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Volumn 11, Issue 12, 2015, Pages

LipidII: Just Another Brick in the Wall?

Author keywords

[No Author keywords available]

Indexed keywords

LIPID II; MEMBRANE LIPID; MEMBRANE PROTEIN; PENICILLIN BINDING PROTEIN; PEPTIDOGLYCAN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN;

EID: 84953326972     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1005213     Document Type: Review
Times cited : (28)

References (71)
  • 1
    • 73649122749 scopus 로고    scopus 로고
    • An oldie but a goodie—cell wall biosynthesis as antibiotic target pathway
    • Schneider T, Sahl HG, An oldie but a goodie—cell wall biosynthesis as antibiotic target pathway. IJMM. 2010;300(2–3):161–9. doi: 10.1016/j.ijmm.2009.10.005 20005776
    • (2010) IJMM , vol.300 , Issue.2-3 , pp. 161-169
    • Schneider, T.1    Sahl, H.G.2
  • 3
    • 84861892432 scopus 로고    scopus 로고
    • Structural perspective of peptidoglycan biosynthesis and assembly
    • Lovering AL, Safadi SS, Strynadka NC, Structural perspective of peptidoglycan biosynthesis and assembly. Annu Rev Biochem. 2012;81:451–78. doi: 10.1146/annurev-biochem-061809-112742 22663080
    • (2012) Annu Rev Biochem , vol.81 , pp. 451-478
    • Lovering, A.L.1    Safadi, S.S.2    Strynadka, N.C.3
  • 4
    • 84855889658 scopus 로고    scopus 로고
    • From the regulation of peptidoglycan synthesis to bacterial growth and morphology
    • Typas A, Banzhaf M, Gross CA, Vollmer W, From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat Rev Microbiol. 2012;10(2):123–36.
    • (2012) Nat Rev Microbiol , vol.10 , Issue.2 , pp. 123-136
    • Typas, A.1    Banzhaf, M.2    Gross, C.A.3    Vollmer, W.4
  • 5
    • 84896694420 scopus 로고    scopus 로고
    • Different walls for rods and balls: the diversity of peptidoglycan
    • Turner RD, Vollmer W, Foster SJ, Different walls for rods and balls: the diversity of peptidoglycan. Mol Microbiol. 2014;91(5):862–74. doi: 10.1111/mmi.12513 24405365
    • (2014) Mol Microbiol , vol.91 , Issue.5 , pp. 862-874
    • Turner, R.D.1    Vollmer, W.2    Foster, S.J.3
  • 6
    • 79952701515 scopus 로고    scopus 로고
    • Bacterial cell wall assembly: still an attractive antibacterial target
    • Bugg TD, Braddick D, Dowson CG, Roper DI, Bacterial cell wall assembly: still an attractive antibacterial target. Trends Biotechnol. 2011;29(4):167–73. doi: 10.1016/j.tibtech.2010.12.006 21232809
    • (2011) Trends Biotechnol , vol.29 , Issue.4 , pp. 167-173
    • Bugg, T.D.1    Braddick, D.2    Dowson, C.G.3    Roper, D.I.4
  • 7
    • 84922937832 scopus 로고    scopus 로고
    • A new antibiotic kills pathogens without detectable resistance
    • Ling LL, Schneider T, Peoples AJ, Spoering AL, Engels I, Conlon BP, et al. A new antibiotic kills pathogens without detectable resistance. Nature. 2015;517(7535):455–9. doi: 10.1038/nature14098 25561178
    • (2015) Nature , vol.517 , Issue.7535 , pp. 455-459
    • Ling, L.L.1    Schneider, T.2    Peoples, A.J.3    Spoering, A.L.4    Engels, I.5    Conlon, B.P.6
  • 8
    • 33645474378 scopus 로고    scopus 로고
    • Lipid II as a target for antibiotics
    • Breukink E, de Kruijff B, Lipid II as a target for antibiotics. Nat Rev Drug Discov. 2006;5(4):321–32. 16531990
    • (2006) Nat Rev Drug Discov , vol.5 , Issue.4 , pp. 321-332
    • Breukink, E.1    de Kruijff, B.2
  • 9
    • 84896708374 scopus 로고    scopus 로고
    • A new metabolic cell-wall labelling method reveals peptidoglycan in Chlamydia trachomatis
    • Liechti GW, Kuru E, Hall E, Kalinda A, Brun YV, VanNieuwenhze M, et al. A new metabolic cell-wall labelling method reveals peptidoglycan in Chlamydia trachomatis. Nature. 2014;506(7489):507–10. doi: 10.1038/nature12892 24336210
    • (2014) Nature , vol.506 , Issue.7489 , pp. 507-510
    • Liechti, G.W.1    Kuru, E.2    Hall, E.3    Kalinda, A.4    Brun, Y.V.5    VanNieuwenhze, M.6
  • 10
    • 84890205605 scopus 로고    scopus 로고
    • Discovery of chlamydial peptidoglycan reveals bacteria with murein sacculi but without FtsZ
    • Pilhofer M, Aistleitner K, Biboy J, Gray J, Kuru E, Hall E, et al. Discovery of chlamydial peptidoglycan reveals bacteria with murein sacculi but without FtsZ. Nat Commun. 2013;4:2856. doi: 10.1038/ncomms3856 24292151
    • (2013) Nat Commun , vol.4 , pp. 2856
    • Pilhofer, M.1    Aistleitner, K.2    Biboy, J.3    Gray, J.4    Kuru, E.5    Hall, E.6
  • 11
    • 70350139038 scopus 로고    scopus 로고
    • Functional conservation of the lipid II biosynthesis pathway in the cell wall-less bacteria Chlamydia and Wolbachia: why is lipid II needed?
    • Henrichfreise B, Schiefer A, Schneider T, Nzukou E, Poellinger C, Hoffmann TJ, et al. Functional conservation of the lipid II biosynthesis pathway in the cell wall-less bacteria Chlamydia and Wolbachia: why is lipid II needed? Molecular Microbiology. 2009;73(5):913–23. doi: 10.1111/j.1365-2958.2009.06815.x 19656295
    • (2009) Molecular Microbiology , vol.73 , Issue.5 , pp. 913-923
    • Henrichfreise, B.1    Schiefer, A.2    Schneider, T.3    Nzukou, E.4    Poellinger, C.5    Hoffmann, T.J.6
  • 12
    • 0033574743 scopus 로고    scopus 로고
    • Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala-D-Ala
    • Ge M, Chen Z, Onishi HR, Kohler J, Silver LL, Kerns R, et al. Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala-D-Ala. Science. 1999;284(5413):507–11. 10205063
    • (1999) Science , vol.284 , Issue.5413 , pp. 507-511
    • Ge, M.1    Chen, Z.2    Onishi, H.R.3    Kohler, J.4    Silver, L.L.5    Kerns, R.6
  • 13
    • 84905924514 scopus 로고    scopus 로고
    • Prospects for novel inhibitors of peptidoglycan transglycosylases
    • Galley NF, O'Reilly AM, Roper DI, Prospects for novel inhibitors of peptidoglycan transglycosylases. Bioorg Chem. 2014;55:16–26. doi: 10.1016/j.bioorg.2014.05.007 24924926
    • (2014) Bioorg Chem , vol.55 , pp. 16-26
    • Galley, N.F.1    O'Reilly, A.M.2    Roper, D.I.3
  • 14
    • 84943817577 scopus 로고    scopus 로고
    • Structural variations of the cell wall precursor lipid II in Gram-positive bacteria—Impact on binding and efficacy of antimicrobial peptides
    • Münch D, Sahl HG, Structural variations of the cell wall precursor lipid II in Gram-positive bacteria—Impact on binding and efficacy of antimicrobial peptides. Biochim Biophys Acta. 2015; 1848(11 Pt B):3062–71. doi: 10.1016/j.bbamem.2015.04.014 25934055
    • (2015) Biochim Biophys Acta , vol.1848 , Issue.11 , pp. 3062-3071
    • Münch, D.1    Sahl, H.G.2
  • 16
    • 84893356438 scopus 로고    scopus 로고
    • Cyclic lipodepsipeptides: a new class of antibacterial agents in the battle against resistant bacteria
    • Bionda N, Pitteloud JP, Cudic P, Cyclic lipodepsipeptides: a new class of antibacterial agents in the battle against resistant bacteria. Future Med Chem. 2013;5(11):1311–30. doi: 10.4155/fmc.13.86 23859209
    • (2013) Future Med Chem , vol.5 , Issue.11 , pp. 1311-1330
    • Bionda, N.1    Pitteloud, J.P.2    Cudic, P.3
  • 17
    • 84861649020 scopus 로고    scopus 로고
    • Discovery, biosynthesis, and engineering of lantipeptides
    • Knerr PJ, van der Donk WA, Discovery, biosynthesis, and engineering of lantipeptides. Annu Rev Biochem. 2012;81:479–505. doi: 10.1146/annurev-biochem-060110-113521 22404629
    • (2012) Annu Rev Biochem , vol.81 , pp. 479-505
    • Knerr, P.J.1    van der Donk, W.A.2
  • 18
    • 4744345463 scopus 로고    scopus 로고
    • The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics
    • Hsu ST, Breukink E, Tischenko E, Lutters MA, de Kruijff B, Kaptein R, et al. The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics. Nat Struct Mol Biol. 2004;11(10):963–7. 15361862
    • (2004) Nat Struct Mol Biol , vol.11 , Issue.10 , pp. 963-967
    • Hsu, S.T.1    Breukink, E.2    Tischenko, E.3    Lutters, M.A.4    de Kruijff, B.5    Kaptein, R.6
  • 19
    • 10044290579 scopus 로고    scopus 로고
    • Targeting extracellular pyrophosphates underpins the high selectivity of nisin
    • Bonev BB, Breukink E, Swiezewska E, De Kruijff B, Watts A, Targeting extracellular pyrophosphates underpins the high selectivity of nisin. FASEB J. 2004;18(15):1862–9. 15576489
    • (2004) FASEB J , vol.18 , Issue.15 , pp. 1862-1869
    • Bonev, B.B.1    Breukink, E.2    Swiezewska, E.3    De Kruijff, B.4    Watts, A.5
  • 20
    • 33748766086 scopus 로고    scopus 로고
    • An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II
    • Hasper HE, Kramer NE, Smith JL, Hillman JD, Zachariah C, Kuipers OP, et al. An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II. Science. 2006;313(5793):1636–7. 16973881
    • (2006) Science , vol.313 , Issue.5793 , pp. 1636-1637
    • Hasper, H.E.1    Kramer, N.E.2    Smith, J.L.3    Hillman, J.D.4    Zachariah, C.5    Kuipers, O.P.6
  • 21
    • 84953255888 scopus 로고    scopus 로고
    • In Vivo Cluster Formation of Nisin and Lipid II Is Correlated with Membrane Depolarization
    • Tol MB, Morales Angeles D, Scheffers DJ, In Vivo Cluster Formation of Nisin and Lipid II Is Correlated with Membrane Depolarization. Antimicrob Agents Chemother. 2015;59(6):3683–6. doi: 10.1128/AAC.04781-14 25870072
    • (2015) Antimicrob Agents Chemother , vol.59 , Issue.6 , pp. 3683-3686
    • Tol, M.B.1    Morales, A.D.2    Scheffers, D.J.3
  • 22
    • 33748506881 scopus 로고    scopus 로고
    • The mode of action of the lantibiotic lacticin 3147—a complex mechanism involving specific interaction of two peptides and the cell wall precursor lipid II
    • Wiedemann I, Bottiger T, Bonelli RR, Wiese A, Hagge SO, Gutsmann T, et al. The mode of action of the lantibiotic lacticin 3147—a complex mechanism involving specific interaction of two peptides and the cell wall precursor lipid II. Mol Microbiol. 2006;61(2):285–96. 16771847
    • (2006) Mol Microbiol , vol.61 , Issue.2 , pp. 285-296
    • Wiedemann, I.1    Bottiger, T.2    Bonelli, R.R.3    Wiese, A.4    Hagge, S.O.5    Gutsmann, T.6
  • 23
    • 80455168091 scopus 로고    scopus 로고
    • Haloduracin alpha binds the peptidoglycan precursor lipid II with 2:1 stoichiometry
    • Oman TJ, Lupoli TJ, Wang TS, Kahne D, Walker S, van der Donk WA, Haloduracin alpha binds the peptidoglycan precursor lipid II with 2:1 stoichiometry. J Am Chem Soc. 2011;133(44):17544–7. doi: 10.1021/ja206281k 22003874
    • (2011) J Am Chem Soc , vol.133 , Issue.44 , pp. 17544-17547
    • Oman, T.J.1    Lupoli, T.J.2    Wang, T.S.3    Kahne, D.4    Walker, S.5    van der Donk, W.A.6
  • 24
    • 33748490494 scopus 로고    scopus 로고
    • A lesson in efficient killing from two-component lantibiotics
    • Breukink E, A lesson in efficient killing from two-component lantibiotics. Mol Microbiol. 2006;61(2):271–3. 16771845
    • (2006) Mol Microbiol , vol.61 , Issue.2 , pp. 271-273
    • Breukink, E.1
  • 25
    • 84899427900 scopus 로고    scopus 로고
    • The lantibiotic NAI-107 binds to bactoprenol-bound cell wall precursors and impairs membrane functions
    • Munch D, Muller A, Schneider T, Kohl B, Wenzel M, Bandow JE, et al. The lantibiotic NAI-107 binds to bactoprenol-bound cell wall precursors and impairs membrane functions. J Biol Chem. 2014;289(17):12063–76. doi: 10.1074/jbc.M113.537449 24627484
    • (2014) J Biol Chem , vol.289 , Issue.17 , pp. 12063-12076
    • Munch, D.1    Muller, A.2    Schneider, T.3    Kohl, B.4    Wenzel, M.5    Bandow, J.E.6
  • 26
    • 77955814236 scopus 로고    scopus 로고
    • Microbisporicin gene cluster reveals unusual features of lantibiotic biosynthesis in actinomycetes
    • Foulston LC, Bibb MJ, Microbisporicin gene cluster reveals unusual features of lantibiotic biosynthesis in actinomycetes. Proc Natl Acad Sci U S A. 2010;107(30):13461–6. doi: 10.1073/pnas.1008285107 20628010
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.30 , pp. 13461-13466
    • Foulston, L.C.1    Bibb, M.J.2
  • 27
    • 0023808730 scopus 로고
    • Plasmid-mediated resistance to vancomycin and teicoplanin in Enterococcus faecium
    • Leclercq R, Derlot E, Duval J, Courvalin P, Plasmid-mediated resistance to vancomycin and teicoplanin in Enterococcus faecium. N Engl J Med. 1988;319(3):157–61. 2968517
    • (1988) N Engl J Med , vol.319 , Issue.3 , pp. 157-161
    • Leclercq, R.1    Derlot, E.2    Duval, J.3    Courvalin, P.4
  • 28
    • 0031944802 scopus 로고    scopus 로고
    • Control of cell shape and elongation by the rodA gene in Bacillus subtilis
    • Henriques AO, Glaser P, Piggot PJ, P MC Jr.Control of cell shape and elongation by the rodA gene in Bacillus subtilis. Mol Microbiol. 1998;28(2):235–47. 9622350
    • (1998) Mol Microbiol , vol.28 , Issue.2 , pp. 235-247
    • Henriques, A.O.1    Glaser, P.2    Piggot, P.J.3    P MC4
  • 29
    • 0032453738 scopus 로고    scopus 로고
    • FtsI and FtsW are localized to the septum in Escherichia coli
    • Wang L, Khattar MK, Donachie WD, Lutkenhaus J, FtsI and FtsW are localized to the septum in Escherichia coli. J Bacteriol. 1998;180(11):2810–6. 9603865
    • (1998) J Bacteriol , vol.180 , Issue.11 , pp. 2810-2816
    • Wang, L.1    Khattar, M.K.2    Donachie, W.D.3    Lutkenhaus, J.4
  • 30
    • 0028034240 scopus 로고
    • Identification of FtsW and characterization of a new ftsW division mutant of Escherichia coli
    • Khattar MM, Begg KJ, Donachie WD, Identification of FtsW and characterization of a new ftsW division mutant of Escherichia coli. J Bacteriol. 1994;176(23):7140–7. 7961485
    • (1994) J Bacteriol , vol.176 , Issue.23 , pp. 7140-7147
    • Khattar, M.M.1    Begg, K.J.2    Donachie, W.D.3
  • 31
    • 84938498767 scopus 로고    scopus 로고
    • Validation of FRET Assay for the Screening of Growth Inhibitors of Escherichia coli Reveals Elongasome Assembly Dynamics
    • van der Ploeg R, Goudelis S, den Blaauwen T, Validation of FRET Assay for the Screening of Growth Inhibitors of Escherichia coli Reveals Elongasome Assembly Dynamics. Int J Mol Sci. 2015;16(8):17637–54. doi: 10.3390/ijms160817637 26263980
    • (2015) Int J Mol Sci , vol.16 , Issue.8 , pp. 17637-17654
    • van der Ploeg, R.1    Goudelis, S.2    den Blaauwen, T.3
  • 32
    • 0034976746 scopus 로고    scopus 로고
    • Constitutive septal murein synthesis in Escherichia coli with impaired activity of the morphogenetic proteins RodA and penicillin-binding protein 2
    • de Pedro MA, Donachie WD, Höltje JV, Schwarz H, Constitutive septal murein synthesis in Escherichia coli with impaired activity of the morphogenetic proteins RodA and penicillin-binding protein 2. J Bacteriol. 2001;183(14):4115–26. 11418550
    • (2001) J Bacteriol , vol.183 , Issue.14 , pp. 4115-4126
    • de Pedro, M.A.1    Donachie, W.D.2    Höltje, J.V.3    Schwarz, H.4
  • 33
    • 79955007775 scopus 로고    scopus 로고
    • Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane
    • Mohammadi T, van Dam V, Sijbrandi R, Vernet T, Zapun A, Bouhss A, et al. Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane. EMBO J. 2011;30(8):1425–32. doi: 10.1038/emboj.2011.61 21386816
    • (2011) EMBO J , vol.30 , Issue.8 , pp. 1425-1432
    • Mohammadi, T.1    van Dam, V.2    Sijbrandi, R.3    Vernet, T.4    Zapun, A.5    Bouhss, A.6
  • 34
    • 84901389207 scopus 로고    scopus 로고
    • Specificity of the transport of lipid II by FtsW in Escherichia coli
    • Mohammadi T, Sijbrandi R, Lutters M, Verheul J, Martin NI, den Blaauwen T, et al. Specificity of the transport of lipid II by FtsW in Escherichia coli. J Biol Chem. 2014;289(21):14707–18. doi: 10.1074/jbc.M114.557371 24711460
    • (2014) J Biol Chem , vol.289 , Issue.21 , pp. 14707-14718
    • Mohammadi, T.1    Sijbrandi, R.2    Lutters, M.3    Verheul, J.4    Martin, N.I.5    den Blaauwen, T.6
  • 35
    • 55749095406 scopus 로고    scopus 로고
    • Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase in Escherichia coli
    • Ruiz N, Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase in Escherichia coli. Proc Natl Acad Sci U S A. 2008;105(40):15553–7. doi: 10.1073/pnas.0808352105 18832143
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.40 , pp. 15553-15557
    • Ruiz, N.1
  • 36
    • 55749104427 scopus 로고    scopus 로고
    • Involvement of an essential gene, mviN, in murein synthesis in Escherichia coli
    • Inoue A, Murata Y, Takahashi H, Tsuji N, Fujisaki S, Kato J, Involvement of an essential gene, mviN, in murein synthesis in Escherichia coli. J Bacteriol. 2008;190(21):7298–301. doi: 10.1128/JB.00551-08 18708495
    • (2008) J Bacteriol , vol.190 , Issue.21 , pp. 7298-7301
    • Inoue, A.1    Murata, Y.2    Takahashi, H.3    Tsuji, N.4    Fujisaki, S.5    Kato, J.6
  • 37
    • 84899816263 scopus 로고    scopus 로고
    • A Burkholderia cenocepacia MurJ (MviN) homolog is essential for cell wall peptidoglycan synthesis and bacterial viability
    • Mohamed YF, Valvano MA, A Burkholderia cenocepacia MurJ (MviN) homolog is essential for cell wall peptidoglycan synthesis and bacterial viability. Glycobiology. 2014;24(6):564–76. doi: 10.1093/glycob/cwu025 24688094
    • (2014) Glycobiology , vol.24 , Issue.6 , pp. 564-576
    • Mohamed, Y.F.1    Valvano, M.A.2
  • 38
    • 84885459056 scopus 로고    scopus 로고
    • Structure-function analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coli
    • Butler EK, Davis RM, Bari V, Nicholson PA, Ruiz N, Structure-function analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coli. J Bacteriol. 2013;195(20):4639–49. doi: 10.1128/JB.00731-13 23935042
    • (2013) J Bacteriol , vol.195 , Issue.20 , pp. 4639-4649
    • Butler, E.K.1    Davis, R.M.2    Bari, V.3    Nicholson, P.A.4    Ruiz, N.5
  • 39
    • 84910011192 scopus 로고    scopus 로고
    • Charge requirements of lipid II flippase activity in Escherichia coli
    • Butler EK, Tan WB, Joseph H, Ruiz N, Charge requirements of lipid II flippase activity in Escherichia coli. J Bacteriol. 2014;196(23):4111–9. doi: 10.1128/JB.02172-14 25225268
    • (2014) J Bacteriol , vol.196 , Issue.23 , pp. 4111-4119
    • Butler, E.K.1    Tan, W.B.2    Joseph, H.3    Ruiz, N.4
  • 40
    • 84904097466 scopus 로고    scopus 로고
    • Bacterial cell wall. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis
    • Sham LT, Butler EK, Lebar MD, Kahne D, Bernhardt TG, Ruiz N, Bacterial cell wall. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis. Science. 2014;345(6193):220–2. doi: 10.1126/science.1254522 25013077
    • (2014) Science , vol.345 , Issue.6193 , pp. 220-222
    • Sham, L.T.1    Butler, E.K.2    Lebar, M.D.3    Kahne, D.4    Bernhardt, T.G.5    Ruiz, N.6
  • 41
    • 70349101331 scopus 로고    scopus 로고
    • Bacillus subtilis homologs of MviN (MurJ), the putative Escherichia coli lipid II flippase, are not essential for growth
    • Fay A, Dworkin J, Bacillus subtilis homologs of MviN (MurJ), the putative Escherichia coli lipid II flippase, are not essential for growth. J Bacteriol. 2009;191(19):6020–8. doi: 10.1128/JB.00605-09 19666716
    • (2009) J Bacteriol , vol.191 , Issue.19 , pp. 6020-6028
    • Fay, A.1    Dworkin, J.2
  • 42
    • 84929428246 scopus 로고    scopus 로고
    • MurJ and a novel lipid II flippase are required for cell wall biogenesis in Bacillus subtilis
    • Meeske AJ, Sham LT, Kimsey H, Koo BM, Gross CA, Bernhardt TG, et al. MurJ and a novel lipid II flippase are required for cell wall biogenesis in Bacillus subtilis. Proc Natl Acad Sci U S A. 2015; 112(20):6437–42. doi: 10.1073/pnas.1504967112 25918422
    • (2015) Proc Natl Acad Sci U S A , vol.112 , Issue.20 , pp. 6437-6442
    • Meeske, A.J.1    Sham, L.T.2    Kimsey, H.3    Koo, B.M.4    Gross, C.A.5    Bernhardt, T.G.6
  • 43
    • 84927164321 scopus 로고    scopus 로고
    • Lipid-linked cell wall precursors regulate membrane association of bacterial actin MreB
    • Schirner K, Eun YJ, Dion M, Luo Y, Helmann JD, Garner EC, et al. Lipid-linked cell wall precursors regulate membrane association of bacterial actin MreB. Nat Chem Biol. 2015;11(1):38–45. doi: 10.1038/nchembio.1689 25402772
    • (2015) Nat Chem Biol , vol.11 , Issue.1 , pp. 38-45
    • Schirner, K.1    Eun, Y.J.2    Dion, M.3    Luo, Y.4    Helmann, J.D.5    Garner, E.C.6
  • 44
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis
    • Garner EC, Bernard R, Wang W, Zhuang X, Rudner DZ, Mitchison T, Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis. Science. 2011;333(6039):222–5. doi: 10.1126/science.1203285 21636745
    • (2011) Science , vol.333 , Issue.6039 , pp. 222-225
    • Garner, E.C.1    Bernard, R.2    Wang, W.3    Zhuang, X.4    Rudner, D.Z.5    Mitchison, T.6
  • 46
    • 84882321076 scopus 로고    scopus 로고
    • Reducing the Level of Undecaprenyl Pyrophosphate Synthase Has Complex Effects on Susceptibility to Cell Wall Antibiotics
    • Lee YH, Helmann JD, Reducing the Level of Undecaprenyl Pyrophosphate Synthase Has Complex Effects on Susceptibility to Cell Wall Antibiotics. Antimicrob Agents Chemother. 2013;57(9):4267–75.
    • (2013) Antimicrob Agents Chemother , vol.57 , Issue.9 , pp. 4267-4275
    • Lee, Y.H.1    Helmann, J.D.2
  • 47
    • 80755143318 scopus 로고    scopus 로고
    • Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan
    • Muchova K, Wilkinson AJ, Barak I, Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan. FEMS Microbiol Lett. 2011;325(1):92–8. doi: 10.1111/j.1574-6968.2011.02417.x 22092867
    • (2011) FEMS Microbiol Lett , vol.325 , Issue.1 , pp. 92-98
    • Muchova, K.1    Wilkinson, A.J.2    Barak, I.3
  • 48
    • 84896797385 scopus 로고    scopus 로고
    • The actin homologue MreB organizes the bacterial cell membrane
    • Strahl H, Burmann F, Hamoen LW, The actin homologue MreB organizes the bacterial cell membrane. Nat Commun. 2014;5:3442. doi: 10.1038/ncomms4442 24603761
    • (2014) Nat Commun , vol.5 , pp. 3442
    • Strahl, H.1    Burmann, F.2    Hamoen, L.W.3
  • 49
    • 33646598425 scopus 로고    scopus 로고
    • Size and orientation of the lipid II headgroup as revealed by AFM imaging
    • Ganchev DN, Hasper HE, Breukink E, de Kruijff B, Size and orientation of the lipid II headgroup as revealed by AFM imaging. Biochemistry. 2006;45(19):6195–202. 16681392
    • (2006) Biochemistry , vol.45 , Issue.19 , pp. 6195-6202
    • Ganchev, D.N.1    Hasper, H.E.2    Breukink, E.3    de Kruijff, B.4
  • 50
    • 67650708496 scopus 로고    scopus 로고
    • Characterization and subcellular localization of a bacterial flotillin homologue
    • Donovan C, Bramkamp M, Characterization and subcellular localization of a bacterial flotillin homologue. Microbiology. 2009;155:1786–99. doi: 10.1099/mic.0.025312-0 19383680
    • (2009) Microbiology , vol.155 , pp. 1786-1799
    • Donovan, C.1    Bramkamp, M.2
  • 51
    • 77956292192 scopus 로고    scopus 로고
    • Functional microdomains in bacterial membranes
    • Lopez D, Kolter R, Functional microdomains in bacterial membranes. Genes Dev. 2010;24(17):1893–902. doi: 10.1101/gad.1945010 20713508
    • (2010) Genes Dev , vol.24 , Issue.17 , pp. 1893-1902
    • Lopez, D.1    Kolter, R.2
  • 52
    • 84879030282 scopus 로고    scopus 로고
    • Flotillins functionally organize the bacterial membrane
    • Bach JN, Bramkamp M, Flotillins functionally organize the bacterial membrane. Mol Microbiol. 2013;88(6):1205–17. doi: 10.1111/mmi.12252 23651456
    • (2013) Mol Microbiol , vol.88 , Issue.6 , pp. 1205-1217
    • Bach, J.N.1    Bramkamp, M.2
  • 53
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell
    • Daniel RA, Errington J, Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell. 2003;113:767–76. 12809607
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 54
    • 84902158114 scopus 로고    scopus 로고
    • Reconstruction of mreB expression in Staphylococcus aureus via a collection of new integrative plasmids
    • Yepes A, Koch G, Waldvogel A, Garcia-Betancur JC, Lopez D, Reconstruction of mreB expression in Staphylococcus aureus via a collection of new integrative plasmids. Appl Environ Microbiol. 2014;80(13):3868–78. doi: 10.1128/AEM.00759-14 24747904
    • (2014) Appl Environ Microbiol , vol.80 , Issue.13 , pp. 3868-3878
    • Yepes, A.1    Koch, G.2    Waldvogel, A.3    Garcia-Betancur, J.C.4    Lopez, D.5
  • 55
    • 22944489133 scopus 로고    scopus 로고
    • Bacillus subtilis actin-like protein MreB influences the positioning of the replication machinery and requires membrane proteins MreC/D and other actin-like proteins for proper localization
    • Defeu Soufo HJ, Graumann PL, Bacillus subtilis actin-like protein MreB influences the positioning of the replication machinery and requires membrane proteins MreC/D and other actin-like proteins for proper localization. BMC Cell Biol. 2005;6(1):10. 15745453
    • (2005) BMC Cell Biol , vol.6 , Issue.1 , pp. 10
    • Defeu, S.H.J.1    Graumann, P.L.2
  • 56
    • 77951608842 scopus 로고    scopus 로고
    • Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD
    • White CL, Kitich A, Gober JW, Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD. Molecular Microbiology. 2010;76(3):616–33. doi: 10.1111/j.1365-2958.2010.07108.x 20233306
    • (2010) Molecular Microbiology , vol.76 , Issue.3 , pp. 616-633
    • White, C.L.1    Kitich, A.2    Gober, J.W.3
  • 58
    • 59649113418 scopus 로고    scopus 로고
    • RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli
    • Bendezu FO, Hale CA, Bernhardt TG, de Boer PA, RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli. EMBO J. 2009;28(3):193–204. doi: 10.1038/emboj.2008.264 19078962
    • (2009) EMBO J , vol.28 , Issue.3 , pp. 193-204
    • Bendezu, F.O.1    Hale, C.A.2    Bernhardt, T.G.3    de Boer, P.A.4
  • 59
    • 57149120088 scopus 로고    scopus 로고
    • Determination of bacterial rod shape by a novel cytoskeletal membrane protein
    • Shiomi D, Sakai M, Niki H, Determination of bacterial rod shape by a novel cytoskeletal membrane protein. EMBO J. 2008;27:3081–91. doi: 10.1038/emboj.2008.234 19008860
    • (2008) EMBO J , vol.27 , pp. 3081-3091
    • Shiomi, D.1    Sakai, M.2    Niki, H.3
  • 61
    • 79960913936 scopus 로고    scopus 로고
    • Direct membrane binding by bacterial actin MreB
    • Salje J, van den Ent F, de Boer P, Lowe J, Direct membrane binding by bacterial actin MreB. Mol Cell. 2011;43(3):478–87. doi: 10.1016/j.molcel.2011.07.008 21816350
    • (2011) Mol Cell , vol.43 , Issue.3 , pp. 478-487
    • Salje, J.1    van den Ent, F.2    de Boer, P.3    Lowe, J.4
  • 62
    • 84900506450 scopus 로고    scopus 로고
    • Bacterial actin MreB forms antiparallel double filaments
    • van den Ent F, Izore T, Bharat TA, Johnson CM, Lowe J, Bacterial actin MreB forms antiparallel double filaments. eLife. 2014;3:e02634. doi: 10.7554/eLife.02634 24843005
    • (2014) eLife , vol.3 , pp. e02634
    • van den Ent, F.1    Izore, T.2    Bharat, T.A.3    Johnson, C.M.4    Lowe, J.5
  • 63
    • 84859579073 scopus 로고    scopus 로고
    • Assembly of MreB filaments on liposome membranes: a synthetic biology approach
    • Maeda YT, Nakadai T, Shin J, Uryu K, Noireaux V, Libchaber A, Assembly of MreB filaments on liposome membranes: a synthetic biology approach. ACS synthetic biology. 2012;1(2):53–9. doi: 10.1021/sb200003v 23651045
    • (2012) ACS synthetic biology , vol.1 , Issue.2 , pp. 53-59
    • Maeda, Y.T.1    Nakadai, T.2    Shin, J.3    Uryu, K.4    Noireaux, V.5    Libchaber, A.6
  • 64
    • 84888203647 scopus 로고    scopus 로고
    • Do the divisome and elongasome share a common evolutionary past?
    • Szwedziak P, Lowe J, Do the divisome and elongasome share a common evolutionary past? Curr Opin Microbiol. 2013;16(6):745–51. doi: 10.1016/j.mib.2013.09.003 24094808
    • (2013) Curr Opin Microbiol , vol.16 , Issue.6 , pp. 745-751
    • Szwedziak, P.1    Lowe, J.2
  • 65
    • 29144477176 scopus 로고    scopus 로고
    • Bacterial cell wall synthesis: new insights from localization studies
    • Scheffers DJ, Pinho MG, Bacterial cell wall synthesis: new insights from localization studies. Microb Mol Biol Rev. 2005;69(4):585–607.
    • (2005) Microb Mol Biol Rev , vol.69 , Issue.4 , pp. 585-607
    • Scheffers, D.J.1    Pinho, M.G.2
  • 66
    • 13444259776 scopus 로고    scopus 로고
    • Recruitment of penicillin-binding protein PBP2 to the division site of Staphylococcus aureus is dependent on its transpeptidation substrates
    • Pinho MG, Errington J, Recruitment of penicillin-binding protein PBP2 to the division site of Staphylococcus aureus is dependent on its transpeptidation substrates. Mol Microbiol. 2005;55(3):799–807. 15661005
    • (2005) Mol Microbiol , vol.55 , Issue.3 , pp. 799-807
    • Pinho, M.G.1    Errington, J.2
  • 67
    • 1642442760 scopus 로고    scopus 로고
    • The carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae
    • Morlot C, Noirclerc-Savoye M, Zapun A, Dideberg O, Vernet T, The carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae. Mol Microbiol. 2004;51(6):1641–8. 15009891
    • (2004) Mol Microbiol , vol.51 , Issue.6 , pp. 1641-1648
    • Morlot, C.1    Noirclerc-Savoye, M.2    Zapun, A.3    Dideberg, O.4    Vernet, T.5
  • 68
    • 79955543481 scopus 로고    scopus 로고
    • Characterization of mutants deficient in the L,D-carboxypeptidase (DacB) and WalRK (VicRK) regulon, involved in peptidoglycan maturation of Streptococcus pneumoniae serotype 2 strain D39
    • Barendt SM, Sham LT, Winkler ME, Characterization of mutants deficient in the L,D-carboxypeptidase (DacB) and WalRK (VicRK) regulon, involved in peptidoglycan maturation of Streptococcus pneumoniae serotype 2 strain D39. J Bacteriol. 2011;193(9):2290–300. doi: 10.1128/JB.01555-10 21378199
    • (2011) J Bacteriol , vol.193 , Issue.9 , pp. 2290-2300
    • Barendt, S.M.1    Sham, L.T.2    Winkler, M.E.3
  • 69
    • 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, Karczmarek A, Verheul J, Piette A, Wilkin JM, Werth N, et al. Septal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment. Mol Microbiol. 2010;77(2):300–23. doi: 10.1111/j.1365-2958.2010.07205.x 20545860
    • (2010) Mol Microbiol , vol.77 , Issue.2 , pp. 300-323
    • Potluri, L.1    Karczmarek, A.2    Verheul, J.3    Piette, A.4    Wilkin, J.M.5    Werth, N.6
  • 70
    • 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, Localization of PBP3 in Caulobacter crescentus is highly dynamic and largely relies on its functional transpeptidase domain. Mol Microbiol. 2008;70(3):634–51. doi: 10.1111/j.1365-2958.2008.06432.x 18786147
    • (2008) Mol Microbiol , vol.70 , Issue.3 , pp. 634-651
    • Costa, T.1    Priyadarshini, R.2    Jacobs-Wagner, C.3
  • 71
    • 84888881225 scopus 로고    scopus 로고
    • The localization of key Bacillus subtilis penicillin binding proteins during cell growth is determined by substrate availability
    • Lages MC, Beilharz K, Morales Angeles D, Veening JW, Scheffers DJ, The localization of key Bacillus subtilis penicillin binding proteins during cell growth is determined by substrate availability. Env Microbiol. 2013;15(12):3272–81.
    • (2013) Env Microbiol , vol.15 , Issue.12 , pp. 3272-3281
    • Lages, M.C.1    Beilharz, K.2    Morales Angeles, D.3    Veening, J.W.4    Scheffers, D.J.5


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