로고    scopus 로고
    • Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers
    • Hale CA, et al. (2011) Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers. J Bacteriol 193:1393-1404.
    • (2011) J Bacteriol , vol.193 , pp. 1393-1404
    • Hale, C.A.1
  • 7
    • 0036791675 scopus 로고    scopus 로고
    • A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ
    • Gueiros-Filho FJ, 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
  • 8
    • 79952403634 scopus 로고    scopus 로고
    • Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli
    • Durand-Heredia JM, Yu HH, De Carlo S, Lesser CF, Janakiraman A (2011) Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli. J Bacteriol 193:1405-1413.
    • (2011) J Bacteriol , vol.193 , pp. 1405-1413
    • Durand-Heredia, J.M.1    Yu, H.H.2    De Carlo, S.3    Lesser, C.F.4    Janakiraman, A.5
  • 9
    • 77953494296 scopus 로고    scopus 로고
    • Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring
    • Galli E, Gerdes K (2010) Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring. Mol Microbiol 76:1514-1526.
    • (2010) Mol Microbiol , vol.76 , pp. 1514-1526
    • Galli, E.1    Gerdes, K.2
  • 10
    • 41749083933 scopus 로고    scopus 로고
    • Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division
    • DOI 10.1111/j.1365-2958.2008.06190.x
    • Ebersbach G, Galli E, Møller-Jensen J, Löwe J, Gerdes K (2008) Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division. Mol Microbiol 68:720-735. (Pubitemid 351490194)
    • (2008) Molecular Microbiology , vol.68 , Issue.3 , pp. 720-735
    • Ebersbach, G.1    Galli, E.2    Moller-Jensen, J.3    Lowe, J.4    Gerdes, K.5
  • 13
    • 0015910158 scopus 로고
    • Process of cellular division in Escherichia coli: Physiological study on thermosensitive mutants defective in cell division
    • Ricard M, Hirota Y (1973) Process of cellular division in Escherichia coli: Physiological study on thermosensitive mutants defective in cell division. J Bacteriol 116:314-322.
    • (1973) J Bacteriol , vol.116 , pp. 314-322
    • Ricard, M.1    Hirota, Y.2
  • 14
    • 0022802404 scopus 로고
    • A new cell division operon in Escherichia coli
    • Gill DR, Hatfull GF, Salmond GP (1986) A new cell division operon in Escherichia coli. Mol Gen Genet 205:134-145.
    • (1986) Mol Gen Genet , vol.205 , pp. 134-145
    • Gill, D.R.1    Hatfull, G.F.2    Salmond, G.P.3
  • 15
    • 0032904859 scopus 로고    scopus 로고
    • Molecular characterization of Escherichia coli FtsE and FtsX
    • de Leeuw E, et al. (1999) Molecular characterization of Escherichia coli FtsE and FtsX. Mol Microbiol 31:983-993.
    • (1999) Mol Microbiol , vol.31 , pp. 983-993
    • De Leeuw, E.1
  • 16
    • 34247859209 scopus 로고    scopus 로고
    • Interaction between cell division proteins FtsE and FtsZ
    • DOI 10.1128/JB.01581-06
    • Corbin BD, Wang Y, Beuria TK, Margolin W (2007) Interaction between cell division proteins FtsE and FtsZ. J Bacteriol 189:3026-3035. (Pubitemid 46697391)
    • (2007) Journal of Bacteriology , vol.189 , Issue.8 , pp. 3026-3035
    • Corbin, B.D.1    Wang, Y.2    Beuria, T.K.3    Margolin, W.4
  • 17
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • DOI 10.1128/JB.187.7.2233-2243.2005
    • 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. (Pubitemid 40389120)
    • (2005) Journal of Bacteriology , vol.187 , Issue.7 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 18
    • 33845944955 scopus 로고    scopus 로고
    • Role of FtsEX in cell division of Escherichia coli: Viability of ftsEX mutants is dependent on functional SufI or high osmotic strength
    • Reddy M (2007) Role of FtsEX in cell division of Escherichia coli: Viability of ftsEX mutants is dependent on functional SufI or high osmotic strength. J Bacteriol 189:98-108.
    • (2007) J Bacteriol , vol.189 , pp. 98-108
    • Reddy, M.1
  • 19
    • 36549022665 scopus 로고    scopus 로고
    • Role of SufI (FtsP) in cell division of Escherichia coli: Evidence for its involvement in stabilizing the assembly of the divisome
    • Samaluru H, SaiSree L, Reddy M (2007) Role of SufI (FtsP) in cell division of Escherichia coli: Evidence for its involvement in stabilizing the assembly of the divisome. J Bacteriol 189:8044-8052.
    • (2007) J Bacteriol , vol.189 , pp. 8044-8052
    • Samaluru, H.1    SaiSree, L.2    Reddy, M.3
  • 20
    • 67549107869 scopus 로고    scopus 로고
    • ATP-binding site lesions in FtsE impair cell division
    • Arends SJ, Kustusch RJ, Weiss DS (2009) ATP-binding site lesions in FtsE impair cell division. J Bacteriol 191:3772-3784.
    • (2009) J Bacteriol , vol.191 , pp. 3772-3784
    • Arends, S.J.1    Kustusch, R.J.2    Weiss, D.S.3
  • 21
    • 39149110299 scopus 로고    scopus 로고
    • Peptidoglycan structure and architecture
    • DOI 10.1111/j.1574-6976.2007.00094.x
    • Vollmer W, Blanot D, de Pedro MA (2008) Peptidoglycan structure and architecture. FEMS Microbiol Rev 32:149-167. (Pubitemid 351257814)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.2 , pp. 149-167
    • Vollmer, W.1    Blanot, D.2    De Pedro, M.A.3
  • 23
    • 34447515813 scopus 로고    scopus 로고
    • Role of peptidoglycan amidases in the development and morphology of the division septum in Escherichia coli
    • DOI 10.1128/JB.00415-07
    • 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. (Pubitemid 47076079)
    • (2007) Journal of Bacteriology , vol.189 , Issue.14 , pp. 5334-5347
    • Priyadarshini, R.1    De Pedro, M.A.2    Young, K.D.3
  • 24
    • 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
  • 25
    • 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 TG (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
  • 26
    • 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
    • DOI 10.1111/j.1365-2958.2004.04063.x
    • Bernhardt TG, de Boer PAJ (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. (Pubitemid 38746301)
    • (2004) Molecular Microbiology , vol.52 , Issue.5 , pp. 1255-1269
    • Bernhardt, T.G.1    De Boer, P.A.J.2
  • 27
    • 78650497005 scopus 로고    scopus 로고
    • Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases
    • Paradis-Bleau C, et al. (2010) Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases. Cell 143:1110-1120.
    • (2010) Cell , vol.143 , pp. 1110-1120
    • Paradis-Bleau, C.1
  • 28
    • 81055126198 scopus 로고    scopus 로고
    • The essential CHAP-domain protein PcsB interacts with the essential cell division protein FtsX in Streptococcus pneumoniae
    • Sham L, Barendt SM, Kopecky KE, Winkler ME (2011) The essential CHAP-domain protein PcsB interacts with the essential cell division protein FtsX in Streptococcus pneumoniae. Proc Natl Acad Sci USA 108:E1061-E1069.
    • (2011) Proc Natl Acad Sci USA , vol.108
    • Sham, L.1    Barendt, S.M.2    Kopecky, K.E.3    Winkler, M.E.4
  • 29
    • 78650431707 scopus 로고    scopus 로고
    • Regulation of peptidoglycan synthesis by outer-membrane proteins
    • Typas A, et al. (2010) Regulation of peptidoglycan synthesis by outer-membrane proteins. Cell 143:1097-1109.
    • (2010) Cell , vol.143 , pp. 1097-1109
    • Typas, A.1
  • 30
    • 0015607366 scopus 로고
    • Morphological mutants of Escherichia coli. Isolation and ultrastructure of a chain-forming envC mutant
    • Rodolakis A, Thomas P, Starka J (1973) Morphological mutants of Escherichia coli. Isolation and ultrastructure of a chain-forming envC mutant. J Gen Microbiol 75:409-416.
    • (1973) J Gen Microbiol , vol.75 , pp. 409-416
    • Rodolakis, A.1    Thomas, P.2    Starka, J.3
  • 31
    • 0036233728 scopus 로고    scopus 로고
    • Proteolytic activity of YibP protein in Escherichia coli
    • DOI 10.1128/JB.184.10.2595-2602.2002
    • Ichimura T, Yamazoe M, Maeda M, Wada C, Hiraga S (2002) Proteolytic activity of YibP protein in Escherichia coli. J Bacteriol 184:2595-2602. (Pubitemid 34457025)
    • (2002) Journal of Bacteriology , vol.184 , Issue.10 , pp. 2595-2602
    • Ichimura, T.1    Yamazoe, M.2    Maeda, M.3    Wada, C.4    Hiraga, S.5
  • 32
    • 0037008119 scopus 로고    scopus 로고
    • Identification and characterization of the Escherichia coli envC gene encoding a periplasmic coiled-coil protein with putative peptidase activity
    • DOI 10.1016/S0378-1097(02)00749-8, PII S0378109702007498
    • Hara H, et al. (2002) Identification and characterization of the Escherichia coli envC gene encoding a periplasmic coiled-coil protein with putative peptidase activity. FEMS Microbiol Lett 212:229-236. (Pubitemid 34756602)
    • (2002) FEMS Microbiology Letters , vol.212 , Issue.2 , pp. 229-236
    • Hara, H.1    Narita, S.2    Karibian, D.3    Park, J.T.4    Yamamoto, Y.5    Nishimura, Y.6
  • 34
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • DOI 10.1128/MMBR.00031-07
    • Davidson AL, Dassa E, Orelle C, Chen J (2008) Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol Mol Biol Rev 72:317-364. (Pubitemid 351822295)
    • (2008) Microbiology and Molecular Biology Reviews , vol.72 , Issue.2 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 35
    • 33750454808 scopus 로고    scopus 로고
    • A novel ligand bound ABC transporter, LolCDE, provides insights into the molecular mechanisms underlying membrane detachment of bacterial lipoproteins
    • DOI 10.1111/j.1365-2958.2006.05378.x
    • Ito Y, Kanamaru K, Taniguchi N, Miyamoto S, Tokuda H (2006) A novel ligand bound ABC transporter, LolCDE, provides insights into the molecular mechanisms underlying membrane detachment of bacterial lipoproteins. Mol Microbiol 62:1064-1075. (Pubitemid 44655318)
    • (2006) Molecular Microbiology , vol.62 , Issue.4 , pp. 1064-1075
    • Ito, Y.1    Kanamaru, K.2    Taniguchi, N.3    Miyamoto, S.4    Tokuda, H.5
  • 36
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare D, Oldham ML, Orelle C, Davidson AL, Chen J (2009) Alternating access in maltose transporter mediated by rigid-body rotations. Mol Cell 33:528-536.
    • (2009) Mol Cell , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 37
    • 0033787084 scopus 로고    scopus 로고
    • A new ABC transporter mediating the detachment of lipid-modified proteins from membranes
    • Yakushi T, Masuda K, Narita S, Matsuyama S, Tokuda H (2000) A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Nat Cell Biol 2:212-218.
    • (2000) Nat Cell Biol , vol.2 , pp. 212-218
    • Yakushi, T.1    Masuda, K.2    Narita, S.3    Matsuyama, S.4    Tokuda, H.5
  • 38
    • 19744376674 scopus 로고    scopus 로고
    • Biochemistry: Global topology analysis of the Escherichia coli inner membrane proteome
    • DOI 10.1126/science.1109730
    • Daley DO, et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308:1321-1323. (Pubitemid 40746130)
    • (2005) Science , vol.308 , Issue.5726 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melen, K.4    Drew, D.5    Von Heijne, G.6
  • 39
    • 4344610718 scopus 로고    scopus 로고
    • Defective cell wall synthesis in Streptococcus pneumoniae R6 depleted for the essential PcsB putative murein hydrolase or the VicR (YycF) response regulator
    • DOI 10.1111/j.1365-2958.2004.04196.x
    • Ng W-L, Kazmierczak KM, Winkler ME (2004) Defective cell wall synthesis in Streptococcus pneumoniae R6 depleted for the essential PcsB putative murein hydrolase or the VicR (YycF) response regulator. Mol Microbiol 53:1161-1175. (Pubitemid 39120437)
    • (2004) Molecular Microbiology , vol.53 , Issue.4 , pp. 1161-1175
    • Ng, W.-L.1    Kazmierczak, K.M.2    Winkler, M.E.3
  • 40
    • 47749095965 scopus 로고    scopus 로고
    • The FtsEX ABC transporter directs cellular differentiation in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2008.06340.x
    • Garti-Levi S, Hazan R, Kain J, Fujita M, Ben-Yehuda S (2008) The FtsEX ABC transporter directs cellular differentiation in Bacillus subtilis. Mol Microbiol 69:1018-1028. (Pubitemid 352033319)
    • (2008) Molecular Microbiology , vol.69 , Issue.4 , pp. 1018-1028
    • Garti-Levi, S.1    Hazan, R.2    Kain, J.3    Fujita, M.4    Ben-Yehuda, S.5
  • 41
    • 0014733740 scopus 로고
    • Model for cell wall growth of Streptococcus faecalis
    • Higgins ML, Shockman GD (1970) Model for cell wall growth of Streptococcus faecalis. J Bacteriol 101:643-648.
    • (1970) J Bacteriol , vol.101 , pp. 643-648
    • Higgins, M.L.1    Shockman, G.D.2
  • 42
    • 0018397527 scopus 로고
    • Electron microscope study of the rod-to-coccus shape change in a temperature-sensitive rod-mutant of Bacillus subtilis
    • Burdett ID (1979) Electron microscope study of the rod-to-coccus shape change in a temperature-sensitive rod- mutant of Bacillus subtilis. J Bacteriol 137:1395-1405.
    • (1979) J Bacteriol , vol.137 , pp. 1395-1405
    • Burdett, I.D.1
  • 43
    • 0028194841 scopus 로고
    • A gene at 59 minutes on the Escherichia coli chromosome encodes a lipoprotein with unusual amino acid repeat sequences
    • Ichikawa JK, Li C, Fu J, Clarke S (1994) A gene at 59 minutes on the Escherichia coli chromosome encodes a lipoprotein with unusual amino acid repeat sequences. J Bacteriol 176:1630-1638. (Pubitemid 24100212)
    • (1994) Journal of Bacteriology , vol.176 , Issue.6 , pp. 1630-1638
    • Ichikawa, J.K.1    Li, C.2    Fu, J.3    Clarke, S.4
  • 44
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
    • Miller JH (1972) Experiments in Molecular Genetics (Cold Spring Harbor Laboratory, Cold Spring Harbor, New York).
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 45
    • 0035682064 scopus 로고    scopus 로고
    • Conditional-replication, integration, excision, and retrieval plasmid-host systems for gene structure-function studies of bacteria
    • DOI 10.1128/JB.183.21.6384-6393.2001
    • Haldimann A, Wanner BL (2001) Conditional-replication, integration, excision, and retrieval plasmid-host systems for gene structure-function studies of bacteria. J Bacteriol 183:6384-6393. (Pubitemid 34059412)
    • (2001) Journal of Bacteriology , vol.183 , Issue.21 , pp. 6384-6393
    • Haldimann, A.1    Wanner, B.L.2
  • 46
    • 19444386428 scopus 로고    scopus 로고
    • SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli
    • DOI 10.1016/j.molcel.2005.04.012, PII S109727650501275X
    • Bernhardt TG, de Boer PAJ (2005) SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli. Mol Cell 18:555-564. (Pubitemid 40726232)
    • (2005) Molecular Cell , vol.18 , Issue.5 , pp. 555-564
    • Bernhardt, T.G.1    De Boer, P.A.J.2


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