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Volumn 186, Issue 4, 2004, Pages 1136-1146

The Bacillus subtilis Extracytoplasmic-Function σX Factor Regulates Modification of the Cell Envelope and Resistance to Cationic Antimicrobial Peptides

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; DEXTRO ALANINE; NISIN; PENICILLIN BINDING PROTEIN; SIGMA FACTOR; SIGMA X FACTOR; UNCLASSIFIED DRUG;

EID: 1142286470     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.4.1136-1146.2004     Document Type: Conference Paper
Times cited : (122)

References (60)
  • 4
    • 0030671325 scopus 로고    scopus 로고
    • SigX of Bacillus subtilis replaces the ECF sigma factor FecI of Escherichia coli and is inhibited by RsiX
    • Brutsche, S., and V. Braun. 1997. SigX of Bacillus subtilis replaces the ECF sigma factor FecI of Escherichia coli and is inhibited by RsiX. Mol. Gen. Genet. 256:416-425.
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 416-425
    • Brutsche, S.1    Braun, V.2
  • 5
    • 0031850630 scopus 로고    scopus 로고
    • Bacillus subtilis contains multiple fur homologues: Identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors
    • Bsat, N., A. Herbig, L. Casillas-Martinez, P. Setlow, and J. D. Helmann. 1998. Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors. Mol. Microbiol. 29:189-198.
    • (1998) Mol. Microbiol. , vol.29 , pp. 189-198
    • Bsat, N.1    Herbig, A.2    Casillas-Martinez, L.3    Setlow, P.4    Helmann, J.D.5
  • 7
    • 0036844128 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis bcrC bacitracin resistance gene by two extracytoplasmic function sigma factors
    • Cao, M., and J. D. Helmann. 2002. Regulation of the Bacillus subtilis bcrC bacitracin resistance gene by two extracytoplasmic function sigma factors. J. Bacteriol. 184:6123-6129.
    • (2002) J. Bacteriol. , vol.184 , pp. 6123-6129
    • Cao, M.1    Helmann, J.D.2
  • 8
    • 0036307635 scopus 로고    scopus 로고
    • Defining the Bacillus subtills sigma(W) regulon: A comparative analysis of promoter consensus search, run-off transcription/macroarray analysis (ROMA), and transcriptional profiling approaches
    • Cao, M., P. A. Kobel, M. M. Morshedi, M. F. Wu, C. Paddon, and J. D. Helmann. 2002. Defining the Bacillus subtills sigma(W) regulon: a comparative analysis of promoter consensus search, run-off transcription/macroarray analysis (ROMA), and transcriptional profiling approaches. J. Mol. Biol. 316:443-457.
    • (2002) J. Mol. Biol. , vol.316 , pp. 443-457
    • Cao, M.1    Kobel, P.A.2    Morshedi, M.M.3    Wu, M.F.4    Paddon, C.5    Helmann, J.D.6
  • 9
    • 0027218065 scopus 로고
    • Metalloregulation in Bacillus subtilis: Isolation and characterization of two genes differentially regulated by metal ions
    • Chen, L., L. P. James, and J. D. Helmann. 1993. Metalloregulation in Bacillus subtilis: isolation and characterization of two genes differentially regulated by metal ions. J. Bacteriol. 175:5428-5437.
    • (1993) J. Bacteriol. , vol.175 , pp. 5428-5437
    • Chen, L.1    James, L.P.2    Helmann, J.D.3
  • 10
    • 0028977969 scopus 로고
    • D: Overproduction, domain analysis, and DNA-binding
    • D: overproduction, domain analysis, and DNA-binding. J. Mol. Biol. 249:743-753.
    • (1995) J. Mol. Biol. , vol.249 , pp. 743-753
    • Chen, Y.-F.1    Helmann, J.D.2
  • 11
    • 0032932438 scopus 로고    scopus 로고
    • Insertional inactivation of genes responsible for the D-alanylation of lipoteichoic acid in Streptococcus gordonii DL1 (Challis) affects intrageneric coaggregations
    • Clemans, D. L., P. E. Kolenbrander, D. V. Debabov, Q. Zhang, R. D. Lunsford, H. Sakone, C. J. Whittaker, M. P. Heaton, and F. C. Neuhaus. 1999. Insertional inactivation of genes responsible for the D-alanylation of lipoteichoic acid in Streptococcus gordonii DL1 (Challis) affects intrageneric coaggregations. Infect. Immun. 67:2464-2474.
    • (1999) Infect. Immun. , vol.67 , pp. 2464-2474
    • Clemans, D.L.1    Kolenbrander, P.E.2    Debabov, D.V.3    Zhang, Q.4    Lunsford, R.D.5    Sakone, H.6    Whittaker, C.J.7    Heaton, M.P.8    Neuhaus, F.C.9
  • 12
    • 0033786504 scopus 로고    scopus 로고
    • Human antimicrobial peptides: Analysis and application
    • Cole, A. M., and T. Ganz. 2000. Human antimicrobial peptides: analysis and application. BioTechniques 29:822-826, 828, 830-831.
    • (2000) BioTechniques , vol.29 , pp. 822-826
    • Cole, A.M.1    Ganz, T.2
  • 13
    • 0031975578 scopus 로고    scopus 로고
    • Nisin resistance in Listeria monocytogenes ATCC 700302 is a complex phenotype
    • Crandall, A. D., and T. J. Montville. 1998. Nisin resistance in Listeria monocytogenes ATCC 700302 is a complex phenotype. Appl. Environ. Microbiol. 64:231-237.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 231-237
    • Crandall, A.D.1    Montville, T.J.2
  • 14
    • 0023800594 scopus 로고
    • Physiology of lipoteichoic acids in bacteria
    • Fischer, W. 1988. Physiology of lipoteichoic acids in bacteria. Adv. Microb. Physiol. 29:233-302.
    • (1988) Adv. Microb. Physiol. , vol.29 , pp. 233-302
    • Fischer, W.1
  • 15
    • 0029832102 scopus 로고    scopus 로고
    • FlgM is a primary regulator of σD activity, and its absence restores motility to a sinR mutant
    • Fredrick, K., and J. D. Helmann. 1996. FlgM is a primary regulator of σD activity, and its absence restores motility to a sinR mutant. J. Bacteriol. 178:7010-7013.
    • (1996) J. Bacteriol. , vol.178 , pp. 7010-7013
    • Fredrick, K.1    Helmann, J.D.2
  • 17
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • Hancock, R. E., and G. Diamond. 2000. The role of cationic antimicrobial peptides in innate host defences. Trends Microbiol. 8:402-410.
    • (2000) Trends Microbiol. , vol.8 , pp. 402-410
    • Hancock, R.E.1    Diamond, G.2
  • 18
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock, R. E., and M. G. Scott. 2000. The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Sci. USA 97:8856-8861.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8856-8861
    • Hancock, R.E.1    Scott, M.G.2
  • 19
    • 0035985580 scopus 로고    scopus 로고
    • The extracytoplasmic function (ECF) sigma factors
    • Helmann, J. D. 2002. The extracytoplasmic function (ECF) sigma factors. Adv. Microb. Physiol. 46:47-110.
    • (2002) Adv. Microb. Physiol. , vol.46 , pp. 47-110
    • Helmann, J.D.1
  • 20
    • 0030971546 scopus 로고    scopus 로고
    • X protein is an extracytoplasmic function sigma factor contributing to survival at high temperature
    • X protein is an extracytoplasmic function sigma factor contributing to survival at high temperature. J. Bacteriol. 179:2915-2921.
    • (1997) J. Bacteriol. , vol.179 , pp. 2915-2921
    • Huang, X.1    Decatur, A.2    Sorokin, A.3    Helmann, J.D.4
  • 22
    • 0032577384 scopus 로고    scopus 로고
    • X factor using a consensus-directed search
    • X factor using a consensus-directed search. J. Mol. Biol. 279:165-173.
    • (1998) J. Mol. Biol. , vol.279 , pp. 165-173
    • Huang, X.1    Helmann, J.D.2
  • 23
    • 0034282698 scopus 로고    scopus 로고
    • D-Alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis
    • Hyyrylainen, H. L., M. Vitikainen, J. Thwaite, H. Wu, M. Sarvas, C. R. Harwood, V. P. Kontinen, and K. Stephenson. 2000. D-Alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis. J. Biol. Chem. 275:26696-26703.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26696-26703
    • Hyyrylainen, H.L.1    Vitikainen, M.2    Thwaite, J.3    Wu, H.4    Sarvas, M.5    Harwood, C.R.6    Kontinen, V.P.7    Stephenson, K.8
  • 24
    • 0028990155 scopus 로고
    • Bacteriocins of Gram-positive bacteria
    • Jack, R. W., J. R. Tagg, and B. Ray. 1995. Bacteriocins of Gram-positive bacteria. Microbiol. Rev. 59:171-200.
    • (1995) Microbiol. Rev. , vol.59 , pp. 171-200
    • Jack, R.W.1    Tagg, J.R.2    Ray, B.3
  • 25
    • 0028353038 scopus 로고
    • The delta subunit of Bacillus subtilis RNA polymerase. An allosteric effector of the initiation and core-recycling phases of transcription
    • Juang, Y. L., and J. D. Helmann. 1994. The delta subunit of Bacillus subtilis RNA polymerase. An allosteric effector of the initiation and core-recycling phases of transcription. J. Mol. Biol. 239:1-14.
    • (1994) J. Mol. Biol. , vol.239 , pp. 1-14
    • Juang, Y.L.1    Helmann, J.D.2
  • 26
    • 0022397946 scopus 로고
    • Maintenance of D-alanine ester substitution of lipoteichoic acid by reesterification in Staphylococcus aureus
    • Koch, H. U., R. Doker, and W. Fischer. 1985. Maintenance of D-alanine ester substitution of lipoteichoic acid by reesterification in Staphylococcus aureus. J. Bacteriol. 164:1211-1217.
    • (1985) J. Bacteriol. , vol.164 , pp. 1211-1217
    • Koch, H.U.1    Doker, R.2    Fischer, W.3
  • 27
    • 0037218495 scopus 로고    scopus 로고
    • MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing
    • Kristian, S. A., M. Durr, J. A. Van Strijp, B. Neumeister, and A. Peschel. 2003. MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing. Infect. Immun. 71:546-549.
    • (2003) Infect. Immun. , vol.71 , pp. 546-549
    • Kristian, S.A.1    Durr, M.2    Van Strijp, J.A.3    Neumeister, B.4    Peschel, A.5
  • 29
    • 0036006036 scopus 로고    scopus 로고
    • Comparison of ribitol and glycerol teichoic acid genes in Bacillus subtilis W23 and 168: Identical function, similar divergent organization, but different regulation
    • Lazarevic, V., F. X. Abellan, S. B. Moller, D. Karamata, and C. Mauel. 2002. Comparison of ribitol and glycerol teichoic acid genes in Bacillus subtilis W23 and 168: identical function, similar divergent organization, but different regulation. Microbiology 148:815-824.
    • (2002) Microbiology , vol.148 , pp. 815-824
    • Lazarevic, V.1    Abellan, F.X.2    Moller, S.B.3    Karamata, D.4    Mauel, C.5
  • 30
    • 0026673165 scopus 로고
    • Sequencing and analysis of the Bacillus subtilis lytRABC divergon: A regulatory unit encompassing the structural genes of the N-acetylmuramoyl-L-alanine amidase and its modifier
    • Lazarevic, V., P. Margot, B. Soldo, and D. Karamata. 1992. Sequencing and analysis of the Bacillus subtilis lytRABC divergon: a regulatory unit encompassing the structural genes of the N-acetylmuramoyl-L-alanine amidase and its modifier. J. Gen. Microbiol. 138:1949-1961.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1949-1961
    • Lazarevic, V.1    Margot, P.2    Soldo, B.3    Karamata, D.4
  • 31
    • 0029087264 scopus 로고
    • Structural analysis of the Bacillus subtilis delta factor: A protein polyanion which displaces RNA from RNA polymerase
    • Lopez de Saro, F. J., A. Y. Woody, and J. D. Helmann. 1995. Structural analysis of the Bacillus subtilis delta factor: a protein polyanion which displaces RNA from RNA polymerase. J. Mol. Biol. 252:189-202.
    • (1995) J. Mol. Biol. , vol.252 , pp. 189-202
    • Lopez De Saro, F.J.1    Woody, A.Y.2    Helmann, J.D.3
  • 33
    • 0031983523 scopus 로고    scopus 로고
    • Cloning, sequencing, and disruption of the Bacillus subtilis psd gene coding for phosphatidylserine decarboxylase
    • Matsumoto, K., M. Okada, Y. Horikoshi, H. Matsuzaki, T. Kishi, M. Itaya, and I. Shibuya. 1998. Cloning, sequencing, and disruption of the Bacillus subtilis psd gene coding for phosphatidylserine decarboxylase. J. Bacteriol. 180:100-106.
    • (1998) J. Bacteriol. , vol.180 , pp. 100-106
    • Matsumoto, K.1    Okada, M.2    Horikoshi, Y.3    Matsuzaki, H.4    Kishi, T.5    Itaya, M.6    Shibuya, I.7
  • 34
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics, p. 352-355. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 35
    • 0141677802 scopus 로고    scopus 로고
    • M, two sigma factors of the extracytoplasmic function subfamily, are required for septum and wall synthesis under batch culture conditions
    • M, two sigma factors of the extracytoplasmic function subfamily, are required for septum and wall synthesis under batch culture conditions. Mol. Microbiol. 49:1435-1447.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1435-1447
    • Minnig, K.1    Barblan, J.L.2    Kehl, S.3    Moller, S.B.4    Mauel, C.5
  • 36
    • 0028935455 scopus 로고
    • SubtiList: A relational database for the Bacillus subtilis genome
    • Moszer, I., P. Glaser, and A. Danchin. 1995. SubtiList: a relational database for the Bacillus subtilis genome. Microbiology 141:261-268.
    • (1995) Microbiology , vol.141 , pp. 261-268
    • Moszer, I.1    Glaser, P.2    Danchin, A.3
  • 37
    • 0028913503 scopus 로고
    • Regulation of citrate-dependent iron transport of Escherichia coli: fecR is required for transcription activation by FecI
    • Ochs, M., S. Veitinger, I. Kim, D. Welz, A. Angerer, and V. Braun. 1995. Regulation of citrate-dependent iron transport of Escherichia coli: fecR is required for transcription activation by FecI. Mol. Microbiol. 15:119-132.
    • (1995) Mol. Microbiol. , vol.15 , pp. 119-132
    • Ochs, M.1    Veitinger, S.2    Kim, I.3    Welz, D.4    Angerer, A.5    Braun, V.6
  • 38
    • 0037214439 scopus 로고    scopus 로고
    • A bacitracin-resistant Bacillus subtilis gene encodes a homologue of the membrane-spanning subunit of the Bacillus licheniformis ABC transporter
    • Ohki, R., K. Tateno, Y. Okada, H. Okajima, K. Asai, Y. Sadaie, M. Murata, and T. Aiso. 2003. A bacitracin-resistant Bacillus subtilis gene encodes a homologue of the membrane-spanning subunit of the Bacillus licheniformis ABC transporter. J. Bacteriol. 185:51-59.
    • (2003) J. Bacteriol. , vol.185 , pp. 51-59
    • Ohki, R.1    Tateno, K.2    Okada, Y.3    Okajima, H.4    Asai, K.5    Sadaie, Y.6    Murata, M.7    Aiso, T.8
  • 39
    • 0027984012 scopus 로고
    • Cloning, sequencing, and expression in Escherichia coli of the Bacillus subtilis gene for phosphatidylserine synthase
    • Okada, M., H. Matsuzaki, I. Shibuya, and K. Matsumoto. 1994. Cloning, sequencing, and expression in Escherichia coli of the Bacillus subtilis gene for phosphatidylserine synthase. J. Bacteriol. 176:7456-7461.
    • (1994) J. Bacteriol. , vol.176 , pp. 7456-7461
    • Okada, M.1    Matsuzaki, H.2    Shibuya, I.3    Matsumoto, K.4
  • 40
    • 0033047685 scopus 로고    scopus 로고
    • A putative two-component signal transduction system regulates sigmaE, a sigma factor required for normal cell wall integrity in Streptomyces coelicolor A3(2)
    • Paget, M. S., E. Leibovitz, and M. J. Buttner. 1999. A putative two-component signal transduction system regulates sigmaE, a sigma factor required for normal cell wall integrity in Streptomyces coelicolor A3(2). Mol. Microbiol. 33:97-107.
    • (1999) Mol. Microbiol. , vol.33 , pp. 97-107
    • Paget, M.S.1    Leibovitz, E.2    Buttner, M.J.3
  • 41
    • 0032898961 scopus 로고    scopus 로고
    • Evidence that the extracytoplasmic function sigma factor σE is required for normal cell wall structure in Streptomyces coelicolor A3(2)
    • Paget, M. S. B., L. Chamberlin, A. Atrih, S. J. Foster, and M. J. Buttner. 1999. Evidence that the extracytoplasmic function sigma factor σE is required for normal cell wall structure in Streptomyces coelicolor A3(2). J. Bacteriol. 181:204-211.
    • (1999) J. Bacteriol. , vol.181 , pp. 204-211
    • Paget, M.S.B.1    Chamberlin, L.2    Atrih, A.3    Foster, S.J.4    Buttner, M.J.5
  • 42
    • 0002151089 scopus 로고
    • Integrational vectors for genetic manipulation in Bacillus subtilis
    • A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.). American Society for Microbiology, Washington, D.C.
    • Perego, M. 1993. Integrational vectors for genetic manipulation in Bacillus subtilis, p. 615-624. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and other gram-positive bacteria: biochemistry, physiology, and molecular genetics. American Society for Microbiology, Washington, D.C.
    • (1993) Bacillus Subtilis and Other Gram-Positive Bacteria: Biochemistry, Physiology, and Molecular Genetics , pp. 615-624
    • Perego, M.1
  • 43
    • 0029897997 scopus 로고    scopus 로고
    • Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis
    • Perego, M., P. Glaser, and J. A. Hoch. 1996. Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis. Mol. Microbiol. 19:1151-1157.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1151-1157
    • Perego, M.1    Glaser, P.2    Hoch, J.A.3
  • 44
    • 0028982844 scopus 로고
    • Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation
    • Perego, M., P. Glaser, A. Minutello, M. A. Strauch, K. Leopold, and W. Fischer. 1995. Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation. J. Biol. Chem. 270:15598-15606.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15598-15606
    • Perego, M.1    Glaser, P.2    Minutello, A.3    Strauch, M.A.4    Leopold, K.5    Fischer, W.6
  • 45
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • Peschel, A., M. Otto, R. W. Jack, H. Kalbacher, G. Jung, and F. Gotz. 1999. Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J. Biol. Chem. 274:8405-8410.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3    Kalbacher, H.4    Jung, G.5    Gotz, F.6
  • 46
    • 0035685114 scopus 로고    scopus 로고
    • Regulation of D-alanyl-lipoteichoic acid biosynthesis in Streptococcus agalactiae involves a novel two-component regulatory system
    • Poyart, C., M. C. Lamy, C. Boumaila, F. Fiedler, and P. Trieu-Cuot. 2001. Regulation of D-alanyl-lipoteichoic acid biosynthesis in Streptococcus agalactiae involves a novel two-component regulatory system. J. Bacteriol. 183:6324-6334.
    • (2001) J. Bacteriol. , vol.183 , pp. 6324-6334
    • Poyart, C.1    Lamy, M.C.2    Boumaila, C.3    Fiedler, F.4    Trieu-Cuot, P.5
  • 47
    • 0141789720 scopus 로고    scopus 로고
    • Attenuated virulence of Streptococcus agalactiae deficient in D-alanyl-lipoteichoic acid is due to an increased susceptibility to defensins and phagocytic cells
    • Poyart, C., E. Pellegrini, M. Marceau, M. Baptista, F. Jaubert, M. C. Lamy, and P. Trieu-Cuot. 2003. Attenuated virulence of Streptococcus agalactiae deficient in D-alanyl-lipoteichoic acid is due to an increased susceptibility to defensins and phagocytic cells. Mol. Microbiol. 49:1615-1625.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1615-1625
    • Poyart, C.1    Pellegrini, E.2    Marceau, M.3    Baptista, M.4    Jaubert, F.5    Lamy, M.C.6    Trieu-Cuot, P.7
  • 49
    • 0142043317 scopus 로고    scopus 로고
    • New members of the Escherichia coli sigmaE regulon identified by a two-plasmid system
    • Rezuchova, B., H. Miticka, D. Homerova, M. Roberts, and J. Kormanec. 2003. New members of the Escherichia coli sigmaE regulon identified by a two-plasmid system. FEMS Microbiol. Lett. 225:1-7.
    • (2003) FEMS Microbiol. Lett. , vol.225 , pp. 1-7
    • Rezuchova, B.1    Miticka, H.2    Homerova, D.3    Roberts, M.4    Kormanec, J.5
  • 51
    • 0027198224 scopus 로고
    • Mutations that relieve nutritional repression of the Bacillus subtilis dipeptide permease operon
    • Slack, F. J., J. P. Mueller, and A. L. Sonenshein. 1993. Mutations that relieve nutritional repression of the Bacillus subtilis dipeptide permease operon. J. Bacteriol. 175:4605-4614.
    • (1993) J. Bacteriol. , vol.175 , pp. 4605-4614
    • Slack, F.J.1    Mueller, J.P.2    Sonenshein, A.L.3
  • 53
    • 0036892206 scopus 로고    scopus 로고
    • Identification and genetic characterization of PmrA-regulated genes and genes involved in polymyxin B resistance in Salmonella enterica serovar Typhimurium
    • Tamayo, R., S. S. Ryan, A. J. McCoy, and J. S. Gunn. 2002. Identification and genetic characterization of PmrA-regulated genes and genes involved in polymyxin B resistance in Salmonella enterica serovar Typhimurium. Infect. Immun. 70:6770-6778.
    • (2002) Infect. Immun. , vol.70 , pp. 6770-6778
    • Tamayo, R.1    Ryan, S.S.2    McCoy, A.J.3    Gunn, J.S.4
  • 54
    • 0036135303 scopus 로고    scopus 로고
    • Optimization of the cell wall microenvironment allows increased production of recombinant Bacillus anthracis protective antigen from B. subtilis
    • Thwaite, J. E., L. W. Baillie, N. M. Carter, K. Stephenson, M. Rees, C. R. Harwood, and P. T. Emmerson. 2002. Optimization of the cell wall microenvironment allows increased production of recombinant Bacillus anthracis protective antigen from B. subtilis. Appl. Environ. Microbiol. 68:227-234.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 227-234
    • Thwaite, J.E.1    Baillie, L.W.2    Carter, N.M.3    Stephenson, K.4    Rees, M.5    Harwood, C.R.6    Emmerson, P.T.7
  • 56
    • 0031737309 scopus 로고    scopus 로고
    • A vector for systematic gene inactivation in Bacillus subtilis
    • Vagner, V., E. Dervyn, and S. D. Ehrlich. 1998. A vector for systematic gene inactivation in Bacillus subtilis. Microbiology 144(Part 11):3097-3104.
    • (1998) Microbiology , vol.144 , Issue.PART 11 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, S.D.3
  • 57
    • 0030819057 scopus 로고    scopus 로고
    • The absence of D-alanine from lipoteichoic acid and wall teichoic acid alters surface charge, enhances autolysis and increases susceptibility to methicillin in Bacillus subtilis
    • Wecke, J., M. Kazimierz, and W. Fischer. 1997. The absence of D-alanine from lipoteichoic acid and wall teichoic acid alters surface charge, enhances autolysis and increases susceptibility to methicillin in Bacillus subtilis. Microbiology 143:2953-2960.
    • (1997) Microbiology , vol.143 , pp. 2953-2960
    • Wecke, J.1    Kazimierz, M.2    Fischer, W.3
  • 58
    • 0029775205 scopus 로고    scopus 로고
    • D-alanine deprivation of Bacillus subtilis teichoic acids is without effect on cell growth and morphology but affects the autolytic activity
    • Wecke, J., M. Perego, and W. Fischer. 1996. D-alanine deprivation of Bacillus subtilis teichoic acids is without effect on cell growth and morphology but affects the autolytic activity. Microb. Drug Resist. 2:123-129.
    • (1996) Microb. Drug Resist. , vol.2 , pp. 123-129
    • Wecke, J.1    Perego, M.2    Fischer, W.3
  • 59
    • 0001673849 scopus 로고
    • Use of transposons and integrational vectors for mutagenesis and construction of gene fusions in Bacillus species
    • C. R. Harwood and S. M. Cutting (ed.). John Wiley and Sons, Ltd., Chichester, United Kingdom
    • Youngman, P. 1990. Use of transposons and integrational vectors for mutagenesis and construction of gene fusions in Bacillus species, p. 221-266. In C. R. Harwood and S. M. Cutting (ed.), Molecular biological methods for bacillus. John Wiley and Sons, Ltd., Chichester, United Kingdom.
    • (1990) Molecular Biological Methods for Bacillus , pp. 221-266
    • Youngman, P.1
  • 60
    • 0023272642 scopus 로고
    • Role of AbrB and SpoOA- and SpoOB-dependent utilization of a sporulation promoter in Bacillus subtilis
    • Zuber, P., and R. Losick. 1987. Role of AbrB and SpoOA- and SpoOB-dependent utilization of a sporulation promoter in Bacillus subtilis. J. Bacteriol. 169:2223-2230.
    • (1987) J. Bacteriol. , vol.169 , pp. 2223-2230
    • Zuber, P.1    Losick, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.