메뉴 건너뛰기




Volumn 144, Issue 1, 1998, Pages 73-82

The role of autolysins during vegetative growth of Bacillus subtilis 168

Author keywords

Autolysins; Bacillus subtilis; Cell separation; Cell wall turnover; Motility

Indexed keywords

AMIDASE; AUTOLYSIN; BACTERIAL ENZYME; GLUCOSAMINIDASE; HYDROLASE; SIGMA FACTOR; SODIUM AZIDE; UNCLASSIFIED DRUG;

EID: 0031963480     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-144-1-73     Document Type: Article
Times cited : (139)

References (41)
  • 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
    • 0017264141 scopus 로고
    • Bacteriophage SP50 as a marker for cell wall growth in Bacillus subtilis
    • Archibald, A. R. & Coapes, H. E. (1976). Bacteriophage SP50 as a marker for cell wall growth in Bacillus subtilis. J Bacteriol 125, 1195-1206.
    • (1976) J Bacteriol , vol.125 , pp. 1195-1206
    • Archibald, A.R.1    Coapes, H.E.2
  • 3
    • 0021906704 scopus 로고
    • Mono-valent cations enable cell-wall turnover of the turnover-deficient lyt-15 mutant of Bacillus subtilis
    • Cheung, H. Y. & Freese, E. (1985). Mono-valent cations enable cell-wall turnover of the turnover-deficient lyt-15 mutant of Bacillus subtilis. J Bacteriol 161, 1222-1225.
    • (1985) J Bacteriol , vol.161 , pp. 1222-1225
    • Cheung, H.Y.1    Freese, E.2
  • 4
    • 0024605246 scopus 로고
    • Cell wall assembly in Bacillus subtilis: Partial conservation of polar wall material and the 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 the 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
  • 5
    • 0002301028 scopus 로고
    • Genetic analysis
    • Edited by C. R. Harwood & S. M. Cutting. Chichester: John Wiley
    • Cutting, S. M. & Vander Horn, P. B. (1990). Genetic analysis. In Molecular Biology Methods for Bacillus, pp. 27-74. Edited by C. R. Harwood & S. M. Cutting. Chichester: John Wiley.
    • (1990) Molecular Biology Methods for Bacillus , pp. 27-74
    • Cutting, S.M.1    Vander Horn, P.B.2
  • 6
    • 0029842085 scopus 로고    scopus 로고
    • Peptidoglycan as a barrier to transenvelope transport
    • Dijkstra, A. J. & Keck, W. (1996). Peptidoglycan as a barrier to transenvelope transport. J Bacteriol 178, 5555-5562.
    • (1996) J Bacteriol , vol.178 , pp. 5555-5562
    • Dijkstra, A.J.1    Keck, W.2
  • 7
    • 0018415260 scopus 로고
    • Possible involvement of bacterial autolysin enzymes in flagellar morphogenesis
    • Fein, J. E. (1979). Possible involvement of bacterial autolysin enzymes in flagellar morphogenesis. J Bacteriol 137, 933-946.
    • (1979) J Bacteriol , vol.137 , pp. 933-946
    • Fein, J.E.1
  • 8
    • 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
  • 9
    • 0019456412 scopus 로고
    • Effect of alanine ester substitution and other structural features of lipoteichoic acids on their inhibitory activity against autolysins of Staphylococcus aureus
    • Fischer, W., Rosel, P. & Koch, H. U. (1981). Effect of alanine ester substitution and other structural features of lipoteichoic acids on their inhibitory activity against autolysins of Staphylococcus aureus. J Bacteriol 146, 467-475.
    • (1981) J Bacteriol , vol.146 , pp. 467-475
    • Fischer, W.1    Rosel, P.2    Koch, H.U.3
  • 10
    • 0015235792 scopus 로고
    • Autolytic enzymes in growth of bacteria
    • Forsberg, C. & Rogers, H. J. (1971). Autolytic enzymes in growth of bacteria. Nature 229, 272-273.
    • (1971) Nature , vol.229 , pp. 272-273
    • Forsberg, C.1    Rogers, H.J.2
  • 11
    • 0025779454 scopus 로고
    • Cloning, expression, sequence analysis and biochemical characterization of an autolytic amidase of Bacillus subtilis 168 trpC2
    • Foster, S. J. (1991). Cloning, expression, sequence analysis and biochemical characterization of an autolytic amidase of Bacillus subtilis 168 trpC2. J Gen Microbiol 137, 1987-1998.
    • (1991) J Gen Microbiol , vol.137 , pp. 1987-1998
    • Foster, S.J.1
  • 12
    • 0026512822 scopus 로고
    • Analysis of the autolysins of Bacillus subtilis 168 during vegetative growth and differentiation by using renaturing polyacrylamide gel electrophoresis
    • Foster, S. J. (1992). Analysis of the autolysins of Bacillus subtilis 168 during vegetative growth and differentiation by using renaturing polyacrylamide gel electrophoresis. J Bacteriol 174, 464-470.
    • (1992) J Bacteriol , vol.174 , pp. 464-470
    • Foster, S.J.1
  • 13
    • 0027154835 scopus 로고
    • Molecular analysis of three major wall-associated proteins of Bacillus subtilis 168: Evidence for processing of the product of a gene encoding a 258 kDa precursor two-domain ligand-binding protein
    • Foster, S. J. (1993). Molecular analysis of three major wall-associated proteins of Bacillus subtilis 168: evidence for processing of the product of a gene encoding a 258 kDa precursor two-domain ligand-binding protein. Mol Microbiol 8, 299-310.
    • (1993) Mol Microbiol , vol.8 , pp. 299-310
    • Foster, S.J.1
  • 14
    • 0029832102 scopus 로고    scopus 로고
    • D activity, and its absence restores motility to a sinR mutant
    • D 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
  • 15
    • 0023022816 scopus 로고
    • Characterization of a cloned Bacillus subtilis gene that inhibits sporulation in multiple copies
    • Gaur, N. K., Dubnau, E. & Smith, I. (1986). Characterization of a cloned Bacillus subtilis gene that inhibits sporulation in multiple copies. J Bacteriol 168, 860-869.
    • (1986) J Bacteriol , vol.168 , pp. 860-869
    • Gaur, N.K.1    Dubnau, E.2    Smith, I.3
  • 17
    • 0029019594 scopus 로고
    • Characterization of cell cycle events during the onset of sporulation in Bacillus subtilis
    • Hauser, P. M. & Errington, J. (1995). Characterization of cell cycle events during the onset of sporulation in Bacillus subtilis. J Bacteriol 177, 3923-3931.
    • (1995) J Bacteriol , vol.177 , pp. 3923-3931
    • Hauser, P.M.1    Errington, J.2
  • 19
    • 0016695987 scopus 로고
    • Bacillus subtilis N-acetyl-muramic acid L-alanine amidase
    • Herbold, D. R. & Glaser, L. (1975). Bacillus subtilis N-acetyl-muramic acid L-alanine amidase. J Biol Chem 250, 1676-1682.
    • (1975) J Biol Chem , vol.250 , pp. 1676-1682
    • Herbold, D.R.1    Glaser, L.2
  • 20
    • 0018838184 scopus 로고
    • Extracellular proteases modify cell wall turnover in Bacillus subtilis
    • Jolliffe, L. K., Doyle, R. J. & Streips, U. N. (1980). Extracellular proteases modify cell wall turnover in Bacillus subtilis. J Bacteriol 141, 1199-1208.
    • (1980) J Bacteriol , vol.141 , pp. 1199-1208
    • Jolliffe, L.K.1    Doyle, R.J.2    Streips, U.N.3
  • 21
    • 0019452877 scopus 로고
    • The energised membrane and cellular autolysis in Bacillus subtilis
    • Jolliffe, L. K., Doyle, R. J. & Streips, U. N. (1981). The energised membrane and cellular autolysis in Bacillus subtilis. Cell 25, 753-763.
    • (1981) Cell , vol.25 , pp. 753-763
    • Jolliffe, L.K.1    Doyle, R.J.2    Streips, U.N.3
  • 23
    • 0025824740 scopus 로고
    • Molecular cloning and sequencing of a major Bacillus subtilis autolysin gene
    • Kuroda, A. & Sekiguchi, J. (1991). Molecular cloning and sequencing of a major Bacillus subtilis autolysin gene. J Bacteriol 173, 7304-7312.
    • (1991) J Bacteriol , vol.173 , pp. 7304-7312
    • Kuroda, A.1    Sekiguchi, J.2
  • 24
    • 0027408496 scopus 로고
    • High-level transcription of the major Bacillus subtilis autolysin operon depends on expression of the sigma D gene and is affected by a sin(flaD) mutation
    • Kuroda, A. & Sekiguchi, J. (1993). High-level transcription of the major Bacillus subtilis autolysin operon depends on expression of the sigma D gene and is affected by a sin(flaD) mutation. J Bacteriol 175, 795-801.
    • (1993) J Bacteriol , vol.175 , pp. 795-801
    • Kuroda, A.1    Sekiguchi, J.2
  • 25
    • 0026694316 scopus 로고
    • Molecular cloning and sequencing of the upstream region of the major Bacillus subtilis autolysin gene: A modifier protein exhibiting sequence homology to the major autolysin and the spoIID product
    • Kuroda, A., Rashid, M. H. & Sekiguchi, J. (1992). Molecular cloning and sequencing of the upstream region of the major Bacillus subtilis autolysin gene: a modifier protein exhibiting sequence homology to the major autolysin and the spoIID product. J Gen Microbiol 138, 1067-1076.
    • (1992) J Gen Microbiol , vol.138 , pp. 1067-1076
    • Kuroda, A.1    Rashid, M.H.2    Sekiguchi, J.3
  • 26
    • 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
  • 27
    • 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., Margot, P., Soldo, B. & Karamata, D. (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
  • 28
    • 2342485557 scopus 로고
    • Chaining and unchaining of Streptococcus faecalis: A hypothesis of the mechanism of bacterial separation
    • Lominski, I., Cameron, J. & Wyllie, G. (1958). Chaining and unchaining of Streptococcus faecalis: a hypothesis of the mechanism of bacterial separation. Nature 181, 1477.
    • (1958) Nature , vol.181 , pp. 1477
    • Lominski, I.1    Cameron, J.2    Wyllie, G.3
  • 29
    • 0026554413 scopus 로고
    • Identification of the structural genes for N-acetylmuramoyl-L-alanine amidase and its modifier in Bacillus subtilis 168: Inactivation of these genes by insertional mutagenesis has no effect on growth or cell separation
    • Margot, P. & Karamata, D. (1992). Identification of the structural genes for N-acetylmuramoyl-L-alanine amidase and its modifier in Bacillus subtilis 168: inactivation of these genes by insertional mutagenesis has no effect on growth or cell separation. Mol Gen Genet 232, 358-366.
    • (1992) Mol Gen Genet , vol.232 , pp. 358-366
    • Margot, P.1    Karamata, D.2
  • 30
    • 0028291159 scopus 로고
    • The gene of the N-acetylglucosaminidase, a Bacillus subtilis cell wall hydrolase not involved in vegetative cell autolysis
    • Margot, P., Mauël, C. & Karamata, D. (1994). The gene of the N-acetylglucosaminidase, a Bacillus subtilis cell wall hydrolase not involved in vegetative cell autolysis. Mol Microbiol 12, 535-545.
    • (1994) Mol Microbiol , vol.12 , pp. 535-545
    • Margot, P.1    Mauël, C.2    Karamata, D.3
  • 31
    • 0021684699 scopus 로고
    • Genetic analysis of autolysindeficient and flagellaless mutants of Bacillus subtilis
    • Pooley, H. & Karamata, D. (1984). Genetic analysis of autolysindeficient and flagellaless mutants of Bacillus subtilis. J Bacteriol 160, 1123-1129.
    • (1984) J Bacteriol , vol.160 , pp. 1123-1129
    • Pooley, H.1    Karamata, D.2
  • 32
    • 85046520823 scopus 로고
    • Bacillus subtilis mutant deficient in the major autolytic amidase and glucosaminidase is impaired in motility
    • Rashid, M. H., Kuroda, A. & Sekiguchi, J. (1993). Bacillus subtilis mutant deficient in the major autolytic amidase and glucosaminidase is impaired in motility. FEMS Microbiol Lett 112, 135-140.
    • (1993) FEMS Microbiol Lett , vol.112 , pp. 135-140
    • Rashid, M.H.1    Kuroda, A.2    Sekiguchi, J.3
  • 33
    • 0028805257 scopus 로고
    • Glucosaminidase of Bacillus subtilis: Cloning, regulation, primary structure and biochemical characterization
    • Rashid, M. H., Mori, H. & Sekiguchi, J. (1995). Glucosaminidase of Bacillus subtilis: cloning, regulation, primary structure and biochemical characterization. Microbiology 141, 2391-2404.
    • (1995) Microbiology , vol.141 , pp. 2391-2404
    • Rashid, M.H.1    Mori, H.2    Sekiguchi, J.3
  • 34
    • 0020660322 scopus 로고
    • The bactericidal action of β-lactam antibiotics on an autolysindeficient strain of Bacillus subtilis
    • Rogers, H. J., Thurman, P. F. & Burdett, I. D. J. (1983). The bactericidal action of β-lactam antibiotics on an autolysindeficient strain of Bacillus subtilis. J Gen Microbiol 129, 465-478.
    • (1983) J Gen Microbiol , vol.129 , pp. 465-478
    • Rogers, H.J.1    Thurman, P.F.2    Burdett, I.D.J.3
  • 35
    • 0021233039 scopus 로고
    • Purification and properties of autolytic endo-β-N-acetylglucosaminidase and the N-acetylmuramoyl-L-alanine amidase from Bacillus subtilis strain 168
    • Rogers, H. J., Taylor, C., Rayter, S. & Ward, J. B. (1984). Purification and properties of autolytic endo-β-N-acetylglucosaminidase and the N-acetylmuramoyl-L-alanine amidase from Bacillus subtilis strain 168. J Gen Microbiol 130, 2395-2402.
    • (1984) J Gen Microbiol , vol.130 , pp. 2395-2402
    • Rogers, H.J.1    Taylor, C.2    Rayter, S.3    Ward, J.B.4
  • 37
    • 0029058134 scopus 로고
    • Characterisation of the involvement of two compensatory autolysins in mother cell lysis during sporulation of Bacillus subtilis 168
    • Smith, T. J. & Foster, S. J. (1995). Characterisation of the involvement of two compensatory autolysins in mother cell lysis during sporulation of Bacillus subtilis 168. J Bacteriol 177, 3855-3862.
    • (1995) J Bacteriol , vol.177 , pp. 3855-3862
    • Smith, T.J.1    Foster, S.J.2
  • 38
    • 0029782491 scopus 로고    scopus 로고
    • Peptidoglycan hydrolases of Bacillus subtilis 168
    • Smith, T. J., Blackman, S. A. & Foster, S. J. (1996). Peptidoglycan hydrolases of Bacillus subtilis 168. Microb Drug Resist 2, 113-118.
    • (1996) Microb Drug Resist , vol.2 , pp. 113-118
    • Smith, T.J.1    Blackman, S.A.2    Foster, S.J.3
  • 39
    • 0028354905 scopus 로고
    • Plasmids designed to alter the antibiotic resistance expressed by insertion mutations in Bacillus subtilis, through in vivo recombination
    • Steinmetz, M. & Richter, R. (1994). Plasmids designed to alter the antibiotic resistance expressed by insertion mutations in Bacillus subtilis, through in vivo recombination. Gene 142, 79-83.
    • (1994) Gene , vol.142 , pp. 79-83
    • Steinmetz, M.1    Richter, R.2
  • 41
    • 0002066459 scopus 로고
    • Bacterial autolysins: Specificity and function
    • Edited by C. Nombela. Amsterdam: Elsevier
    • Ward, J. B. & Williamson, R. (1984). Bacterial autolysins: specificity and function. In Microbial Wall Synthesis and Function, pp. 159-166. Edited by C. Nombela. Amsterdam: Elsevier.
    • (1984) Microbial Wall Synthesis and Function , pp. 159-166
    • Ward, J.B.1    Williamson, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.