메뉴 건너뛰기




Volumn 72, Issue 6, 2009, Pages 1448-1461

The high-molecular-mass amylase (HMMA) of Geobacillus stearothermophilus ATCC 12980 interacts with the cell wall components by virtue of three specific binding regions

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; CELL MEMBRANE PROTEIN; EXOENZYME C3; PEPTIDOGLYCAN; POLYMER; RECOMBINANT PROTEIN; RECOMBINANT S LAYER PROTEIN; SECONDARY CELL WALL POLYMER; UNCLASSIFIED DRUG;

EID: 67049158420     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06734.x     Document Type: Article
Times cited : (13)

References (51)
  • 2
    • 23944439582 scopus 로고    scopus 로고
    • Lactobacillus surface layers and their applications
    • DOI 10.1016/j.femsre.2005.04.003, PII S0168644505000264
    • Avall-Jaaskelainen, S. Palva, A. (2005) Lactobacillus surface layers and their applications. FEMS Microbiol Rev 29 : 511 529. (Pubitemid 41186054)
    • (2005) FEMS Microbiology Reviews , vol.29 , Issue.3 SPEC. ISS. , pp. 511-529
    • Avall-Jaaskelainen, S.1    Palva, A.2
  • 3
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • Bendtsen, J.D., Nielsen, H., von Heijne, G. Brunak, S. (2004) Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 340 : 783 795. (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 4
    • 0032839730 scopus 로고    scopus 로고
    • In Thermoanaerobacterium thermosulfurigenes EM1 S-layer homology domains do not attach to peptidoglycan
    • Brechtel, E. Bahl, H. (1999) In Thermoanaerobacterium thermosulfurigenes EM1 S-layer homology domains do not attach to peptidoglycan. J Bacteriol 181 : 5017 5023. (Pubitemid 29383533)
    • (1999) Journal of Bacteriology , vol.181 , Issue.16 , pp. 5017-5023
    • Brechtel, E.1    Bahl, H.2
  • 5
    • 0026620295 scopus 로고
    • Evidence for an S-layer protein pool in the peptidoglycan of Bacillus stearothermophilus
    • Breitwieser, A., Gruber, K. Sleytr, U.B. (1992) Evidence for an S-layer protein pool in the peptidoglycan of Bacillus stearothermophilus. J Bacteriol 174 : 8008 8015. (Pubitemid 23002934)
    • (1992) Journal of Bacteriology , vol.174 , Issue.24 , pp. 8008-8015
    • Breitwieser, A.1    Gruber, K.2    Sleytr, U.B.3
  • 6
    • 2442511062 scopus 로고    scopus 로고
    • Binding to pyruvylated compounds as an ancestral mechanism to anchor the outer envelope in primitive bacteria
    • DOI 10.1111/j.1365-2958.2004.04011.x
    • Cava, F., de Pedro, M.A., Schwarz, H., Henne, A. Berenguer, J. (2004) Binding to pyruvylated compounds as an ancestral mechanism to anchor the outer envelope in primitive bacteria. Mol Microbiol 52 : 677 690. (Pubitemid 38621739)
    • (2004) Molecular Microbiology , vol.52 , Issue.3 , pp. 677-690
    • Cava, F.1    De Pedro, M.A.2    Schwarz, H.3    Henne, A.4    Berenguer, J.5
  • 7
    • 0001841906 scopus 로고
    • Strategies for obtaining partial amino acid sequence data from small quantities (< 5 nmol) of pure or partially purified protein
    • In. Matsudaira, P.T. (ed.). San Diego, CA. Academic Press. pp.
    • Charbonneau, H. (1989) Strategies for obtaining partial amino acid sequence data from small quantities (< 5 nmol) of pure or partially purified protein. In A Practical Guide to Protein and Peptide Purification for Microsequencing. Matsudaira, P.T. (ed.). San Diego, CA : Academic Press, pp. 15 29.
    • (1989) A Practical Guide to Protein and Peptide Purification for Microsequencing. , pp. 15-29
    • Charbonneau, H.1
  • 8
    • 0032929261 scopus 로고    scopus 로고
    • Distinct affinity of binding sites for S-layer homologous domains in Clostridium thermocellum and Bacillus anthracis cell envelopes
    • Chauvaux, S., Matuschek, M. Beguin, P. (1999) Distinct affinity of binding sites for S-layer homologous domains in Clostridium thermocellum and Bacillus anthracis cell envelopes. J Bacteriol 181 : 2455 2458. (Pubitemid 29181568)
    • (1999) Journal of Bacteriology , vol.181 , Issue.8 , pp. 2455-2458
    • Chauvaux, S.1    Matuschek, M.2    Beguin, P.3
  • 9
    • 0029819431 scopus 로고    scopus 로고
    • Evidence that an N-terminal S-layer protein fragment triggers the release of a cell-associated high-molecular-weight amylase in Bacillus stearothermophilus ATCC 12980
    • Egelseer, E.M., Schocher, I., Sleytr, U.B. Sára, M. (1996) Evidence that an N-terminal S-layer protein fragment triggers the release of a cell-associated high-molecular-weight amylase in Bacillus stearothermophilus ATCC 12980. J Bacteriol 178 : 5602 5609. (Pubitemid 26327659)
    • (1996) Journal of Bacteriology , vol.178 , Issue.19 , pp. 5602-5609
    • Egelseer, E.M.1    Schocher, I.2    Sleytr, U.B.3    Sara, M.4
  • 10
    • 0031941002 scopus 로고    scopus 로고
    • The S-layer proteins of two Bacillus stearothermophilus wild-type strains are bound via their N-terminal region to a secondary cell wall polymer of identical chemical composition
    • Egelseer, E.M., Leitner, K., Jarosch, M., Hotzy, C., Zayni, S., Sleytr, U.B. Sára, M. (1998) The S-layer proteins of two Bacillus stearothermophilus wild-type strains are bound via their N-terminal region to a secondary cell wall polymer of identical chemical composition. J Bacteriol 180 : 1488 1495. (Pubitemid 28125734)
    • (1998) Journal of Bacteriology , vol.180 , Issue.6 , pp. 1488-1495
    • Egelseer, E.M.1    Leitner, K.2    Jarosch, M.3    Hotzy, C.4    Zayni, S.5    Sleytr, U.B.6    Sara, M.7
  • 11
    • 0033824477 scopus 로고    scopus 로고
    • ISBst12, a novel type of insertion-sequence element causing loss of S-layer-gene expression in Bacillus stearothermophilus ATCC
    • 12980.
    • Egelseer, E.M., Idris, R., Jarosch, M., Danhorn, T., Sleytr, U.B. Sara, M. (2000) ISBst12, a novel type of insertion-sequence element causing loss of S-layer-gene expression in Bacillus stearothermophilus ATCC 12980. Microbiology 146 (Part 9 2175 2183.
    • (2000) Microbiology , vol.146 , Issue.PART 9 , pp. 2175-2183
    • Egelseer, E.M.1    Idris, R.2    Jarosch, M.3    Danhorn, T.4    Sleytr, U.B.5    Sara, M.6
  • 12
    • 0036136957 scopus 로고    scopus 로고
    • Characterization of an S-layer glycoprotein produced in the course of S-layer variation of Bacillus stearothermophilus ATCC
    • 12980 and sequencing and cloning of the sbsD Gene encoding the protein.
    • Egelseer, E.M., Danhorn, T., Pleschberger, M., Hotzy, C., Sleytr, U.B. Sára, M. (2001) Characterization of an S-layer glycoprotein produced in the course of S-layer variation of Bacillus stearothermophilus ATCC 12980 and sequencing and cloning of the sbsD Gene encoding the protein. Arch Microbiol 177 : 70 80.
    • (2001) Arch Microbiol , vol.177 , pp. 70-80
    • Egelseer, E.M.1    Danhorn, T.2    Pleschberger, M.3    Hotzy, C.4    Sleytr, U.B.5    Sára, M.6
  • 14
    • 0032464347 scopus 로고    scopus 로고
    • Structural research on surface layers: A focus on stability, surface layer homology domains, and surface layer-cell wall interactions
    • DOI 10.1006/jsbi.1998.4070
    • Engelhardt, H. Peters, J. (1998) Structural research on surface layers: a focus on stability, surface layer homology domains, and surface layer-cell wall interactions. J Struct Biol 124 : 276 302. (Pubitemid 29143066)
    • (1998) Journal of Structural Biology , vol.124 , Issue.2-3 , pp. 276-302
    • Engelhardt, H.1    Peters, J.2
  • 15
    • 34948870365 scopus 로고    scopus 로고
    • High-affinity interaction between the S-layer protein SbsC and the secondary cell wall polymer of Geobacillus stearothermophilus ATCC
    • 12980 determined by surface plasmon resonance technology.
    • Ferner-Ortner, J., Mader, C., Ilk, N., Sleytr, U.B. Egelseer, E.M. (2007) High-affinity interaction between the S-layer protein SbsC and the secondary cell wall polymer of Geobacillus stearothermophilus ATCC 12980 determined by surface plasmon resonance technology. J Bacteriol 189 : 7154 7158.
    • (2007) J Bacteriol , vol.189 , pp. 7154-7158
    • Ferner-Ortner, J.1    Mader, C.2    Ilk, N.3    Sleytr, U.B.4    Egelseer, E.M.5
  • 16
    • 12344305653 scopus 로고    scopus 로고
    • The three S-layer-like homology motifs of the S-layer protein SbpA of Bacillus sphaericus CCM 2177 are not sufficient for binding to the pyruvylated secondary cell wall polymer
    • DOI 10.1111/j.1365-2958.2004.04351.x
    • Huber, C., Ilk, N., Rünzler, D., Egelseer, E.M., Weigert, S., Sleytr, U.B. Sára, M. (2005) The three S-layer-like homology motifs of the S-layer protein SbpA of Bacillus sphaericus CCM 2177 are not sufficient for binding to the pyruvylated secondary cell wall polymer. Mol Microbiol 55 : 197 205. (Pubitemid 40127896)
    • (2005) Molecular Microbiology , vol.55 , Issue.1 , pp. 197-205
    • Huber, C.1    Ilk, N.2    Runzler, D.3    Egelseer, E.M.4    Weigert, S.5    Sleytr, U.B.6    Sara, M.7
  • 17
    • 0032786249 scopus 로고    scopus 로고
    • Structural and functional analyses of the secondary cell wall polymer of Bacillus sphaericus CCM 2177 that serves as an S-layer-specific anchor
    • Ilk, N., Kosma, P., Puchberger, M., Egelseer, E.M., Mayer, H.F., Sleytr, U.B. Sára, M. (1999) Structural and functional analyses of the secondary cell wall polymer of Bacillus sphaericus CCM 2177 that serves as an S-layer-specific anchor. J Bacteriol 181 : 7643 7646.
    • (1999) J Bacteriol , vol.181 , pp. 7643-7646
    • Ilk, N.1    Kosma, P.2    Puchberger, M.3    Egelseer, E.M.4    Mayer, H.F.5    Sleytr, U.B.6    Sára, M.7
  • 18
    • 0036308492 scopus 로고    scopus 로고
    • Molecular characterization of the S-layer gene, sbpA, of Bacillus sphaericus CCM 2177 and production of a functional S-layer fusion protein with the ability to recrystallize in a defined orientation while presenting the fused allergen
    • DOI 10.1128/AEM.68.7.3251-3260.2002
    • Ilk, N., Völlenkle, C., Egelseer, E.M., Breitwieser, A., Sleytr, U.B. Sára, M. (2002) Molecular characterization of the S-layer gene, sbpA, of Bacillus sphaericus CCM 2177 and production of a functional S-layer fusion protein with the ability to recrystallize in a defined orientation while presenting the fused allergen. Appl Environ Microbiol 68 : 3251 3260. (Pubitemid 34734018)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.7 , pp. 3251-3260
    • Ilk, N.1    Vollenkle, C.2    Egelseer, E.M.3    Breitwieser, A.4    Sleytr, U.B.5    Sara, M.6
  • 19
    • 0033975875 scopus 로고    scopus 로고
    • S-layer gene sbsC of Bacillus stearothermophilus ATCC
    • 12980: molecular characterization and heterologous expression in Escherichia coli.
    • Jarosch, M., Egelseer, E.M., Mattanovich, D., Sleytr, U.B. Sára, M. (2000) S-layer gene sbsC of Bacillus stearothermophilus ATCC 12980: molecular characterization and heterologous expression in Escherichia coli. Microbiology 146 (Part 2 273 281.
    • (2000) Microbiology , vol.146 , Issue.PART 2 , pp. 273-281
    • Jarosch, M.1    Egelseer, E.M.2    Mattanovich, D.3    Sleytr, U.B.4    Sára, M.5
  • 20
    • 0034998889 scopus 로고    scopus 로고
    • Analysis of the structure-function relationship of the S-layer protein SbsC of Bacillus stearothermophilus ATCC
    • 12980 by producing truncated forms.
    • Jarosch, M., Egelseer, E.M., Huber, C., Moll, D., Mattanovich, D., Sleytr, U.B. Sára, M. (2001) Analysis of the structure-function relationship of the S-layer protein SbsC of Bacillus stearothermophilus ATCC 12980 by producing truncated forms. Microbiology 147 : 1353 1363.
    • (2001) Microbiology , vol.147 , pp. 1353-1363
    • Jarosch, M.1    Egelseer, E.M.2    Huber, C.3    Moll, D.4    Mattanovich, D.5    Sleytr, U.B.6    Sára, M.7
  • 21
    • 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
  • 22
    • 0028262129 scopus 로고
    • Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis
    • Lupas, A., Engelhardt, H., Peters, J., Santarius, U., Volker, S. Baumeister, W. (1994) Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis. J Bacteriol 176 : 1224 1233. (Pubitemid 24080034)
    • (1994) Journal of Bacteriology , vol.176 , Issue.5 , pp. 1224-1233
    • Lupas, A.1    Engelhardt, H.2    Peters, J.3    Santarius, U.4    Volker, S.5    Baumeister, W.6
  • 23
    • 1542346915 scopus 로고    scopus 로고
    • Interaction of the Crystalline Bacterial Cell Surface Layer Protein SbsB and the Secondary Cell Wall Polymer of Geobacillus stearothermophilus PV72 Assessed by Real-Time Surface Plasmon Resonance Biosensor Technology
    • DOI 10.1128/JB.186.6.1758-1768.2004
    • Mader, C., Huber, C., Moll, D., Sleytr, U.B. Sára, M. (2004) Interaction of the crystalline bacterial cell surface layer protein SbsB and the secondary cell wall polymer of Geobacillus stearothermophilus PV72 assessed by real-time surface plasmon resonance biosensor technology. J Bacteriol 186 : 1758 1768. (Pubitemid 38324528)
    • (2004) Journal of Bacteriology , vol.186 , Issue.6 , pp. 1758-1768
    • Mader, C.1    Huber, C.2    Moll, D.3    Sleytr, U.B.4    Sara, M.5
  • 24
    • 33645965876 scopus 로고    scopus 로고
    • Mutagenesis of conserved charged amino acids in SLH domains of Thermoanaerobacterium thermosulfurigenes EM1 affects attachment to cell wall sacculi
    • May, A., Pusztahelyi, T., Hoffmann, N., Fischer, R.J. Bahl, H. (2006) Mutagenesis of conserved charged amino acids in SLH domains of Thermoanaerobacterium thermosulfurigenes EM1 affects attachment to cell wall sacculi. Arch Microbiol 185 : 263 269.
    • (2006) Arch Microbiol , vol.185 , pp. 263-269
    • May, A.1    Pusztahelyi, T.2    Hoffmann, N.3    Fischer, R.J.4    Bahl, H.5
  • 25
    • 0021261426 scopus 로고
    • Paracrystalline cell wall surface layers of different Bacillus stearothermophilus strains
    • Messner, P., Hollaus, F. Sleytr, U.B. (1984) Paracrystalline cell wall surface layers of different Bacillus stearothermophilus strains. Int J Syst Bacteriol 34 : 202 210. (Pubitemid 14103610)
    • (1984) International Journal of Systematic Bacteriology , vol.34 , Issue.2 , pp. 202-210
    • Messner, P.1    Hollaus, F.2    Sleytr, U.B.3
  • 26
    • 0035064602 scopus 로고    scopus 로고
    • Taxonomic study of aerobic thermophilic bacilli: Descriptions of Geobacillus subterraneus gen. nov., sp. nov. and Geobacillus uzenensis sp. nov. from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans, Bacillus kaustophilus, Bacillus thermodenitrificans to Geobacillus as the new combinations G. stearothermophilus, G. th
    • Nazina, T.N., Tourova, T.P., Poltaraus, A.B., Novikova, E.V., Grigoryan, A.A., Ivanova, A.E., et al. (2001) Taxonomic study of aerobic thermophilic bacilli: descriptions of Geobacillus subterraneus gen. nov., sp. nov. and Geobacillus uzenensis sp. nov. from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans, Bacillus kaustophilus, Bacillus thermodenitrificans to Geobacillus as the new combinations G. stearothermophilus, G. th. Int J Syst Evol Microbiol 51 : 433 446.
    • (2001) Int J Syst Evol Microbiol , vol.51 , pp. 433-446
    • Nazina, T.N.1    Tourova, T.P.2    Poltaraus, A.B.3    Novikova, E.V.4    Grigoryan, A.A.5    Ivanova, A.E.6
  • 27
    • 48149095082 scopus 로고    scopus 로고
    • The structure and binding behavior of the bacterial cell surface layer protein SbsC
    • Pavkov, T., Egelseer, E.M., Tesarz, M., Svergun, D.I., Sleytr, U.B. Keller, W. (2008) The structure and binding behavior of the bacterial cell surface layer protein SbsC. Structure 16 : 1226 1237.
    • (2008) Structure , vol.16 , pp. 1226-1237
    • Pavkov, T.1    Egelseer, E.M.2    Tesarz, M.3    Svergun, D.I.4    Sleytr, U.B.5    Keller, W.6
  • 28
    • 0031010863 scopus 로고    scopus 로고
    • Evidence that the N-terminal part of the S-layer protein from Bacillus stearothermophilus PV72/p2 recognizes a secondary cell wall polymer
    • Ries, W., Hotzy, C., Schocher, I., Sleytr, U.B. Sára, M. (1997) Evidence that the N-terminal part of the S-layer protein from Bacillus stearothermophilus PV72/p2 recognizes a secondary cell wall polymer. J Bacteriol 179 : 3892 3898. (Pubitemid 27259907)
    • (1997) Journal of Bacteriology , vol.179 , Issue.12 , pp. 3892-3898
    • Ries, W.1    Hotzy, C.2    Schocker, I.3    Sleytr, U.B.4    Sara, M.5
  • 29
    • 0031781285 scopus 로고    scopus 로고
    • Identification and analysis of a gene (abpA) encoding a major amylase-binding protein in Streptococcus gordonii
    • Rogers, J.D., Haase, E.M., Brown, A.E., Douglas, C.W., Gwynn, J.P. Scannapieco, F.A. (1998) Identification and analysis of a gene (abpA) encoding a major amylase-binding protein in Streptococcus gordonii. Microbiology 144 (Part 5 1223 1233. (Pubitemid 28233826)
    • (1998) Microbiology , vol.144 , Issue.5 , pp. 1223-1233
    • Rogers, J.D.1    Haase, E.M.2    Brown, A.E.3    Douglas, C.W.I.4    Gwynn, J.P.5    Scannapieco, F.A.6
  • 30
    • 1242339692 scopus 로고    scopus 로고
    • Biophysical Characterization of the Entire Bacterial Surface Layer Protein SbsB and Its Two Distinct Functional Domains
    • DOI 10.1074/jbc.M308819200
    • Rünzler, D., Huber, C., Moll, D., Köhler, G. Sára, M. (2004) Biophysical characterization of the entire bacterial surface layer protein SbsB and its two distinct functional domains. J Biol Chem 279 : 5207 5215. (Pubitemid 38220539)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5207-5215
    • Runzler, D.1    Huber, C.2    Moll, D.3    Kohler, G.4    Sara, M.5
  • 31
    • 0028271237 scopus 로고
    • Subcellular localization of Clostridium thermocellum ORF3p, a protein carrying a receptor for the docking sequence borne by the catalytic components of the cellulosome
    • Salamitou, S., Lemaire, M., Fujino, T., Ohayon, H., Gounon, P., Beguin, P. Aubert, J.P. (1994) Subcellular localization of Clostridium thermocellum ORF3p, a protein carrying a receptor for the docking sequence borne by the catalytic components of the cellulosome. J Bacteriol 176 : 2828 2834. (Pubitemid 24152926)
    • (1994) Journal of Bacteriology , vol.176 , Issue.10 , pp. 2828-2834
    • Salamitou, S.1    Lemaire, M.2    Fujino, T.3    Ohayon, H.4    Gounon, P.5    Beguin, P.6    Aubert -, J.P.7
  • 32
    • 0017681196 scopus 로고
    • DNA sequencing with chain-terminating inhibitors
    • Sanger, F., Nicklen, S. Coulson, A.R. (1977) DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74 : 5463 5467.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5463-5467
    • Sanger, F.1    Nicklen, S.2    Coulson, A.R.3
  • 33
    • 0035253107 scopus 로고    scopus 로고
    • Conserved anchoring mechanisms between crystalline cell surface S-layer proteins and secondary cell wall polymers in Gram-positive bacteria?
    • DOI 10.1016/S0966-842X(00)01905-3, PII S0966842X00019053
    • Sára, M. (2001) Conserved anchoring mechanisms between crystalline cell surface S-layer proteins and secondary cell wall polymers in Gram-positive bacteria? Trends Microbiol 9 : 47 49. (Pubitemid 32155315)
    • (2001) Trends in Microbiology , vol.9 , Issue.2 , pp. 47-49
    • Sara, M.1
  • 34
    • 0028171373 scopus 로고
    • Comparative studies of S-layer proteins from Bacillus stearothermophilus strains expressed during growth in continuous culture under oxygen-limited and non-oxygen-limited conditions
    • Sára, M. Sleytr, U.B. (1994) Comparative studies of S-layer proteins from Bacillus stearothermophilus strains expressed during growth in continuous culture under oxygen-limited and non-oxygen-limited conditions. J Bacteriol 176 : 7182 7189. (Pubitemid 24364043)
    • (1994) Journal of Bacteriology , vol.176 , Issue.23 , pp. 7182-7189
    • Sara, M.1    Sleytr, U.B.2
  • 35
    • 0033984760 scopus 로고    scopus 로고
    • S-layer proteins
    • DOI 10.1128/JB.182.4.859-868.2000
    • Sára, M. Sleytr, U.B. (2000) S-layer proteins. J Bacteriol 182 : 859 868. (Pubitemid 30075004)
    • (2000) Journal of Bacteriology , vol.182 , Issue.4 , pp. 859-868
    • Sara, M.1    Sleytr, U.B.2
  • 36
    • 0026680440 scopus 로고
    • Permeability and charge-dependent adsorption properties of the S-layer lattice from Bacillus coagulans E38-66
    • Sára, M., Pum, D. Sleytr, U.B. (1992) Permeability and charge-dependent adsorption properties of the S-layer lattice from Bacillus coagulans E38-66. J Bacteriol 174 : 3487 3493.
    • (1992) J Bacteriol , vol.174 , pp. 3487-3493
    • Sára, M.1    Pum, D.2    Sleytr, U.B.3
  • 37
    • 0029876584 scopus 로고    scopus 로고
    • Dynamics in oxygen-induced changes in S-layer protein synthesis from Bacillus stearothermophilus PV72 and the S-layer-deficient variant T5 in continuous culture and studies of the cell wall composition
    • Sára, M., Kuen, B., Mayer, H.F., Mandl, F., Schuster, K.C. Sleytr, U.B. (1996) Dynamics in oxygen-induced changes in S-layer protein synthesis from Bacillus stearothermophilus PV72 and the S-layer-deficient variant T5 in continuous culture and studies of the cell wall composition. J Bacteriol 178 : 2108 2117.
    • (1996) J Bacteriol , vol.178 , pp. 2108-2117
    • Sára, M.1    Kuen, B.2    Mayer, H.F.3    Mandl, F.4    Schuster, K.C.5    Sleytr, U.B.6
  • 38
    • 15844394070 scopus 로고    scopus 로고
    • The structure of secondary cell wall polymers: How Gram-positive bacteria stick their cell walls together
    • DOI 10.1099/mic.0.27749-0
    • Schäffer, C. Messner, P. (2005) The structure of secondary cell wall polymers: how Gram-positive bacteria stick their cell walls together. Microbiology 151 : 643 651. (Pubitemid 40425000)
    • (2005) Microbiology , vol.151 , Issue.3 , pp. 643-651
    • Schaffer, C.1    Messner, P.2
  • 39
    • 0032799160 scopus 로고    scopus 로고
    • The diacetamidodideoxyuronic-acid-containing glycan chain of Bacillus stearothermophilus NRS 2004/3a represents the secondary cell-wall polymer of wild-type B. stearothermophilus strains
    • Schäffer, C., Kahlig, H., Christian, R., Schulz, G., Zayni, S. Messner, P. (1999) The diacetamidodideoxyuronic-acid-containing glycan chain of Bacillus stearothermophilus NRS 2004/3a represents the secondary cell-wall polymer of wild-type B. stearothermophilus strains. Microbiology 145 : 1575 1583. (Pubitemid 29352001)
    • (1999) Microbiology , vol.145 , Issue.7 , pp. 1575-1583
    • Schaffer, C.1    Kahlig, H.2    Christian, R.3    Schulz, G.4    Zayni, S.5    Messner, P.6
  • 40
    • 0033870741 scopus 로고    scopus 로고
    • The transposable element IS4712 prevents S-layer gene (sbsA) expression in Bacillus stearothermophilus and also affects the synthesis of altered surface layer proteins
    • DOI 10.1007/s002030000181, PII S002030000181
    • Scholz, H., Hummel, S., Witte, A., Lubitz, W. Kuen, B. (2000) The transposable element IS4712 prevents S-layer gene (sbsA) expression in Bacillus stearothermophilus and also affects the synthesis of altered surface layer proteins. Arch Microbiol 174 : 97 103. (Pubitemid 30627502)
    • (2000) Archives of Microbiology , vol.174 , Issue.1-2 , pp. 97-103
    • Scholz, H.1    Hummel, S.2    Witte, A.3    Lubitz, W.4    Kuen, B.5
  • 41
    • 0035117468 scopus 로고    scopus 로고
    • S-layer variation in Bacillus stearothermophilus PV72 is based on DNA rearrangements between the chromosome and the naturally occurring megaplasmids
    • DOI 10.1128/JB.183.5.1672-1679.2001
    • Scholz, H.C., Riedmann, E., Witte, A., Lubitz, W. Kuen, B. (2001) S-layer variation in Bacillus stearothermophilus PV72 is based on DNA rearrangements between the chromosome and the naturally occurring megaplasmids. J Bacteriol 183 : 1672 1679. (Pubitemid 32172310)
    • (2001) Journal of Bacteriology , vol.183 , Issue.5 , pp. 1672-1679
    • Scholz, H.C.1    Riedmann, E.2    Witte, A.3    Lubitz, W.4    Kuen, B.5
  • 42
    • 0033152613 scopus 로고    scopus 로고
    • Bacterial S-layers
    • DOI 10.1016/S0966-842X(99)01513-9, PII S0966842X99015139
    • Sleytr, U.B. Beveridge, T.J. (1999) Bacterial S-layers. Trends Microbiol 7 : 253 260. (Pubitemid 29317307)
    • (1999) Trends in Microbiology , vol.7 , Issue.6 , pp. 253-260
    • Sleytr, U.B.1    Beveridge, T.J.2
  • 43
  • 44
    • 0033583512 scopus 로고    scopus 로고
    • Crystalline bacterial cell surface layers (S-layers): From supramolecular cell structure to biomimetics and nanotechnology
    • Sleytr, U.B., Messner, P., Pum, D. Sára, M. (1999) Crystalline bacterial cell surface layers (S-layers): from supramolecular cell structure to biomimetics and nanotechnology. Angew Chem Int Ed Engl 38 : 1034 1054.
    • (1999) Angew Chem Int Ed Engl , vol.38 , pp. 1034-1054
    • Sleytr, U.B.1    Messner, P.2    Pum, D.3    Sára, M.4
  • 45
    • 0002877469 scopus 로고    scopus 로고
    • Molecular nanotechnology and nanobiotechnology with two-dimensional protein crystals (S-layers)
    • In. Rosoff, M. (ed.). New York - Basel. Marcel Dekker. pp.
    • Sleytr, U.B., Sára, M., Pum, D. Schuster, B. (2002) Molecular nanotechnology and nanobiotechnology with two-dimensional protein crystals (S-layers). In Nano-Surface Chemistry. Rosoff, M. (ed.). New York - Basel : Marcel Dekker, pp. 333 389.
    • (2002) Nano-Surface Chemistry. , pp. 333-389
    • Sleytr, U.B.1    Sára, M.2    Pum, D.3    Schuster, B.4
  • 47
    • 27944466452 scopus 로고    scopus 로고
    • Crystalline bacterial cell surface layers (S-layers): A versatile self-assembly system
    • In. Ciferri, A. (ed.). Boca Raton, FL. Taylor and Francis. pp.
    • Sleytr, U.B., Sára, M., Pum, D. Schuster, B. (2005) Crystalline bacterial cell surface layers (S-layers): a versatile self-assembly system. In Supramolecular Polymers. Ciferri, A. (ed.). Boca Raton, FL : Taylor and Francis, pp. 583 612.
    • (2005) Supramolecular Polymers. , pp. 583-612
    • Sleytr, U.B.1    Sára, M.2    Pum, D.3    Schuster, B.4
  • 48
    • 33846006521 scopus 로고    scopus 로고
    • S-Layers as a basic building block in a molecular construction kit
    • DOI 10.1111/j.1742-4658.2006.05606.x
    • Sleytr, U.B., Egelseer, E.M., Ilk, N., Pum, D. Schuster, B. (2007a) S-layers as a basic building block in a molecular construction kit. FEBS J 274 : 323 334. (Pubitemid 46046643)
    • (2007) FEBS Journal , vol.274 , Issue.2 , pp. 323-334
    • Sleytr, U.B.1    Egelseer, E.M.2    Ilk, N.3    Pum, D.4    Schuster, B.5
  • 49
    • 33846273815 scopus 로고    scopus 로고
    • S-layers as a tool kit for nanobiotechnological applications
    • DOI 10.1111/j.1574-6968.2006.00573.x
    • Sleytr, U.B., Huber, C., Ilk, N., Pum, D., Schuster, B. Egelseer, E.M. (2007b) S-layers as a tool kit for nanobiotechnological applications. FEMS Microbiol Lett 267 : 131 144. (Pubitemid 46114965)
    • (2007) FEMS Microbiology Letters , vol.267 , Issue.2 , pp. 131-144
    • Sleytr, U.B.1    Huber, C.2    Ilk, N.3    Pum, D.4    Schuster, B.5    Egelseer, E.M.6
  • 51
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of cloned genes
    • DOI 10.1016/0076-6879(90)85008-C
    • Studier, F.W., Rosenberg, A.H., Dunn, J.J. Dubendorff, J.W. (1990) Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol 185 : 60 89. (Pubitemid 20219811)
    • (1990) Methods in Enzymology , vol.185 , pp. 60-89
    • Studier, F.W.1    Rosenberg, A.H.2    Dunn, J.J.3    Dubendorff, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.