메뉴 건너뛰기




Volumn 49, Issue 3, 1998, Pages 321-327

Protein secretion in phosphate-limited cultures of Bacillus subtilis 168

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; MAGNESIUM; PHOSPHATE;

EID: 0031945604     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002530051176     Document Type: Article
Times cited : (7)

References (32)
  • 1
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagostopoulos C, Spizizen J (1961) Requirements for transformation in Bacillus subtilis. J Bacteriol 81: 741-746
    • (1961) J Bacteriol , vol.81 , pp. 741-746
    • Anagostopoulos, C.1    Spizizen, J.2
  • 3
    • 0023761756 scopus 로고
    • Transient association of newly synthesised unfolded proteins with the heatsock GroEL protein
    • Bochkareva ES, Lissin NM, Girshovich AS (1988) Transient association of newly synthesised unfolded proteins with the heatsock GroEL protein. Nature 336: 254-257
    • (1988) Nature , vol.336 , pp. 254-257
    • Bochkareva, E.S.1    Lissin, N.M.2    Girshovich, A.S.3
  • 4
    • 0019906163 scopus 로고
    • Cloning of the cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Escherichia coli
    • Edens L, Heslinga L, Klok R, Ledeboer AM, Maat J, Toonen MY, Visser C, Verrips CT (1982) Cloning of the cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Escherichia coli. Gene 18: 1-12
    • (1982) Gene , vol.18 , pp. 1-12
    • Edens, L.1    Heslinga, L.2    Klok, R.3    Ledeboer, A.M.4    Maat, J.5    Toonen, M.Y.6    Visser, C.7    Verrips, C.T.8
  • 5
    • 0029849654 scopus 로고    scopus 로고
    • A Bacillus subtilis secreted phosphodiesterase alkaline phosphatase is the product of a Pho reunlon gene, phoD
    • Eder S, Shi L, Jensen K, Yamane K, Hulett FM (1996) A Bacillus subtilis secreted phosphodiesterase alkaline phosphatase is the product of a Pho reunlon gene, phoD. Microbiology 142: 2041-2047
    • (1996) Microbiology , vol.142 , pp. 2041-2047
    • Eder, S.1    Shi, L.2    Jensen, K.3    Yamane, K.4    Hulett, F.M.5
  • 6
    • 0029905620 scopus 로고    scopus 로고
    • Phosphate-starvation-inducible proteins in Bacillus subtilis: A two-dimensional gel electrophoresis study
    • Eymann C, Mach H, Harwood CR and Hecker M (1996) Phosphate-starvation-inducible proteins in Bacillus subtilis: a two-dimensional gel electrophoresis study. Microbiology 142: 3163-3170
    • (1996) Microbiology , vol.142 , pp. 3163-3170
    • Eymann, C.1    Mach, H.2    Harwood, C.R.3    Hecker, M.4
  • 8
    • 0017342488 scopus 로고
    • Biochemical localisation of the alkaline phosphatase of Bacillus subtilis MC14 as a function of culture age
    • Glynn JA, Schaffel SD, McNicholas JM, Hulett FM (1977) Biochemical localisation of the alkaline phosphatase of Bacillus subtilis MC14 as a function of culture age. J Bacteriol 129: 1010-1019
    • (1977) J Bacteriol , vol.129 , pp. 1010-1019
    • Glynn, J.A.1    Schaffel, S.D.2    McNicholas, J.M.3    Hulett, F.M.4
  • 9
    • 0021183555 scopus 로고
    • Specificity of subcellular distribution of alkaline phosphatase in Bacillus subtilis 749/C
    • Ghosh A, Vallespir S, Ghosh BK (1883) Specificity of subcellular distribution of alkaline phosphatase in Bacillus subtilis 749/C. Can J Microbiol 30: 113-125
    • (1883) Can J Microbiol , vol.30 , pp. 113-125
    • Ghosh, A.1    Vallespir, S.2    Ghosh, B.K.3
  • 10
    • 0026752273 scopus 로고
    • Bacillus subtilis and its relatives: Molecular biological and industrial workhorses
    • Harwood CR (1992) Bacillus subtilis and its relatives: molecular biological and industrial workhorses. Trends Biotechnol 10: 247-256
    • (1992) Trends Biotechnol , vol.10 , pp. 247-256
    • Harwood, C.R.1
  • 11
    • 0026714390 scopus 로고
    • Improving the production of E. col: β-lactamase in Bacillus subtilis: The effect of glucose, pH and temperature on the production level
    • Hemilä H, Pokkinen M, Palva I (1992) Improving the production of E. col: β-lactamase in Bacillus subtilis: the effect of glucose, pH and temperature on the production level. J Biotechnol 26: 245-256
    • (1992) J Biotechnol , vol.26 , pp. 245-256
    • Hemilä, H.1    Pokkinen, M.2    Palva, I.3
  • 13
    • 0025977645 scopus 로고
    • Bacillus subtilis alkaline phosphatases III and IV: Cloning, sequencing, and comparison of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure
    • Hulett FM, Kim EE, Bookstein C, Kapp NV, Edwards CW, Wyckoff HW (1991) Bacillus subtilis alkaline phosphatases III and IV: cloning, sequencing, and comparison of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure. J Biol Chem 266: 1077-1084
    • (1991) J Biol Chem , vol.266 , pp. 1077-1084
    • Hulett, F.M.1    Kim, E.E.2    Bookstein, C.3    Kapp, N.V.4    Edwards, C.W.5    Wyckoff, H.W.6
  • 15
    • 0028203258 scopus 로고
    • Sequential action of two-component genetic switches regulates the PHO regulon in Bacillus subtilis
    • Hulett FM, Lee J, Shi L, Sun G, Chestnut R, Sharkova E, Duggan MF, Kapp NV (1994b) Sequential action of two-component genetic switches regulates the PHO regulon in Bacillus subtilis. J Bacteriol 176: 1348-1358
    • (1994) J Bacteriol , vol.176 , pp. 1348-1358
    • Hulett, F.M.1    Lee, J.2    Shi, L.3    Sun, G.4    Chestnut, R.5    Sharkova, E.6    Duggan, M.F.7    Kapp, N.V.8
  • 16
    • 0027264910 scopus 로고
    • Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesised either with or without prosequences
    • Jacobs M, Anderson JB, Kontinen V, Sarvas M (1993) Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesised either with or without prosequences. Mol Microbiol 8: 957-966
    • (1993) Mol Microbiol , vol.8 , pp. 957-966
    • Jacobs, M.1    Anderson, J.B.2    Kontinen, V.3    Sarvas, M.4
  • 17
    • 0027513153 scopus 로고
    • Lysine 106 of the putative catalytic binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli sec A mutants in vivo
    • Klose M, Schimz K-L, van der Wolk J, Driessen AJ, Freudl R (1993) Lysine 106 of the putative catalytic binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli sec A mutants in vivo. J Biol Chem 268: 4504-4510
    • (1993) J Biol Chem , vol.268 , pp. 4504-4510
    • Klose, M.1    Schimz, K.-L.2    Van Der Wolk, J.3    Driessen, A.J.4    Freudl, R.5
  • 18
    • 0024461843 scopus 로고
    • Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli
    • Kusukawa N, Yura T, Ueguchi C, Akiyama Y, Ito K (1989) Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli. EMBO J 8: 3517-3521
    • (1989) EMBO J , vol.8 , pp. 3517-3521
    • Kusukawa, N.1    Yura, T.2    Ueguchi, C.3    Akiyama, Y.4    Ito, K.5
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 20
    • 0025291463 scopus 로고
    • The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the β-lactamase precursor
    • Laminet AA, Ziegelhoffer T, Georgopoulos C, Plückthun A (1990) The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the β-lactamase precursor. EMBO J 9: 2315-2319
    • (1990) EMBO J , vol.9 , pp. 2315-2319
    • Laminet, A.A.1    Ziegelhoffer, T.2    Georgopoulos, C.3    Plückthun, A.4
  • 21
    • 0024544714 scopus 로고
    • Cell wall assembly in Bacillus subtilis: Visualization of the old and new material by electron microscopic examination of samples stained selectively for teichoic acid and teichuronic acid
    • Merad T, Archibald AR, Hancock IC, Harwood CR, Hobot JA (1989) Cell wall assembly in Bacillus subtilis: visualization of the old and new material by electron microscopic examination of samples stained selectively for teichoic acid and teichuronic acid. J Gen Microbiol 135: 645-655
    • (1989) J Gen 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
  • 22
    • 0141742610 scopus 로고    scopus 로고
    • The influence of Bacillus subtilis pho R on cell wall anionic polymers
    • Müller JP, An Z, Merad T, Hancock IC, Harwood CR (1997) The influence of Bacillus subtilis pho R on cell wall anionic polymers. Microbiology 143: 947-956
    • (1997) Microbiology , vol.143 , pp. 947-956
    • Müller, J.P.1    An, Z.2    Merad, T.3    Hancock, I.C.4    Harwood, C.R.5
  • 23
    • 0021819750 scopus 로고
    • Stable hyper-production of Escherichia coli β-lactamase by Bacillus subtilis grown on a 0.5 M succinate-medium using a B subtilis a-amylase secretion vector
    • Nakamura K, Furusato T, Shiroza T, Yamane K (1985) Stable hyper-production of Escherichia coli β-lactamase by Bacillus subtilis grown on a 0.5 M succinate-medium using a B subtilis a-amylase secretion vector. Biochem Biophys Res Commun 128: 601-606
    • (1985) Biochem Biophys Res Commun , vol.128 , pp. 601-606
    • Nakamura, K.1    Furusato, T.2    Shiroza, T.3    Yamane, K.4
  • 24
    • 0025336259 scopus 로고
    • SecA protein: Autoregulated initiator of secretory precursor protein translocation across the E. coli plasma membrane
    • Oliver DB, Cabelli RJ, Jarosik GP (1990) SecA protein: autoregulated initiator of secretory precursor protein translocation across the E. coli plasma membrane. J Bioenerg Biomembr 22: 311-336
    • (1990) J Bioenerg Biomembr , vol.22 , pp. 311-336
    • Oliver, D.B.1    Cabelli, R.J.2    Jarosik, G.P.3
  • 26
    • 0023192483 scopus 로고
    • Cloning and nucleotide sequence of phoP. the regulatory gene for alkaline phosphatase and phosphodiesterase in Bacillus subtilis
    • Seki T, Yoshikawa H, Takahashi H, Saito H (1987) Cloning and nucleotide sequence of phoP. the regulatory gene for alkaline phosphatase and phosphodiesterase in Bacillus subtilis. J Bacteriol 169: 2913-2916
    • (1987) J Bacteriol , vol.169 , pp. 2913-2916
    • Seki, T.1    Yoshikawa, H.2    Takahashi, H.3    Saito, H.4
  • 27
    • 0020691610 scopus 로고
    • Fluorographic detection of radioactivity in polyacrylamide gels with 2.5-diphenyloxazole in acetic acid and its comparison with existing procedures
    • Skinner MK, Griswold MD (1983) Fluorographic detection of radioactivity in polyacrylamide gels with 2.5-diphenyloxazole in acetic acid and its comparison with existing procedures. Biochem J 209: 81-284
    • (1983) Biochem J , vol.209 , pp. 81-284
    • Skinner, M.K.1    Griswold, M.D.2
  • 29
    • 0029839845 scopus 로고    scopus 로고
    • A Bacillus subtilis gene cluster similar to the Escherichia coli phosphate-specific transport (pst) operon: Evidence for a tandemly arranged pst B gene
    • Takemaru K, Mizuno M, Kobayashi Y (1996) A Bacillus subtilis gene cluster similar to the Escherichia coli phosphate-specific transport (pst) operon: evidence for a tandemly arranged pst B gene. Microbiology 142: 2017-2020
    • (1996) Microbiology , vol.142 , pp. 2017-2020
    • Takemaru, K.1    Mizuno, M.2    Kobayashi, Y.3
  • 30
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76: 4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 31
    • 0026772152 scopus 로고
    • Signal peptidase I of Bacillus subtilis: Patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases
    • van Dijl JM, de Jong A, Vehmaanperä J, Venema G, Bron S (1992) Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases. EMBO J 11: 2819-2828
    • (1992) EMBO J , vol.11 , pp. 2819-2828
    • Dijl, J.M.1    De Jong, A.2    Vehmaanperä, J.3    Venema, G.4    Bron, S.5
  • 32
    • 0017847680 scopus 로고
    • Alkaline phosphatase processing alkaline phosphodiesterase activity and other phosphodiesterases in Bacillus subtilis
    • Yamane K, Maruo B (1978) Alkaline phosphatase processing alkaline phosphodiesterase activity and other phosphodiesterases in Bacillus subtilis. J Bacteriol 134: 108-114
    • (1978) J Bacteriol , vol.134 , pp. 108-114
    • Yamane, K.1    Maruo, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.