메뉴 건너뛰기




Volumn 70, Issue 2, 2008, Pages 297-310

The major and minor wall teichoic acids prevent the sidewall localization of vegetative DL-endopeptidase LytF in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; MREB PROTEIN; PEPTIDOGLYCAN; PROTEIN LYTF; PROTEINASE; TEICHOIC ACID; UNCLASSIFIED DRUG;

EID: 52649134462     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2008.06397.x     Document Type: Article
Times cited : (56)

References (52)
  • 1
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos, C. Spizizen, J. (1961) Requirements for transformation in Bacillus subtilis. J Bacteriol 81 : 741 746.
    • (1961) J Bacteriol , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 2
    • 8744309111 scopus 로고    scopus 로고
    • New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, Gram-positive bacteria
    • Arnaud, M., Chastanet, A. Débarbouillé, M. (2004) New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, Gram-positive bacteria. Appl Environ Microbiol 70 : 6887 6891.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 6887-6891
    • Arnaud, M.1    Chastanet, A.2    Débarbouillé, M.3
  • 3
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)
    • Bateman, A. Bycroft, M. (2000) The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J Mol Biol 299 : 1113 1119.
    • (2000) J Mol Biol , vol.299 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 4
    • 34250632446 scopus 로고    scopus 로고
    • The essential YycFG two-component system controls cell wall metabolism in Bacillus subtilis
    • Bisicchia, P., Noone, D., Lioliou, E., Howell, A., Quigley, S., Jensen, T., et al. (2007) The essential YycFG two-component system controls cell wall metabolism in Bacillus subtilis. Mol Microbiol 65 : 180 200.
    • (2007) Mol Microbiol , vol.65 , pp. 180-200
    • Bisicchia, P.1    Noone, D.2    Lioliou, E.3    Howell, A.4    Quigley, S.5    Jensen, T.6
  • 6
    • 42549103340 scopus 로고    scopus 로고
    • LysM, a widely distributed protein motif for binding to (peptido)glycans
    • Buist, G., Steen, A., Kok, J. Kuipers, O.P. (2008) LysM, a widely distributed protein motif for binding to (peptido)glycans. Mol Microbiol 68 : 838 847.
    • (2008) Mol Microbiol , vol.68 , pp. 838-847
    • Buist, G.1    Steen, A.2    Kok, J.3    Kuipers, O.P.4
  • 7
    • 0037237123 scopus 로고    scopus 로고
    • The bacterial cytoskeleton. in vivo dynamics of the actin-like protein Mbl of Bacillus subtilis
    • Carballido-López, R. Errington, J. (2003) The bacterial cytoskeleton. In vivo dynamics of the actin-like protein Mbl of Bacillus subtilis. Dev Cell 4 : 19 28.
    • (2003) Dev Cell , vol.4 , pp. 19-28
    • Carballido-López, R.1    Errington, J.2
  • 8
    • 33747837700 scopus 로고    scopus 로고
    • Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE
    • Carballido-López, R., Formstone, A., Li, Y., Ehrlich, S.D., Noirot, P. Errington, J. (2006) Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE. Dev Cell 11 : 399 409.
    • (2006) Dev Cell , vol.11 , pp. 399-409
    • Carballido-López, R.1    Formstone, A.2    Li, Y.3    Ehrlich, S.D.4    Noirot, P.5    Errington, J.6
  • 9
    • 0344393481 scopus 로고    scopus 로고
    • Identification and characterization of a peptidoglycan hydrolase, MurA, of Listeria monocytogenes, a muramidase needed for cell separation
    • Carroll, S.A., Hain, T., Technow, U., Darji, A., Pashalidis, P., Joseph, S.W. Chakraborty, T. (2003) Identification and characterization of a peptidoglycan hydrolase, MurA, of Listeria monocytogenes, a muramidase needed for cell separation. J Bacteriol 185 : 6801 6808.
    • (2003) J Bacteriol , vol.185 , pp. 6801-6808
    • Carroll, S.A.1    Hain, T.2    Technow, U.3    Darji, A.4    Pashalidis, P.5    Joseph, S.W.6    Chakraborty, T.7
  • 10
    • 0024605246 scopus 로고
    • Cell wall assembly in Bacillus subtilis: Partial conservation of polar wall material and effect of growth conditions on the pattern of incorporation of new material at the polar caps
    • Clarke-Sturman, A.J., Archibald, A.R., Hancock, I.C., Harwood, C.R., Merad, T. Hobot, J.A. (1989) Cell wall assembly in Bacillus subtilis: partial conservation of polar wall material and effect of growth conditions on the pattern of incorporation of new material at the polar caps. J Gen Microbiol 135 : 657 665.
    • (1989) J Gen Microbiol , vol.135 , pp. 657-665
    • Clarke-Sturman, A.J.1    Archibald, A.R.2    Hancock, I.C.3    Harwood, C.R.4    Merad, T.5    Hobot, J.A.6
  • 11
    • 33751585943 scopus 로고    scopus 로고
    • Wall teichoic acid polymers are dispensable for cell viability in Bacillus subtilis
    • D'Elia, M.A., Millar, K.E., Beveridge, T.J. Brown, E.D. (2006) Wall teichoic acid polymers are dispensable for cell viability in Bacillus subtilis. J Bacteriol 188 : 8313 8316.
    • (2006) J Bacteriol , vol.188 , pp. 8313-8316
    • D'Elia, M.A.1    Millar, K.E.2    Beveridge, T.J.3    Brown, E.D.4
  • 12
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: Two distinct ways to make a rod-shaped cell
    • Daniel, R.A. 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
  • 13
    • 0028961002 scopus 로고
    • The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus
    • DeHart, H.P., Heath, H.E., Heath, L.S., LeBlanc, P.A. Sloan, G.L. (1995) The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus. Appl Environ Microbiol 61 : 1475 1479.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1475-1479
    • Dehart, H.P.1    Heath, H.E.2    Heath, L.S.3    Leblanc, P.A.4    Sloan, G.L.5
  • 14
    • 0033735885 scopus 로고    scopus 로고
    • The CtsR regulator of stress response is active as a dimmer and specifically degraded in vivo at 37°C
    • Derré, I., Rapoport, G. Msadek, T. (2000) The CtsR regulator of stress response is active as a dimmer and specifically degraded in vivo at 37°C. Mol Microbiol 38 : 335 347.
    • (2000) Mol Microbiol , vol.38 , pp. 335-347
    • Derré, I.1    Rapoport, G.2    Msadek, T.3
  • 15
    • 0002327866 scopus 로고    scopus 로고
    • Cell division during growth and sporulation
    • In. Sonenshein, A.L., Losick, R. Hoch, J.A. (eds). Washington, DC: American Society for Microbiology Press, pp.
    • Errington, J. Daniel, R.A. (2002) Cell division during growth and sporulation. In Bacillus subtilis and Its Closest Relatives: From Genes to Cells. Sonenshein, A.L., Losick, R. Hoch, J.A. (eds). Washington, DC : American Society for Microbiology Press, pp. 97 109.
    • (2002) Bacillus Subtilis and Its Closest Relatives: From Genes to Cells. , pp. 97-109
    • Errington, J.1    Daniel, R.A.2
  • 16
    • 0025802670 scopus 로고
    • Genetic and biochemical characterization of Bacillus subtilis 168 mutants specifically blocked in the synthesis of the teichoic acid poly(3-O-β-d- glucopyranosyl-N-acetylgalactosamine 1-phospate): GneA, a new locus, is associated with UDP-N-acetylglucosamine 4-epimerase activity
    • Estrela, A.I., Pooley, H.M., de Lencastre, H. Karamata, D. (1991) Genetic and biochemical characterization of Bacillus subtilis 168 mutants specifically blocked in the synthesis of the teichoic acid poly(3-O-β-d-glucopyranosyl- N-acetylgalactosamine 1-phospate): gneA, a new locus, is associated with UDP-N-acetylglucosamine 4-epimerase activity. J Gen Microbiol 137 : 943 950.
    • (1991) J Gen Microbiol , vol.137 , pp. 943-950
    • Estrela, A.I.1    Pooley, H.M.2    De Lencastre, H.3    Karamata, D.4
  • 17
    • 0017104106 scopus 로고
    • Autolytic enzyme-deficient mutants of Bacillus subtilis 168
    • Fein, J.E. Rogers, H.J. (1976) Autolytic enzyme-deficient mutants of Bacillus subtilis 168. J Bacteriol 127 : 1427 1442.
    • (1976) J Bacteriol , vol.127 , pp. 1427-1442
    • Fein, J.E.1    Rogers, H.J.2
  • 18
    • 15944399775 scopus 로고    scopus 로고
    • A magnesium-dependent mreB null mutant: Implications for the role of mreB in Bacillus subtilis
    • Formstone, A. Errington, J. (2005) A magnesium-dependent mreB null mutant: implications for the role of mreB in Bacillus subtilis. Mol Microbiol 55 : 1646 1657.
    • (2005) Mol Microbiol , vol.55 , pp. 1646-1657
    • Formstone, A.1    Errington, J.2
  • 19
    • 39749184735 scopus 로고    scopus 로고
    • Localization and interactions of teichoic acid synthetic enzymes in Bacillus subtilis
    • Formstone, A., Carballido-López, R., Noirot, P., Errington, J. Scheffers, D.J. (2008) Localization and interactions of teichoic acid synthetic enzymes in Bacillus subtilis. J Bacteriol 190 : 1812 1821.
    • (2008) J Bacteriol , vol.190 , pp. 1812-1821
    • Formstone, A.1    Carballido-López, R.2    Noirot, P.3    Errington, J.4    Scheffers, D.J.5
  • 20
    • 0001904527 scopus 로고    scopus 로고
    • Structure and synthesis of cell wall, spore cortex, teichoic acids, S-layers, and capsules
    • In. Sonenshein, A.L., Losick, R. Hoch, J.A. (eds). Washington, DC: American Society for Microbiology Press, pp.
    • Foster, S.J. Popham, D.L. (2002) Structure and synthesis of cell wall, spore cortex, teichoic acids, S-layers, and capsules. In Bacillus subtilis and Its Closest Relatives: From Genes to Cells. Sonenshein, A.L., Losick, R. Hoch, J.A. (eds). Washington, DC : American Society for Microbiology Press, pp. 21 41.
    • (2002) Bacillus Subtilis and Its Closest Relatives: From Genes to Cells. , pp. 21-41
    • Foster, S.J.1    Popham, D.L.2
  • 21
    • 33745252174 scopus 로고    scopus 로고
    • Poly(glucosyl-N-acetylgalactosamine 1-phosphate), a wall teichoic acid of Bacillus subtilis 168: Its biosynthetic pathway and mode of attachment to peptidoglycan
    • Freymond, P., Lazarevic, V., Soldo, B. Karamata, D. (2006) Poly(glucosyl-N-acetylgalactosamine 1-phosphate), a wall teichoic acid of Bacillus subtilis 168: its biosynthetic pathway and mode of attachment to peptidoglycan. Microbiology 152 : 1709 1718.
    • (2006) Microbiology , vol.152 , pp. 1709-1718
    • Freymond, P.1    Lazarevic, V.2    Soldo, B.3    Karamata, D.4
  • 22
    • 33746648727 scopus 로고    scopus 로고
    • A new d,l-endopeptidase gene product, YojL (renamed CwlS), plays a role in cell separation with LytE and LytF in Bacillus subtilis
    • Fukushima, T., Afkham, A., Kurosawa, S., Tanabe, T., Yamamoto, H. Sekiguchi, J. (2006) A new d,l-endopeptidase gene product, YojL (renamed CwlS), plays a role in cell separation with LytE and LytF in Bacillus subtilis. J Bacteriol 188 : 5541 5550.
    • (2006) J Bacteriol , vol.188 , pp. 5541-5550
    • Fukushima, T.1    Afkham, A.2    Kurosawa, S.3    Tanabe, T.4    Yamamoto, H.5    Sekiguchi, J.6
  • 23
    • 0023990265 scopus 로고
    • Cloning, sequencing, and disruption of the Bacillus subtilis sigma 28 gene
    • Helmann, J.D., Marquez, L.M. Chamberlin, M.J. (1988) Cloning, sequencing, and disruption of the Bacillus subtilis sigma 28 gene. J Bacteriol 170 : 1568 1574.
    • (1988) J Bacteriol , vol.170 , pp. 1568-1574
    • Helmann, J.D.1    Marquez, L.M.2    Chamberlin, M.J.3
  • 24
    • 0031978461 scopus 로고    scopus 로고
    • Regulation of a new cell wall hydrolase gene, cwlF, which affects cell separation in Bacillus subtilis
    • Ishikawa, S., Hara, Y., Ohnishi, R. Sekiguchi, J. (1998) Regulation of a new cell wall hydrolase gene, cwlF, which affects cell separation in Bacillus subtilis. J Bacteriol 180 : 2549 2555.
    • (1998) J Bacteriol , vol.180 , pp. 2549-2555
    • Ishikawa, S.1    Hara, Y.2    Ohnishi, R.3    Sekiguchi, J.4
  • 25
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • Jones, L.J., Carballido-López, R. Errington, J. (2001) Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104 : 913 922.
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-López, R.2    Errington, J.3
  • 26
    • 27944473534 scopus 로고    scopus 로고
    • Identification and molecular characterization of an N-acetylmuramoyl-l- alanine amidase Sle1 involved in cell separation of Staphylococcus aureus
    • Kajimura, J., Fujiwara, T., Yamada, S., Suzawa, Y., Nishida, T., Oyamada, Y., et al. (2005) Identification and molecular characterization of an N-acetylmuramoyl-l-alanine amidase Sle1 involved in cell separation of Staphylococcus aureus. Mol Microbiol 58 : 1087 1101.
    • (2005) Mol Microbiol , vol.58 , pp. 1087-1101
    • Kajimura, J.1    Fujiwara, T.2    Yamada, S.3    Suzawa, Y.4    Nishida, T.5    Oyamada, Y.6
  • 28
    • 0025011966 scopus 로고
    • Cloning, sequencing and genetic mapping of a Bacillus subtilis cell wall hydrolase gene
    • Kuroda, A. Sekiguchi, J. (1990) Cloning, sequencing and genetic mapping of a Bacillus subtilis cell wall hydrolase gene. J Gen Microbiol 136 : 2209 2216.
    • (1990) J Gen Microbiol , vol.136 , pp. 2209-2216
    • Kuroda, A.1    Sekiguchi, J.2
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 : 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0029035870 scopus 로고
    • The tagGH operon of Bacillus subtilis 168 encodes a two-component ABC transporter involved in the metabolism of two wall teichoic acids
    • Lazarevic, V. Karamata, D. (1995) The tagGH operon of Bacillus subtilis 168 encodes a two-component ABC transporter involved in the metabolism of two wall teichoic acids. Mol Microbiol 16 : 345 355.
    • (1995) Mol Microbiol , vol.16 , pp. 345-355
    • Lazarevic, V.1    Karamata, D.2
  • 31
    • 0005763375 scopus 로고    scopus 로고
    • Teichoic and teichuronic acids from Gram-positive bacteria
    • In. Vandamme, E.J., de Baets, S. Steinbüchel, A. (eds). Weinheim: Wiley. pp.
    • Lazarevic, V., Pooley, H.M., Mauël, C. Karamata, D. (2002) Teichoic and teichuronic acids from Gram-positive bacteria. In Biopolymers, Vol. 5, Polysaccharides I: Polysaccharides from Prokaryotes. Vandamme, E.J., de Baets, S. Steinbüchel, A. (eds). Weinheim : Wiley-VCH, pp. 465 492.
    • (2002) Biopolymers , vol.51 , pp. 465-492
    • Lazarevic, V.1    Pooley, H.M.2    Mauël, C.3    Karamata, D.4
  • 32
    • 0142104972 scopus 로고    scopus 로고
    • A receptor kinase gene of the LysM type is involved in legume perception of rhizobial signals
    • Madsen, E.B., Madsen, L.H., Radutoiu, S., Olbryt, M., Rakwalska, M., Szczyglowski, K., et al. (2003) A receptor kinase gene of the LysM type is involved in legume perception of rhizobial signals. Nature 425 : 637 640.
    • (2003) Nature , vol.425 , pp. 637-640
    • Madsen, E.B.1    Madsen, L.H.2    Radutoiu, S.3    Olbryt, M.4    Rakwalska, M.5    Szczyglowski, K.6
  • 33
  • 35
    • 0024544714 scopus 로고
    • Cell wall assembly in Bacillus subtilis: Visualization of old and new wall material by electron microscopic examination of samples stained selectively for teichoic acid and teichuronic acid
    • Merad, T., Archibald, A.R., Hancock, I.C., Harwood, C.R. Hobot, J.A. (1989) Cell wall assembly in Bacillus subtilis: visualization of old and new wall material by electron microscopic examination of samples stained selectively for teichoic acid and teichuronic acid. J General Microbiol 135 : 645 655.
    • (1989) J General Microbiol , vol.135 , pp. 645-655
    • Merad, T.1    Archibald, A.R.2    Hancock, I.C.3    Harwood, C.R.4    Hobot, J.A.5
  • 36
    • 0021191674 scopus 로고
    • Insertion and fate of cell wall in Bacillus subtilis
    • Mobley, H.L., Koch, A.L., Doyle, R.J. Streips, U.N. (1984) Insertion and fate of cell wall in Bacillus subtilis. J Bacteriol 158 : 169 179.
    • (1984) J Bacteriol , vol.158 , pp. 169-179
    • Mobley, H.L.1    Koch, A.L.2    Doyle, R.J.3    Streips, U.N.4
  • 37
    • 0032964960 scopus 로고    scopus 로고
    • Peptidoglycan hydrolase LytF plays a role in cell separation with LytE during vegetative growth of Bacillus subtilis
    • Ohnishi, R., Ishikawa, S. Sekiguchi, J. (1999) Peptidoglycan hydrolase LytF plays a role in cell separation with LytE during vegetative growth of Bacillus subtilis. J Bacteriol 181 : 3178 3184.
    • (1999) J Bacteriol , vol.181 , pp. 3178-3184
    • Ohnishi, R.1    Ishikawa, S.2    Sekiguchi, J.3
  • 38
    • 0028072297 scopus 로고
    • Changes in wall teichoic acid during the rod-sphere transition of Bacillus subtilis 168
    • Pollack, J.H. Neuhaus, F.C. (1994) Changes in wall teichoic acid during the rod-sphere transition of Bacillus subtilis 168. J Bacteriol 176 : 7252 7259.
    • (1994) J Bacteriol , vol.176 , pp. 7252-7259
    • Pollack, J.H.1    Neuhaus, F.C.2
  • 39
    • 0026584777 scopus 로고
    • CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase, which is involved in the synthesis of the major wall teichoic acid in Bacillus subtilis 168, is encoded by tagF (rodC)
    • Pooley, H.M., Abellan, F.X. Karamata, D. (1992) CDP-glycerol: poly(glycerophosphate) glycerophosphotransferase, which is involved in the synthesis of the major wall teichoic acid in Bacillus subtilis 168, is encoded by tagF (rodC). J Bacteriol 174 : 646 649.
    • (1992) J Bacteriol , vol.174 , pp. 646-649
    • Pooley, H.M.1    Abellan, F.X.2    Karamata, D.3
  • 40
    • 0142041483 scopus 로고    scopus 로고
    • Plant recognition of symbiotic bacteria requires two LysM receptor-like kinases
    • Radutoiu, S., Madsen, L.H., Madsen, E.B., Felle, H.H., Umehara, Y., Gronlund, M., et al. (2003) Plant recognition of symbiotic bacteria requires two LysM receptor-like kinases. Nature 425 : 585 592.
    • (2003) Nature , vol.425 , pp. 585-592
    • Radutoiu, S.1    Madsen, L.H.2    Madsen, E.B.3    Felle, H.H.4    Umehara, Y.5    Gronlund, M.6
  • 41
    • 0028784908 scopus 로고
    • Analysis of the minor autolysins of Bacillus subtilis during vegetative growth by zymography
    • Rashid, M.H., Sato, N. Sekiguchi, J. (1995) Analysis of the minor autolysins of Bacillus subtilis during vegetative growth by zymography. FEMS Microbiol Lett 132 : 131 137.
    • (1995) FEMS Microbiol Lett , vol.132 , pp. 131-137
    • Rashid, M.H.1    Sato, N.2    Sekiguchi, J.3
  • 43
    • 0027787618 scopus 로고
    • Sequencing and analysis of the divergon comprising gtaB, the structural gene of UDP-glucose pyrophosphorylase of Bacillus subtilis 168
    • Soldo, B., Lazarevic, V., Margot, P. Karamata, D. (1993) Sequencing and analysis of the divergon comprising gtaB, the structural gene of UDP-glucose pyrophosphorylase of Bacillus subtilis 168. J Gen Microbiol 139 : 3185 3195.
    • (1993) J Gen Microbiol , vol.139 , pp. 3185-3195
    • Soldo, B.1    Lazarevic, V.2    Margot, P.3    Karamata, D.4
  • 44
    • 0032929191 scopus 로고    scopus 로고
    • Teichuronic acid operon of Bacillus subtilis 168
    • Soldo, B., Lazarevic, V., Pagni, M. Karamata, D. (1999) Teichuronic acid operon of Bacillus subtilis 168. Mol Microbiol 31 : 795 805.
    • (1999) Mol Microbiol , vol.31 , pp. 795-805
    • Soldo, B.1    Lazarevic, V.2    Pagni, M.3    Karamata, D.4
  • 45
    • 0036066470 scopus 로고    scopus 로고
    • TagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168
    • Soldo, B., Lazarevic, V. Karamata, D. (2002) tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168. Microbiology 148 : 2079 2087.
    • (2002) Microbiology , vol.148 , pp. 2079-2087
    • Soldo, B.1    Lazarevic, V.2    Karamata, D.3
  • 46
    • 0037930133 scopus 로고    scopus 로고
    • Cell wall attachment of a widely distributed peptidoglycan binding domain is hindered by cell wall constituents
    • Steen, A., Buist, G., Leenhouts, K.J., El Khattabi, M., Grijpstra, F., Zomer, A.L., et al. (2003) Cell wall attachment of a widely distributed peptidoglycan binding domain is hindered by cell wall constituents. J Biol Chem 278 : 23874 23881.
    • (2003) J Biol Chem , vol.278 , pp. 23874-23881
    • Steen, A.1    Buist, G.2    Leenhouts, K.J.3    El Khattabi, M.4    Grijpstra, F.5    Zomer, A.L.6
  • 47
    • 20444471564 scopus 로고    scopus 로고
    • AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning
    • Steen, A., Buist, G., Horsburgh, G.J., Venema, G., Kuipers, O.P., Foster, S.J. Kok, J. (2005) AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning. FEBS J 272 : 2854 2868.
    • (2005) FEBS J , vol.272 , pp. 2854-2868
    • Steen, A.1    Buist, G.2    Horsburgh, G.J.3    Venema, G.4    Kuipers, O.P.5    Foster, S.J.6    Kok, J.7
  • 48
    • 33746639594 scopus 로고    scopus 로고
    • Imaging peptidoglycan biosynthesis in Bacillus subtilis with fluorescent antibiotics
    • Tiyanont, K., Doan, T., Lazarus, M.B., Fang, X., Rudner, D.Z. Walker, S. (2006) Imaging peptidoglycan biosynthesis in Bacillus subtilis with fluorescent antibiotics. Proc Natl Acad Sci USA 103 : 11033 11038.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11033-11038
    • Tiyanont, K.1    Doan, T.2    Lazarus, M.B.3    Fang, X.4    Rudner, D.Z.5    Walker, S.6
  • 49
    • 0031737309 scopus 로고    scopus 로고
    • A vector for systematic gene inactivation in Bacillus subtilis
    • Vagner, V., Dervyn, E. Ehrlich, D. (1998) A vector for systematic gene inactivation in Bacillus subtilis. Microbiology 144 : 3097 3104.
    • (1998) Microbiology , vol.144 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, D.3
  • 51
    • 0015237808 scopus 로고
    • Structure of the peptidoglycan from vegetative cell wall of Bacillus subtilis
    • Warth, A.D. Strominger, J.L. (1971) Structure of the peptidoglycan from vegetative cell wall of Bacillus subtilis. Biochemistry 10 : 4349 4358.
    • (1971) Biochemistry , vol.10 , pp. 4349-4358
    • Warth, A.D.1    Strominger, J.L.2
  • 52
    • 0242575014 scopus 로고    scopus 로고
    • Localization of the vegetative cell wall hydrases LytC, LytE, and LytF on the Bacillus subtilis cell surface and stability of these enzymes to cell wall-bound or extracellular proteases
    • Yamamoto, H., Kurosawa, S. Sekiguchi, J. (2003) Localization of the vegetative cell wall hydrases LytC, LytE, and LytF on the Bacillus subtilis cell surface and stability of these enzymes to cell wall-bound or extracellular proteases. J Bacteriol 185 : 6666 6677.
    • (2003) J Bacteriol , vol.185 , pp. 6666-6677
    • Yamamoto, H.1    Kurosawa, S.2    Sekiguchi, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.