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Volumn 194, Issue 20, 2012, Pages 5576-5588

The β-lactam resistance protein Blr, a small membrane polypeptide, is a component of the Escherichia coli cell division machinery

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAM; OLIGONUCLEOTIDE; POLYPEPTIDE; PROTEIN BLR; PROTEIN FTSL; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 84868602418     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00774-12     Document Type: Article
Times cited : (29)

References (52)
  • 2
    • 0030856502 scopus 로고    scopus 로고
    • FtsN, a late recruit to the septum in Escherichia coli
    • Addinall SG, 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
  • 3
    • 77954376358 scopus 로고    scopus 로고
    • Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET
    • Alexeeva S, Gadella TWJ, Verheul J, Verhoeven GS, den Blaauwen T. 2010 Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET. Mol. Microbiol. 77:384-398.
    • (2010) Mol. Microbiol. , vol.77 , pp. 384-398
    • Alexeeva, S.1    Gadella, T.W.J.2    Verheul, J.3    Verhoeven, G.S.4    Blaauwen, T.D.5
  • 4
    • 62949231327 scopus 로고    scopus 로고
    • Hydrophobic peptides: novel regulators within bacterial membrane
    • Alix E, Blanc-Potard AB. 2009. Hydrophobic peptides: novel regulators within bacterial membrane. Mol. Microbiol. 72:5-11.
    • (2009) Mol. Microbiol. , vol.72 , pp. 5-11
    • Alix, E.1    Blanc-Potard, A.B.2
  • 5
    • 38949185102 scopus 로고    scopus 로고
    • Peptide-assisted degradation of the Salmonella MgtC virulence factor
    • Alix E, Blanc-Potard AB. 2008. Peptide-assisted degradation of the Salmonella MgtC virulence factor. EMBO J. 27:546-557.
    • (2008) EMBO J. , vol.27 , pp. 546-557
    • Alix, E.1    Blanc-Potard, A.B.2
  • 6
    • 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 SJ, et al. 2010. 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.
    • (2010) J. Bacteriol. , vol.192 , pp. 242-255
    • Arends, S.J.1
  • 7
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, singlegene knockout mutants: the Keio collection
    • 2006.0008. doi:10.1038/msb41000050
    • Baba T, et al. 2006. Construction of Escherichia coli K-12 in-frame, singlegene knockout mutants: the Keio collection. Mol. Syst. Biol. 2:2006.0008. doi:10.1038/msb41000050.
    • (2006) Mol. Syst. Biol. , vol.2
    • Baba, T.1
  • 8
    • 0019119965 scopus 로고
    • Identification of new genes in a cell envelope-cell division gene cluster of Escherichia coli: cell division gene ftsQ
    • Begg KJ, Hatfull GF, Donachie WD. 1980. Identification of new genes in a cell envelope-cell division gene cluster of Escherichia coli: cell division gene ftsQ. J. Bacteriol. 144:435-437.
    • (1980) J. Bacteriol. , vol.144 , pp. 435-437
    • Begg, K.J.1    Hatfull, G.F.2    Donachie, W.D.3
  • 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    Boer, P.A.D.2
  • 10
    • 0033983166 scopus 로고    scopus 로고
    • Towards single-copy gene expression systems making gene cloning physiologically relevant: lambda InCh, a simple Escherichia coli plasmid-chromosome shuttle system
    • Boyd D, Weiss DS, Chen JC, Beckwith J. 2000. Towards single-copy gene expression systems making gene cloning physiologically relevant: lambda InCh, a simple Escherichia coli plasmid-chromosome shuttle system. J. Bacteriol. 182:842-847.
    • (2000) J. Bacteriol. , vol.182 , pp. 842-847
    • Boyd, D.1    Weiss, D.S.2    Chen, J.C.3    Beckwith, J.4
  • 11
    • 71549130716 scopus 로고    scopus 로고
    • Division site selection in rod-shaped bacteria
    • Bramkamp M, van Baarle S. 2009. Division site selection in rod-shaped bacteria. Curr. Opin. Microbiol. 12:683-688.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 683-688
    • Bramkamp, M.1    Baarle, S.V.2
  • 12
    • 0031752827 scopus 로고    scopus 로고
    • Localization of cell division protein FtsQ by immunofluorescence microscopy in dividing and nondividing cells of Escherichia coli
    • Buddelmeijer N, Aarsman ME, Kolk AH, Vicente M, Nanninga N. 1998. Localization of cell division protein FtsQ by immunofluorescence microscopy in dividing and nondividing cells of Escherichia coli. J. Bacteriol. 180:6107-6116.
    • (1998) J. Bacteriol. , vol.180 , pp. 6107-6116
    • Buddelmeijer, N.1    Aarsman, M.E.2    Kolk, A.H.3    Vicente, M.4    Nanninga, N.5
  • 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
    • 0034740520 scopus 로고    scopus 로고
    • FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division
    • Chen JC, Beckwith J. 2001. FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division. Mol. Microbiol. 42:395-413.
    • (2001) Mol. Microbiol. , vol.42 , pp. 395-413
    • Chen, J.C.1    Beckwith, J.2
  • 15
    • 0032953197 scopus 로고    scopus 로고
    • Septal localization of FtsQ, an essential cell division protein in Escherichia coli
    • Chen JC, Weiss DS, Ghigo JM, Beckwith J. 1999. Septal localization of FtsQ, an essential cell division protein in Escherichia coli. J. Bacteriol. 181: 521-530.
    • (1999) J. Bacteriol. , vol.181 , pp. 521-530
    • Chen, J.C.1    Weiss, D.S.2    Ghigo, J.M.3    Beckwith, J.4
  • 16
    • 0029065955 scopus 로고
    • Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • Cherepanov PP, Wackernagel W. 1995. Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158:9-14.
    • (1995) Gene. , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 17
    • 78049300491 scopus 로고    scopus 로고
    • FtsK DNA translocase: the fast motor that knows where it's going
    • Crozat E, Grainge I. 2010. FtsK DNA translocase: the fast motor that knows where it's going. Chembiochem 11:2232-2243.
    • (2010) Chembiochem , vol.11 , pp. 2232-2243
    • Crozat, E.1    Grainge, I.2
  • 19
    • 78649646536 scopus 로고    scopus 로고
    • Advances in understanding E. coli cell fission
    • de Boer PA. 2010. Advances in understanding E. coli cell fission. Curr. Opin. Microbiol. 13:730-737.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 730-737
    • Boer, P.A.D.1
  • 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
    • Reading
    • 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 (Reading) 149:3353-3359.
    • (2003) Microbiology , vol.149 , pp. 3353-3359
    • Lallo, G.D.1    Fagioli, M.2    Barionovi, D.3    Ghelardini, P.4    Paolozzi, L.5
  • 21
    • 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    Carlo, S.D.3    Lesser, C.F.4    Janakiraman, A.5
  • 22
    • 0342546514 scopus 로고    scopus 로고
    • The KdpF subunit is part of the K(+)-translocating Kdp complex of Escherichia coli and is responsible for stabilization of the complex in vitro
    • Gassel M, Möllenkamp T, Puppe W, Altendorf K. 1999. The KdpF subunit is part of the K(+)-translocating Kdp complex of Escherichia coli and is responsible for stabilization of the complex in vitro. J. Biol. Chem. 274:37901-37907.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37901-37907
    • Gassel, M.1    Möllenkamp, T.2    Puppe, W.3    Altendorf, K.4
  • 23
    • 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 MA, Ogata Y, Pecora ND, Niki H, de Boer PA. 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    Boer, P.A.D.5
  • 24
    • 33745195461 scopus 로고    scopus 로고
    • Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly
    • Goehring NW, Gonzalez MD, Beckwith J. 2006. Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly. Mol. Microbiol. 61:33-45.
    • (2006) Mol. Microbiol. , vol.61 , pp. 33-45
    • Goehring, N.W.1    Gonzalez, M.D.2    Beckwith, J.3
  • 25
    • 77952577603 scopus 로고    scopus 로고
    • Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex
    • Gonzalez MD, Akbay EA, Boyd D, Beckwith J. 2010. Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex. J. Bacteriol. 192:2757-2768.
    • (2010) J. Bacteriol. , vol.192 , pp. 2757-2768
    • Gonzalez, M.D.1    Akbay, E.A.2    Boyd, D.3    Beckwith, J.4
  • 26
    • 0036291504 scopus 로고    scopus 로고
    • Measuring beta-galactosidase activity in bacteria: cell growth, permeabilization, and enzyme assays in 96-well arrays
    • Griffith KL, Wolf RE. 2002. Measuring beta-galactosidase activity in bacteria: cell growth, permeabilization, and enzyme assays in 96-well arrays. Biochem. Biophys. Res. Commun. 290:397-402.
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 397-402
    • Griffith, K.L.1    Wolf, R.E.2
  • 27
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 28
    • 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
  • 29
    • 33846246039 scopus 로고    scopus 로고
    • Bacterial cell division: the mechanism and its precison
    • Harry E, Monahan L, Thompson L. 2006. Bacterial cell division: the mechanism and its precison. Int. Rev. Cytol. 253:27-94.
    • (2006) Int. Rev. Cytol. , vol.253 , pp. 27-94
    • Harry, E.1    Monahan, L.2    Thompson, L.3
  • 30
    • 73849131808 scopus 로고    scopus 로고
    • Small RNAs and small proteins involved in resistance to cell envelope stress and acid shock in Escherichia coli: analysis of a bar-coded mutant collection
    • Hobbs EC, Astarita JL, Storz G. 2010. Small RNAs and small proteins involved in resistance to cell envelope stress and acid shock in Escherichia coli: analysis of a bar-coded mutant collection. J. Bacteriol. 192:59-67.
    • (2010) J. Bacteriol. , vol.192 , pp. 59-67
    • Hobbs, E.C.1    Astarita, J.L.2    Storz, G.3
  • 32
    • 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
  • 33
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial twohybrid system based on a reconstituted signal transduction pathway
    • U. S. A.
    • Karimova G, Pidoux J, Ullmann A, Ladant D. 1998. A bacterial twohybrid system based on a reconstituted signal transduction pathway. Proc. Natl. Acad. Sci. U. S. A. 95:5752-5756.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 34
    • 58149492417 scopus 로고    scopus 로고
    • Characterization of YmgF, a 72-residue inner membrane protein that associates with the Escherichia coli cell division machinery
    • Karimova G, Robichon C, Ladant D. 2009. Characterization of YmgF, a 72-residue inner membrane protein that associates with the Escherichia coli cell division machinery. J. Bacteriol. 191:333-346.
    • (2009) J. Bacteriol. , vol.191 , pp. 333-346
    • Karimova, G.1    Robichon, C.2    Ladant, D.3
  • 35
    • 0035151432 scopus 로고    scopus 로고
    • Protein-protein interaction between Bacillus stearothermophilus tyrosyl-tRNA synthetase subdomains revealed by a bacterial two-hybrid system
    • Karimova G, Ullmann A, Ladant D. 2001. Protein-protein interaction between Bacillus stearothermophilus tyrosyl-tRNA synthetase subdomains revealed by a bacterial two-hybrid system. J. Mol. Microbiol. Biotechnol. 3:73-82.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 73-82
    • Karimova, G.1    Ullmann, A.2    Ladant, D.3
  • 36
    • 0037195381 scopus 로고    scopus 로고
    • Topological characterization of the essential Escherichia coli cell division protein FtsW
    • Lara B, Ayala JA. 2002. Topological characterization of the essential Escherichia coli cell division protein FtsW. FEMS Microbiol. Lett. 216: 23-32.
    • (2002) FEMS Microbiol. Lett. , vol.216 , pp. 23-32
    • Lara, B.1    Ayala, J.A.2
  • 37
    • 69949158186 scopus 로고    scopus 로고
    • Sculpting the bacterial cell
    • doi:10.1016/j.cub.2009.06.033
    • Margolin W. 2009. Sculpting the bacterial cell. Curr. Biol. 19:R812-R822. doi:10.1016/j.cub.2009.06.033.
    • (2009) Curr. Biol. , vol.19
    • Margolin, W.1
  • 39
    • 79959677792 scopus 로고    scopus 로고
    • A DNA damage checkpoint in Caulobacter crescentus inhibits cell division through a direct interaction with FtsW
    • Modell JW, Hopkins AC, Laub MT. 2011. A DNA damage checkpoint in Caulobacter crescentus inhibits cell division through a direct interaction with FtsW. Genes Dev. 25:1328-1343.
    • (2011) Genes. Dev. , vol.25 , pp. 1328-1343
    • Modell, J.W.1    Hopkins, A.C.2    Laub, M.T.3
  • 40
    • 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
  • 41
    • 80052525834 scopus 로고    scopus 로고
    • A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators
    • Peters NT, Dinh T, Bernhardt TG. 2011. A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators. J. Bacteriol. 193:4973-4983.
    • (2011) J. Bacteriol. , vol.193 , pp. 4973-4983
    • Peters, N.T.1    Dinh, T.2    Bernhardt, T.G.3
  • 42
    • 0024078007 scopus 로고
    • Cell division control in Escherichia coli K-12: some properties of the ftsZ84 mutation and suppression of this mutation by the product of a newly identified gene
    • Phoenix P, Drapeau GR. 1988. Cell division control in Escherichia coli K-12: some properties of the ftsZ84 mutation and suppression of this mutation by the product of a newly identified gene. J. Bacteriol. 170:4338-4342.
    • (1988) J. Bacteriol. , vol.170 , pp. 4338-4342
    • Phoenix, P.1    Drapeau, G.R.2
  • 43
    • 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
  • 44
    • 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
  • 45
    • 77951562635 scopus 로고    scopus 로고
    • Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring
    • Rico AI, García-Ovalle M, Palacios P, Casanova M, Vicente M. 2010. Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring. Mol. Microbiol. 76:760-771.
    • (2010) Mol. Microbiol. , vol.76 , pp. 760-771
    • Rico, A.I.1    García-Ovalle, M.2    Palacios, P.3    Casanova, M.4    Vicente, M.5
  • 46
    • 80052543964 scopus 로고    scopus 로고
    • Role of leucine zipper motifs in association of the Escherichia coli cell division proteins FtsL and FtsB
    • Robichon C, Karimova G, Beckwith J, Ladant D. 2011. Role of leucine zipper motifs in association of the Escherichia coli cell division proteins FtsL and FtsB. J. Bacteriol. 193:4988-4992.
    • (2011) J. Bacteriol. , vol.193 , pp. 4988-4992
    • Robichon, C.1    Karimova, G.2    Beckwith, J.3    Ladant, D.4
  • 48
    • 0025960091 scopus 로고
    • A novel rho promoter::Tn10 mutation suppresses an ftsQ1(Ts) missense mutation in an essential Escherichia coli cell division gene by a mechanism not involving polarity suppression
    • Storts DR, Markovitz A. 1991. A novel rho promoter::Tn10 mutation suppresses an ftsQ1(Ts) missense mutation in an essential Escherichia coli cell division gene by a mechanism not involving polarity suppression. J. Bacteriol. 173:655-663.
    • (1991) J. Bacteriol. , vol.173 , pp. 655-663
    • Storts, D.R.1    Markovitz, A.2
  • 49
    • 78650431707 scopus 로고    scopus 로고
    • Regulation of peptidoglycan synthesis by outermembrane proteins
    • Typas A, et al. 2010. Regulation of peptidoglycan synthesis by outermembrane proteins. Cell 143:1097-1109.
    • (2010) Cell , vol.143 , pp. 1097-1109
    • Typas, A.1
  • 50
    • 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
  • 51
    • 0032932435 scopus 로고    scopus 로고
    • Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL
    • Weiss DS, Chen JC, Ghigo JM, Boyd D, Beckwith J. 1999. Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL. J. Bacteriol. 181:508-520.
    • (1999) J. Bacteriol. , vol.181 , pp. 508-520
    • Weiss, D.S.1    Chen, J.C.2    Ghigo, J.M.3    Boyd, D.4    Beckwith, J.5
  • 52
    • 0033913572 scopus 로고    scopus 로고
    • 'Intergenic' blr gene in Escherichia coli encodes a 41-residue membrane protein affecting intrinsic susceptibility to certain inhibitors of peptidoglycan synthesis
    • Wong RS, McMurry LM, Levy SB. 2000. 'Intergenic' blr gene in Escherichia coli encodes a 41-residue membrane protein affecting intrinsic susceptibility to certain inhibitors of peptidoglycan synthesis. Mol. Microbiol. 37:364-370.
    • (2000) Mol. Microbiol. , vol.37 , pp. 364-370
    • Wong, R.S.1    Mcmurry, L.M.2    Levy, S.B.3


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