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Volumn 267, Issue 3, 2000, Pages 901-909

Engineering a disulfide bond and free thiols in the lantibiotic nisin Z

Author keywords

Cysteine; Lactococcus lactis; Mutagenesis; Nisin; Protein engineering

Indexed keywords

AMINO ACID; CYSTEINE; DISULFIDE; IODOACETAMIDE; LANTHIONINE; LANTIBIOTIC; NISIN Z; SERINE; SULFIDE; THIOL DERIVATIVE; THREONINE; UNCLASSIFIED DRUG;

EID: 0033950308     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01075.x     Document Type: Article
Times cited : (45)

References (32)
  • 1
    • 0003148144 scopus 로고
    • Jung, G. & Sahl, H.-G., eds, ESCOM Science Publishers, Leiden
    • 1. Jung, G. (1991) Nisin and Novel Lantibiotics (Jung, G. & Sahl, H.-G., eds), pp. 1-31, ESCOM Science Publishers, Leiden.
    • (1991) Nisin and Novel Lantibiotics , pp. 1-31
    • Jung, G.1
  • 2
    • 0029055380 scopus 로고
    • Biosynthesis and biological activities of lantibiotics with unique post-translational modifications
    • 2. Sahl, H.-G., Jack, R.W. & Bierbaum, G. (1995) Biosynthesis and biological activities of lantibiotics with unique post-translational modifications. Eur. J. Biochem. 230, 827-853.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 827-853
    • Sahl, H.-G.1    Jack, R.W.2    Bierbaum, G.3
  • 3
    • 0003107982 scopus 로고
    • Jung, G. & Sahl, H.-G., eds, ESCOM Science Publishers, Leiden
    • 3. Sahl, H.-G. (1991) Nisin and Novel Lantibiotics (Jung, G. & Sahl, H.-G., eds), pp. 347-358, ESCOM Science Publishers, Leiden.
    • (1991) Nisin and Novel Lantibiotics , pp. 347-358
    • Sahl, H.-G.1
  • 5
    • 0030923340 scopus 로고    scopus 로고
    • The C-terminal region of nisin is responsible for the initial interaction of nisin with the targetmembrane
    • 5. Breukink, E., Kraaij, C., Demel, A., Siezen, R.J., Kuipers, O.P. & de Kruijff, B. (1997) The C-terminal region of nisin is responsible for the initial interaction of nisin with the targetmembrane. Biochemistry 36, 6968-6976.
    • (1997) Biochemistry , vol.36 , pp. 6968-6976
    • Breukink, E.1    Kraaij, C.2    Demel, A.3    Siezen, R.J.4    Kuipers, O.P.5    De Kruijff, B.6
  • 8
    • 0029897154 scopus 로고    scopus 로고
    • Interaction of the lantibiotic nisin with membranes revealed by fluorescence quenching of an introduced tryptophan
    • 8. Martin, I., Ruysschaert, J., Sanders, D. & Giffard, C.J. (1996) Interaction of the lantibiotic nisin with membranes revealed by fluorescence quenching of an introduced tryptophan. Eur. J. Biochem. 239, 156-164.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 156-164
    • Martin, I.1    Ruysschaert, J.2    Sanders, D.3    Giffard, C.J.4
  • 9
    • 0030900197 scopus 로고    scopus 로고
    • Structure-function relations of variant and fragment nisins studied with model membrane systems
    • 9. Giffard, C.J., Dodd, H.M., Horn, N., Ladha, S., Mackie, A.R., Parr, A., Gasson, M.J. & Sanders, D. (1997) Structure-function relations of variant and fragment nisins studied with model membrane systems. Biochemistry 36, 3802-3810.
    • (1997) Biochemistry , vol.36 , pp. 3802-3810
    • Giffard, C.J.1    Dodd, H.M.2    Horn, N.3    Ladha, S.4    Mackie, A.R.5    Parr, A.6    Gasson, M.J.7    Sanders, D.8
  • 10
    • 0029125825 scopus 로고
    • Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification
    • 10. Walker, B. & Bayley, H. (1995) Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification. J. Biol. Chem. 270, 23065-23071.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23065-23071
    • Walker, B.1    Bayley, H.2
  • 11
    • 0030685033 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis of helix IV and the adjoining loops in the lactose permease of Escherichia coli: Glu126 and Arg144 are essential
    • 11. Frillingos, S., Gonzalez, A. & Kaback, H.R. (1997) Cysteine-scanning mutagenesis of helix IV and the adjoining loops in the lactose permease of Escherichia coli: Glu126 and Arg144 are essential. Biochemistry 36, 14284-14290.
    • (1997) Biochemistry , vol.36 , pp. 14284-14290
    • Frillingos, S.1    Gonzalez, A.2    Kaback, H.R.3
  • 12
    • 0032488545 scopus 로고    scopus 로고
    • Avidin-FITC topological studies with three cysteine mutants of equinatoxin II, a sea anemone pore-forming protein
    • 12. Anderluh, G., Barlic, A., Krizaj, I., Menestrina, G., Gubensek, F. & Macek, P. (1998) Avidin-FITC topological studies with three cysteine mutants of equinatoxin II, a sea anemone pore-forming protein. Biochem. Biophys. Res. Commun. 242, 187-190.
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 187-190
    • Anderluh, G.1    Barlic, A.2    Krizaj, I.3    Menestrina, G.4    Gubensek, F.5    Macek, P.6
  • 15
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • 15. Casadaban, M.J. & Cohen, S.N. (1980) Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 143, 179-207.
    • (1980) J. Mol. Biol. , vol.143 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 18
    • 0027230871 scopus 로고
    • Improved cloning vectors and transformation procedure for Lactococcus lactis
    • 18. Wells, J.M., Wilson, P.W. & Le Page, R.W.F. (1993) Improved cloning vectors and transformation procedure for Lactococcus lactis. J. Appl. Bacteriol. 74, 629-636.
    • (1993) J. Appl. Bacteriol. , vol.74 , pp. 629-636
    • Wells, J.M.1    Wilson, P.W.2    Le Page, R.W.F.3
  • 21
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • 21. Schägger, H. & Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Jagow, G.2
  • 24
    • 0032483367 scopus 로고    scopus 로고
    • Identification and characterization of the structural and transporter genes for, and the chemical and biological properties of, sublancin 168, a novel lantibiotic produced by Bacillus subtilis 168
    • 24. Paik, S.H., Chakicherla, A. & Hansen, J.N. (1998) Identification and characterization of the structural and transporter genes for, and the chemical and biological properties of, sublancin 168, a novel lantibiotic produced by Bacillus subtilis 168. J. Biol. Chem. 273, 23134-23142.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23134-23142
    • Paik, S.H.1    Chakicherla, A.2    Hansen, J.N.3
  • 26
    • 0030597972 scopus 로고    scopus 로고
    • Structure-activity relationships in the peptide antibiotic nisin: Antibacterial activity of fragments of nisin
    • 26. Chan, W.C., Leyland, M., Clark, J., Dodd, H.M., Lian, L.-Y., Gasson, M.J., Bycroft, B.W. & Roberts, G.C.K. (1996) Structure-activity relationships in the peptide antibiotic nisin: antibacterial activity of fragments of nisin. FEBS Lett. 390, 129-132.
    • (1996) FEBS Lett. , vol.390 , pp. 129-132
    • Chan, W.C.1    Leyland, M.2    Clark, J.3    Dodd, H.M.4    Lian, L.-Y.5    Gasson, M.J.6    Bycroft, B.W.7    Roberts, G.C.K.8
  • 27
    • 0031784281 scopus 로고    scopus 로고
    • Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics
    • 27. Brötz, H., Josten, M., Wiedemann, I., Schneider, U., Bierbaum, G. & Sahl, H.-G. (1998) Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics. Mol. Microbiol. 30, 317-327.
    • (1998) Mol. Microbiol. , vol.30 , pp. 317-327
    • Brötz, H.1    Josten, M.2    Wiedemann, I.3    Schneider, U.4    Bierbaum, G.5    Sahl, H.-G.6
  • 29
    • 0029954539 scopus 로고    scopus 로고
    • Mutational analysis and chemical modification of Cys24 of lactococcin B, a bacteriocin produced by Lactococcus lactis
    • 29. Venema, K., Dost, M.H.R., Venema, G. & Kok, J. (1996) Mutational analysis and chemical modification of Cys24 of lactococcin B, a bacteriocin produced by Lactococcus lactis. Microbiology 142, 2825-2830.
    • (1996) Microbiology , vol.142 , pp. 2825-2830
    • Venema, K.1    Dost, M.H.R.2    Venema, G.3    Kok, J.4
  • 30
    • 0025989653 scopus 로고
    • Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae
    • 30. Boulnois, G.J., Paton, J.C., Mitchell, T.J. & Andrew, P.W. (1991) Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae. Mol. Microbiol. 5, 2611-2616.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2611-2616
    • Boulnois, G.J.1    Paton, J.C.2    Mitchell, T.J.3    Andrew, P.W.4
  • 31
    • 0021688528 scopus 로고
    • Identification and characterization of some bacterial membrane sulfhydryl groups which are targets of bacteriostatic and antibiotic action
    • 31. Morris, S.L., Walsh, R.C. & Hansen, J.N. (1984) Identification and characterization of some bacterial membrane sulfhydryl groups which are targets of bacteriostatic and antibiotic action. J. Biol. Chem. 259, 13590-13594.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13590-13594
    • Morris, S.L.1    Walsh, R.C.2    Hansen, J.N.3
  • 32
    • 4243291938 scopus 로고
    • Fuscin, an inhibitor of mitochondrial SH-dependent transport-linked functions
    • 32. Vignais, P.M. & Vignais, P.V. (1973) Fuscin, an inhibitor of mitochondrial SH-dependent transport-linked functions. Biochim. Biophys. Acta 462, 131-140.
    • (1973) Biochim. Biophys. Acta , vol.462 , pp. 131-140
    • Vignais, P.M.1    Vignais, P.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.