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Volumn 18, Issue 1, 1999, Pages 137-146

Synthesis and biochemical characterization of obligatory dimers of the sugar non-specific nuclease from Serratia marcescens using specifically designed bismaleimidoalkanes as SH-specific crosslinking reagents

Author keywords

Circular dichroism; Crosslink; Monomer dimer equilibrium; Peptide mapping; Site directed mutagenesis

Indexed keywords

CYSTEINE; MALEIMIDE DERIVATIVE; NUCLEASE; THIOL GROUP;

EID: 53149140261     PISSN: 02778033     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020616020507     Document Type: Article
Times cited : (6)

References (28)
  • 1
    • 0023470603 scopus 로고
    • The extracellular nuclease gene of Serratia marcescens and its secretion from Escherichia coli
    • Ball, T. K., Saurugger, P. N. and Benedik, M. J. (1987) The extracellular nuclease gene of Serratia marcescens and its secretion from Escherichia coli, Gene 57, 183-92.
    • (1987) Gene , vol.57 , pp. 183-192
    • Ball, T.K.1    Saurugger, P.N.2    Benedik, M.J.3
  • 2
    • 0026675734 scopus 로고
    • Disulfide bonds are required for Serratia marcescens nuclease activity
    • Ball, T. K., Sih, Y., and Benedik, M. J. (1992) Disulfide bonds are required for Serratia marcescens nuclease activity, Nucleic Acids Res. 20, 4971-4974.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4971-4974
    • Ball, T.K.1    Sih, Y.2    Benedik, M.J.3
  • 3
    • 0027234753 scopus 로고
    • Deoxyribonuclease of Syncephalastrum racemosum: Enzymatic properties and molecular structure
    • Chen, L. Y., Ho, H. C., Tsai, Y. C. and Liao, T. H. (1993) Deoxyribonuclease of Syncephalastrum racemosum: enzymatic properties and molecular structure, Arch Biochem Biophys 303, 51-56.
    • (1993) Arch Biochem Biophys , vol.303 , pp. 51-56
    • Chen, L.Y.1    Ho, H.C.2    Tsai, Y.C.3    Liao, T.H.4
  • 5
    • 0024278708 scopus 로고
    • Purification and properties of the major nuclease from mitochondria of Saccharomyces cerevisiae
    • Dake, E., Hofmann, T. J., McIntire, S., Hudson, A. and Zassenhaus, H. P. (1988) Purification and properties of the major nuclease from mitochondria of Saccharomyces cerevisiae, J. Biol. Chem. 263, 7691-7702.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7691-7702
    • Dake, E.1    Hofmann, T.J.2    McIntire, S.3    Hudson, A.4    Zassenhaus, H.P.5
  • 6
    • 0001713635 scopus 로고
    • Isolation and properties of an exocellular nuclease of Serratia marcescens
    • Eaves, G. N. and Jeffries, C. D.: (1963) Isolation and properties of an exocellular nuclease of Serratia marcescens, J. Bacteriol. 85, 273-278.
    • (1963) J. Bacteriol. , vol.85 , pp. 273-278
    • Eaves, G.N.1    Jeffries, C.D.2
  • 7
    • 0028373557 scopus 로고
    • A procedure for renaturation and purification of the extracellular Serratia marcescens nuclease from genetically engineered Escherichia coli
    • Friedhoff, P., Gimadutdinow, O., Rüter, T., Wende, W., Urbanke, C., Thole, H., and Pingoud, A. (1994a) A procedure for renaturation and purification of the extracellular Serratia marcescens nuclease from genetically engineered Escherichia coli, Prot. Express. Purif. 5, 37-43.
    • (1994) Prot. Express. Purif. , vol.5 , pp. 37-43
    • Friedhoff, P.1    Gimadutdinow, O.2    Rüter, T.3    Wende, W.4    Urbanke, C.5    Thole, H.6    Pingoud, A.7
  • 8
    • 0028114075 scopus 로고
    • Identification of catalytically relevant amino acids of the extracellular Serratia marcescens endonuclease by alignment-guided mutagenesis
    • Friedhoff, P., Gimadutinow, O., and Pingoud, A. (1994b) Identification of catalytically relevant amino acids of the extracellular Serratia marcescens endonuclease by alignment-guided mutagenesis, Nucleic Acids Res. 22, 3280-3287.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3280-3287
    • Friedhoff, P.1    Gimadutinow, O.2    Pingoud, A.3
  • 9
    • 0029982644 scopus 로고    scopus 로고
    • Analysis of the mechanism of the Serratia nuclease using site directed mutagenesis
    • Friedhoff, P., Kolmes, B., Gimadutdinow, O., Wende, W., Krause, K. L. and Pingoud, A. (1996a) Analysis of the mechanism of the Serratia nuclease using site directed mutagenesis, Nucleic Acids Res. 24(14), 2632-2639.
    • (1996) Nucleic Acids Res. , vol.24 , Issue.14 , pp. 2632-2639
    • Friedhoff, P.1    Kolmes, B.2    Gimadutdinow, O.3    Wende, W.4    Krause, K.L.5    Pingoud, A.6
  • 11
    • 0029857896 scopus 로고    scopus 로고
    • Identification and characterization of a mitochondrial endonuclease from yeast, Schizosaccharomyces pombe
    • Ikeda, S., Maeda, N., Ohshima, T. and Takata, N. (1996) Identification and characterization of a mitochondrial endonuclease from yeast, Schizosaccharomyces pombe, Biochem. Mol. Biol. Intern. 40, 1017-1024.
    • (1996) Biochem. Mol. Biol. Intern. , vol.40 , pp. 1017-1024
    • Ikeda, S.1    Maeda, N.2    Ohshima, T.3    Takata, N.4
  • 12
    • 0030592844 scopus 로고    scopus 로고
    • Analysis of the reaction mechanism of the non-specific endonuclease of Serratia marcescens using an artificial substrate
    • Kolmes, B., Franke, I., Friedhoff, P. and Pingoud, A. (1996) Analysis of the reaction mechanism of the non-specific endonuclease of Serratia marcescens using an artificial substrate, FEBS Lett. 397, 343-346.
    • (1996) FEBS Lett. , vol.397 , pp. 343-346
    • Kolmes, B.1    Franke, I.2    Friedhoff, P.3    Pingoud, A.4
  • 13
    • 76549250377 scopus 로고
    • Crystalline deoxyribonuclease I. Isolation and general properties. Spectrophotometric method for the measurement of deoxyribonuclease activity
    • Kunitz, M. (1950) Crystalline deoxyribonuclease I. Isolation and general properties. Spectrophotometric method for the measurement of deoxyribonuclease activity, J. Gen. Physiol. 33, 349-362
    • (1950) J. Gen. Physiol. , vol.33 , pp. 349-362
    • Kunitz, M.1
  • 14
    • 0016622399 scopus 로고
    • Membrane location of a deoxyri-bonuclease implicated in the genetic transformation of Diplococcus pneumoniae
    • Lacks, S. & Neuberger, M. (1975) Membrane location of a deoxyri-bonuclease implicated in the genetic transformation of Diplococcus pneumoniae, J. Bacteriol. 124, 1321-1329.
    • (1975) J. Bacteriol. , vol.124 , pp. 1321-1329
    • Lacks, S.1    Neuberger, M.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of bacteriophage T4, Nature 227, 680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 16
    • 0032006766 scopus 로고    scopus 로고
    • Biochemical characterization of Anabaena sp. strain PCC 7120 non-specific nuclease NucA and ist inhibitor NuiA
    • in press
    • Meiss, G., Franke, I., Gimadutdinow, O., Urbanke, C. and Pingoud, A. (1998) Biochemical characterization of Anabaena sp. strain PCC 7120 non-specific nuclease NucA and ist inhibitor NuiA, Eur. J. Biochem. in press.
    • (1998) Eur. J. Biochem.
    • Meiss, G.1    Franke, I.2    Gimadutdinow, O.3    Urbanke, C.4    Pingoud, A.5
  • 17
    • 0029084590 scopus 로고
    • Sequence preferences in cleavage of dsDNA and ssDNA by the extracellular Serratia marcescens endonuclease
    • Meiss, G., Friedhoff, P., Hahn, M., Gimadutdinow, O., and Pingoud, A. (1995) Sequence preferences in cleavage of dsDNA and ssDNA by the extracellular Serratia marcescens endonuclease, Biochemistry 34, 11979-11988.
    • (1995) Biochemistry , vol.34 , pp. 11979-11988
    • Meiss, G.1    Friedhoff, P.2    Hahn, M.3    Gimadutdinow, O.4    Pingoud, A.5
  • 18
    • 33947472042 scopus 로고
    • Maleamic and Citraconamic Acids, Methyl Esters, and Imides
    • Metha, N. B., Phillips, A. P., Lui, F. F., and Brooks, R. E. (1960) Maleamic and Citraconamic Acids, Methyl Esters, and Imides, J. Org. Chem. 25, 1012-1015.
    • (1960) J. Org. Chem. , vol.25 , pp. 1012-1015
    • Metha, N.B.1    Phillips, A.P.2    Lui, F.F.3    Brooks, R.E.4
  • 19
    • 0030068478 scopus 로고    scopus 로고
    • Identification of the Serratia endonuclease dimer: Structural basis and implications for catalysis
    • Miller, M. D., and Krause, K. L. (1996) Identification of the Serratia endonuclease dimer: Structural basis and implications for catalysis, Protein Science 5, 24-33
    • (1996) Protein Science , vol.5 , pp. 24-33
    • Miller, M.D.1    Krause, K.L.2
  • 20
    • 0027977143 scopus 로고
    • 2.1 Å structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA
    • Miller, M. D., Tanner, J., Alpaugh, M., Benedik, M. J., and Krause, K. L. (1994) 2.1 Å structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA, Structural Biology 1, 461-468.
    • (1994) Structural Biology , vol.1 , pp. 461-468
    • Miller, M.D.1    Tanner, J.2    Alpaugh, M.3    Benedik, M.J.4    Krause, K.L.5
  • 21
    • 0026746322 scopus 로고
    • Identification, genetic analysis and characterization of a sugar-non-specific nuclease from the cyanobacterium Anabaena sp. strain PCC 7120
    • Muro-Pastor, A. M., Flores, E., Herrero, A. and Wolk, C. P. (1992) Identification, genetic analysis and characterization of a sugar-non-specific nuclease from the cyanobacterium Anabaena sp. strain PCC 7120, Mol. Microbiol. 6, 3021-3030.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3021-3030
    • Muro-Pastor, A.M.1    Flores, E.2    Herrero, A.3    Wolk, C.P.4
  • 22
    • 0028120676 scopus 로고
    • Transfer of a genetic marker from a megaplasmid of Anabaena sp. strain PCC 7120 to a megaplasmid of a different Anabaena strain
    • Muro-Pastor, A. M., Kuritz, T., Flores, E., Herrero, A. and Wolk, C. P. (1994). Transfer of a genetic marker from a megaplasmid of Anabaena sp. strain PCC 7120 to a megaplasmid of a different Anabaena strain, J. Bacteriology 176, 1093-1098.
    • (1994) J. Bacteriology , vol.176 , pp. 1093-1098
    • Muro-Pastor, A.M.1    Kuritz, T.2    Flores, E.3    Herrero, A.4    Wolk, C.P.5
  • 23
    • 0014670660 scopus 로고
    • An extracellular nuclease from Serratia marcescens - I. Purification and some properties of the enzyme
    • Nestle, M. and Roberts, W. K. (1969a). An extracellular nuclease from Serratia marcescens - I. Purification and some properties of the enzyme, J. Biol. Chem. 244, 5213-5218.
    • (1969) J. Biol. Chem. , vol.244 , pp. 5213-5218
    • Nestle, M.1    Roberts, W.K.2
  • 24
    • 0025315488 scopus 로고
    • Genetic and structural characterization of EndA: A membrane-bound nuclease required for transformation of Streptococcus pneumoniae
    • Puyet, A., Greenberg, B. and Lacks, S. A. (1990) Genetic and structural characterization of EndA: A membrane-bound nuclease required for transformation of Streptococcus pneumoniae, J. Mol. Biol. 213, 727-738.
    • (1990) J. Mol. Biol. , vol.213 , pp. 727-738
    • Puyet, A.1    Greenberg, B.2    Lacks, S.A.3
  • 25
    • 0017401236 scopus 로고
    • Nuclease detection in SDS-polyacrylamide gel electrophoresis
    • Rosenthal, A. L. and Lacks, S. A. (1977) Nuclease detection in SDS-polyacrylamide gel electrophoresis, Anal. Biochem. 80, 76-90.
    • (1977) Anal. Biochem. , vol.80 , pp. 76-90
    • Rosenthal, A.L.1    Lacks, S.A.2
  • 26
    • 0027284549 scopus 로고
    • Primers for mitochondrial DNA replication generated by endonuclease G
    • Ruiz-Carrillo, A. and Cote, J. (1993) Primers for mitochondrial DNA replication generated by endonuclease G, Science 261, 765-769.
    • (1993) Science , vol.261 , pp. 765-769
    • Ruiz-Carrillo, A.1    Cote, J.2
  • 27
    • 0024296644 scopus 로고
    • Sequence and expression of NUC1, the gene encoding the mitochondrial nuclease in Saccharomyces cerevisae
    • Vincent, R. D., Hofmann, T. J. and Zassenhaus, H. P. (1988) Sequence and expression of NUC1, the gene encoding the mitochondrial nuclease in Saccharomyces cerevisae, Nucleic Acids Res. 16, 3297-3312.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 3297-3312
    • Vincent, R.D.1    Hofmann, T.J.2    Zassenhaus, H.P.3
  • 28
    • 0020761009 scopus 로고
    • Isolation and characterization of nucleases from a clinical isolate of Serratia marcescens kums 3958
    • Yonemura, K., Matsumoto, K. and Maeda, H. (1983) Isolation and characterization of nucleases from a clinical isolate of Serratia marcescens kums 3958, J. Biochem. 93, 1287-1295.
    • (1983) J. Biochem. , vol.93 , pp. 1287-1295
    • Yonemura, K.1    Matsumoto, K.2    Maeda, H.3


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