메뉴 건너뛰기




Volumn 18, Issue 2, 2000, Pages 242-248

Staphylococcal protein A as a fusion partner directs secretion of the E1α and E1β subunits of pea mitochondrial pyruvate dehydrogenase by Bacillus subtilis

Author keywords

Bacillus subtilis; Protein association; Pyruvate dehydrogenase; Secretion; Staphlococcal protein A

Indexed keywords

AMINO TERMINAL SEQUENCE; BINDING SITE; CELL SECRETION; ENZYME SUBUNIT; EXPRESSION VECTOR; GENE INSERTION; GENETIC TRANSFORMATION; HYBRID PROTEIN; MITOCHONDRION; OPEN READING FRAME; PLASMID; PROTEIN PROTEIN INTERACTION; PROTEIN SYNTHESIS; PYRUVATE DEHYDROGENASE; SIGNAL PEPTIDE; STAPHYLOCOCCUS PROTEIN A;

EID: 0034067488     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1175     Document Type: Article
Times cited : (6)

References (29)
  • 1
    • 2642644904 scopus 로고
    • Multienzyme complexes
    • Reed L. J. Multienzyme complexes. Acc. Chem. Res. 7:1974;40-46.
    • (1974) Acc. Chem. Res. , vol.7 , pp. 40-46
    • Reed, L.J.1
  • 4
    • 0025362617 scopus 로고
    • Fusions to staphylococcal protein A
    • Nilsson B., Abrahmsén L. Fusions to staphylococcal protein A. Methods Enzymol. 185:1990;144-161.
    • (1990) Methods Enzymol. , vol.185 , pp. 144-161
    • Nilsson, B.1    Abrahmsén, L.2
  • 5
    • 0027403836 scopus 로고
    • Expression and functional analysis of steroid receptor fragments secreted from Staphylococcus aureus
    • Cao X., Preiss T., Slater E. P., Westphal H. M., Beato M. J. Expression and functional analysis of steroid receptor fragments secreted from Staphylococcus aureus. Steroid Biochem. Mol. Biol. 44:1993;1-11.
    • (1993) Steroid Biochem. Mol. Biol. , vol.44 , pp. 1-11
    • Cao, X.1    Preiss, T.2    Slater, E.P.3    Westphal, H.M.4    Beato, M.J.5
  • 6
    • 0011292514 scopus 로고
    • Efficient expression of a Trypanosoma cruzi antigen in Escherichia coli and Staphylococcus aureus and its rapid purification
    • Moreno J. I., Segelchifer M., Zorzopulos J. Efficient expression of a Trypanosoma cruzi antigen in Escherichia coli and Staphylococcus aureus and its rapid purification. World J. Microbiol. Biotechnol. 7:1991;316-323.
    • (1991) World J. Microbiol. Biotechnol. , vol.7 , pp. 316-323
    • Moreno, J.I.1    Segelchifer, M.2    Zorzopulos, J.3
  • 7
    • 0030293074 scopus 로고    scopus 로고
    • A Trypanosoma cruzi polyantigen obtained by gene fusion: Its expression in Staphylococcus aureus and rapid purification
    • Moreno J. I. A Trypanosoma cruzi polyantigen obtained by gene fusion: Its expression in Staphylococcus aureus and rapid purification. Protein Expression Purif. 8:1996;322-340.
    • (1996) Protein Expression Purif. , vol.8 , pp. 322-340
    • Moreno, J.I.1
  • 9
    • 0023504685 scopus 로고
    • Engineering for protein secretion in gram-positive bacteria
    • Chang S. Engineering for protein secretion in gram-positive bacteria. Methods Enzymol. 153:1987;507-516.
    • (1987) Methods Enzymol. , vol.153 , pp. 507-516
    • Chang, S.1
  • 11
    • 0028842609 scopus 로고
    • Advances in the use of Bacillus subtilis for the expression and secretion of heterologous proteins
    • Wong S.-L. Advances in the use of Bacillus subtilis for the expression and secretion of heterologous proteins. Curr. Opin. Biotechnol. 6:1995;517-522.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 517-522
    • Wong, S.-L.1
  • 12
    • 0027401020 scopus 로고
    • Protein secretion in Bacillus species
    • Simonen M., Palva I. Protein secretion in Bacillus species. Microbiol. Rev. 57:1993;109-137.
    • (1993) Microbiol. Rev. , vol.57 , pp. 109-137
    • Simonen, M.1    Palva, I.2
  • 13
    • 0026338822 scopus 로고
    • Engineering a Bacillus subtilis expression-secretion system with a strain deficient in six extracellular proteases
    • Wu X. C., Lee W., Tran L., Wong S.-L. Engineering a Bacillus subtilis expression-secretion system with a strain deficient in six extracellular proteases. J. Bacteriol. 173:1991;4952-4958.
    • (1991) J. Bacteriol. , vol.173 , pp. 4952-4958
    • Wu, X.C.1    Lee, W.2    Tran, L.3    Wong, S.-L.4
  • 14
    • 0024344452 scopus 로고
    • Expression of the MuIFN alpha 7 gene in Bacillus subtilis using the levansucrase system
    • Dion M., Rapoport G., Doly J. Expression of the MuIFN alpha 7 gene in Bacillus subtilis using the levansucrase system. Biochimie. 71:1989;747-755.
    • (1989) Biochimie , vol.71 , pp. 747-755
    • Dion, M.1    Rapoport, G.2    Doly, J.3
  • 16
    • 0022445340 scopus 로고
    • Expression of the staphylococcal protein A gene in Bacillus subtilis by gene fusions utilizing the promoter from a Bacillus amyloliquefaciens alpha-amylase gene
    • Fahnestock S. R., Fisher K. E. Expression of the staphylococcal protein A gene in Bacillus subtilis by gene fusions utilizing the promoter from a Bacillus amyloliquefaciens alpha-amylase gene. J. Bacteriol. 165:1986;796-804.
    • (1986) J. Bacteriol. , vol.165 , pp. 796-804
    • Fahnestock, S.R.1    Fisher, K.E.2
  • 17
    • 0024305946 scopus 로고
    • Development of an inducible and enhancible expression and secretion system in Bacillus subtilis
    • Wong S.-L. Development of an inducible and enhancible expression and secretion system in Bacillus subtilis. Gene. 83:1989;215-223.
    • (1989) Gene , vol.83 , pp. 215-223
    • Wong, S.-L.1
  • 19
    • 0017698858 scopus 로고
    • Zinc is associated with the beta subunit of DNA-dependent RNA polymerase of Bacillus subtilis
    • Halling S. M., Sanchez-Anzaldo F. J., Fukuda R., Doi R. H., Meares C. F. Zinc is associated with the beta subunit of DNA-dependent RNA polymerase of Bacillus subtilis. Biochemistry. 16:1977;2880-2884.
    • (1977) Biochemistry , vol.16 , pp. 2880-2884
    • Halling, S.M.1    Sanchez-Anzaldo, F.J.2    Fukuda, R.3    Doi, R.H.4    Meares, C.F.5
  • 21
    • 0001615271 scopus 로고
    • Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate
    • Spizizen J. Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate. Proc. Natl. Acad. Sci. USA. 44:1958;1072-1078.
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 1072-1078
    • Spizizen, J.1
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0029105760 scopus 로고
    • Characterization of a monoclonal antibody recognizing the E1α subunit of the plant mitochondrial pyruvate dehydrogenase
    • Luethy M. H., David N. R., Elthon T. E., Miernyk J. A., Randall D. D. Characterization of a monoclonal antibody recognizing the E1α subunit of the plant mitochondrial pyruvate dehydrogenase. J. Plant Physiol. 145:1995;443-449.
    • (1995) J. Plant Physiol. , vol.145 , pp. 443-449
    • Luethy, M.H.1    David, N.R.2    Elthon, T.E.3    Miernyk, J.A.4    Randall, D.D.5
  • 24
    • 0024506471 scopus 로고
    • Secretion of recombinant proteins into the culture medium by Escherichia coli and Staphylococcus aureus
    • Uhlén M., Abrahmsén L. Secretion of recombinant proteins into the culture medium by Escherichia coli and Staphylococcus aureus. Biochem. Soc. Trans. 2:1989;340-341.
    • (1989) Biochem. Soc. Trans. , vol.2 , pp. 340-341
    • Uhlén, M.1    Abrahmsén, L.2
  • 25
    • 0001173681 scopus 로고
    • The mitochondrial pyruvate dehydrogenase complex
    • Randall D. D., Miernyk J. A. The mitochondrial pyruvate dehydrogenase complex. Methods Plant Biochem. 3:1990;175-192.
    • (1990) Methods Plant Biochem. , vol.3 , pp. 175-192
    • Randall, D.D.1    Miernyk, J.A.2
  • 26
    • 0026679757 scopus 로고
    • Characterization of the secretion efficiency of a plant signal peptide in Bacillus subtilis
    • Ribbe J., Nagarajan V. Characterization of the secretion efficiency of a plant signal peptide in Bacillus subtilis. Mol. Gen. Genet. 235:1992;333-339.
    • (1992) Mol. Gen. Genet. , vol.235 , pp. 333-339
    • Ribbe, J.1    Nagarajan, V.2
  • 27
    • 0023150174 scopus 로고
    • Protease-deficient Bacillus subtilis host strains for production of Staphylococcal protein A
    • Fahnestock S. R., Fisher K. E. Protease-deficient Bacillus subtilis host strains for production of Staphylococcal protein A. Appl. Environ. Microbiol. 53:1987;379-384.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 379-384
    • Fahnestock, S.R.1    Fisher, K.E.2
  • 28
    • 0344457370 scopus 로고    scopus 로고
    • Protein secretion and possible roles for multiple signal peptidases for precursor processing in bacilli
    • Bron S., Bolhuis A., Tjalsma H., Holsappel S., Venema G., van Dijl J. M. Protein secretion and possible roles for multiple signal peptidases for precursor processing in bacilli. J. Biotechnol. 17:1998;3-13.
    • (1998) J. Biotechnol. , vol.17 , pp. 3-13
    • Bron, S.1    Bolhuis, A.2    Tjalsma, H.3    Holsappel, S.4    Venema, G.5    Van Dijl, J.M.6
  • 29
    • 0027989306 scopus 로고
    • Production of an enzymatically active E1 component of human pyruvate dehydrogenase complex in Escherichia coli: Supporting role of E1β subunit in E1 activity
    • Jeng J., Huh T.-L., Song B. J. Production of an enzymatically active E1 component of human pyruvate dehydrogenase complex in Escherichia coli: Supporting role of E1β subunit in E1 activity. Biochem. Biophys. Res. Commun. 203:1994;225-230.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 225-230
    • Jeng, J.1    Huh, T.-L.2    Song, B.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.