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Volumn 180, Issue 18, 1998, Pages 4879-4885

Spore photoproduct lyase from Bacillus subtilis spores is a novel iron- sulfur DNA repair enzyme which shares features with proteins such as class III anaerobic ribonucleotide reductases and pyruvate-formate lyases

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; FORMIC ACID; IRON SULFUR PROTEIN; LYASE; PYRUVIC ACID; RIBONUCLEOTIDE REDUCTASE; THYMINE DERIVATIVE;

EID: 0031679414     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.18.4879-4885.1998     Document Type: Article
Times cited : (93)

References (51)
  • 2
    • 3543060842 scopus 로고    scopus 로고
    • Personal communication
    • Begley, T. Personal communication.
    • Begley, T.1
  • 3
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert, H., R. H. Holm, and E. Münck. 1997. Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277:653-659.
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 4
    • 0030920430 scopus 로고    scopus 로고
    • The Arcanobacterium (Actinomyces) pyogenes hemolysin, pyolysin, is a novel member of the thiol-activated cytolysin family
    • Billington, S. J., B. H. Jost, W. A. Cuevas, K. R. Bright, and J. G. Songer. 1997. The Arcanobacterium (Actinomyces) pyogenes hemolysin, pyolysin, is a novel member of the thiol-activated cytolysin family. J. Bacteriol. 179:6100-6106.
    • (1997) J. Bacteriol. , vol.179 , pp. 6100-6106
    • Billington, S.J.1    Jost, B.H.2    Cuevas, W.A.3    Bright, K.R.4    Songer, J.G.5
  • 5
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C., and J. Doly. 1979. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7:1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 6
    • 0015325072 scopus 로고
    • Regulation of the bacterial cell wall: Analysis of a mutant of Bacillus subtilis defective in biosynthesis of teichoic acid
    • Boylan, R. J., N. H. Mendelson, D. Brooks, and F. E. Young. 1972. Regulation of the bacterial cell wall: analysis of a mutant of Bacillus subtilis defective in biosynthesis of teichoic acid. J. Bacteriol. 110:281-290.
    • (1972) J. Bacteriol. , vol.110 , pp. 281-290
    • Boylan, R.J.1    Mendelson, N.H.2    Brooks, D.3    Young, F.E.4
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0024571640 scopus 로고
    • The helix-turn-helix DNA binding motif
    • Brennan, R. G., and B. W. Matthews. 1989. The helix-turn-helix DNA binding motif. J. Biol. Chem. 264:1903-1906.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1903-1906
    • Brennan, R.G.1    Matthews, B.W.2
  • 9
    • 0002301028 scopus 로고
    • Genetic analysis
    • C. R. Harwood and S. M. Cutting (ed.). John Wiley and Sons, Sussex, England
    • Cutting, S. M., and P. B. Vander Horn. 1990. Genetic analysis, p. 27-74. In C. R. Harwood and S. M. Cutting (ed.). Molecular biological methods for Bacillus. John Wiley and Sons, Sussex, England.
    • (1990) Molecular Biological Methods for Bacillus , pp. 27-74
    • Cutting, S.M.1    Vander Horn, P.B.2
  • 10
    • 0000454531 scopus 로고
    • Thymine photoproducts but not thymine dimers are found in ultraviolet irradiated bacterial spores
    • Donnellan, J. E., Jr., and R. B. Setlow. 1965. Thymine photoproducts but not thymine dimers are found in ultraviolet irradiated bacterial spores. Science 149:308-310.
    • (1965) Science , vol.149 , pp. 308-310
    • Donnellan Jr., J.E.1    Setlow, R.B.2
  • 11
    • 0014244318 scopus 로고
    • The ultraviolet photochemistry and photobiology of vegetative cells and spores of Bacillus megaterium
    • Donnellan, J. E., Jr., and R. S. Stafford. 1968. The ultraviolet photochemistry and photobiology of vegetative cells and spores of Bacillus megaterium. Biophys. J. 8:17-28.
    • (1968) Biophys. J. , vol.8 , pp. 17-28
    • Donnellan Jr., J.E.1    Stafford, R.S.2
  • 13
    • 0029154205 scopus 로고
    • Molecular dissection of mutations in the Bacillus subtilis spore photoproduct lyase gene which affect repair of spore DNA damage caused by UV radiation
    • Fajardo-Cavazos, P., and W. L. Nicholson. 1995. Molecular dissection of mutations in the Bacillus subtilis spore photoproduct lyase gene which affect repair of spore DNA damage caused by UV radiation. J. Bacteriol. 177: 4402-4409.
    • (1995) J. Bacteriol. , vol.177 , pp. 4402-4409
    • Fajardo-Cavazos, P.1    Nicholson, W.L.2
  • 14
    • 0027453081 scopus 로고
    • Molecular cloning and characterization of the Bacillus subtilis spore photoproduct lyase (spl) gene, which is involved in repair of UV radiation-induced DNA damage during spore germination
    • Fajardo-Cavazos, P., C. Salazar, and W. L. Nicholson. 1993. Molecular cloning and characterization of the Bacillus subtilis spore photoproduct lyase (spl) gene, which is involved in repair of UV radiation-induced DNA damage during spore germination. J. Bacteriol. 175:1735-1744.
    • (1993) J. Bacteriol. , vol.175 , pp. 1735-1744
    • Fajardo-Cavazos, P.1    Salazar, C.2    Nicholson, W.L.3
  • 16
    • 0029790760 scopus 로고    scopus 로고
    • SoxR, a (2Fe-2S) transcription factor, is active only in its oxidized form
    • Gaudu, P., and B. Weiss. 1996. SoxR, a (2Fe-2S) transcription factor, is active only in its oxidized form. Proc. Natl. Acad. Sci. USA 93:10094-10098.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10094-10098
    • Gaudu, P.1    Weiss, B.2
  • 17
    • 0029152251 scopus 로고
    • Binuclear (2Fe-2S) clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription
    • Hidalgo, E., J. M. Bollinger, Jr., T. M. Bradley, C. T. Walsh, and B. Demple. 1995. Binuclear (2Fe-2S) clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription. J. Biol. Chem. 270:20908-20914.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20908-20914
    • Hidalgo, E.1    Bollinger Jr., J.M.2    Bradley, T.M.3    Walsh, C.T.4    Demple, B.5
  • 18
    • 0030029817 scopus 로고    scopus 로고
    • DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen
    • Lazazzera, B. A., H. Beinert, N. Khoroshilova, M. C. Kennedy, and P. J. Kiley. 1996. DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen. J. Biol. Chem. 271: 2762-2768.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2762-2768
    • Lazazzera, B.A.1    Beinert, H.2    Khoroshilova, N.3    Kennedy, M.C.4    Kiley, P.J.5
  • 19
    • 0025601634 scopus 로고
    • Reconstitution of nucleotide excision nuclease with UvrA and UvrB proteins from Escherichia coli and UvrC protein from Bacillus subtilis
    • Lin, J.-J., and A. Sancar. 1990. Reconstitution of nucleotide excision nuclease with UvrA and UvrB proteins from Escherichia coli and UvrC protein from Bacillus subtilis. J. Biol. Chem. 265:21337-21341.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21337-21341
    • Lin, J.-J.1    Sancar, A.2
  • 20
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 21
    • 0027407871 scopus 로고
    • An iron sulfur center and a free radical in the active anaerobic ribonucleotide reductase of Escherichia coli
    • Mulliez, E., M. Fontecave, J. Gaillard, and P. Reichard. 1993. An iron sulfur center and a free radical in the active anaerobic ribonucleotide reductase of Escherichia coli. J. Biol. Chem. 268:2296-2299.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2296-2299
    • Mulliez, E.1    Fontecave, M.2    Gaillard, J.3    Reichard, P.4
  • 22
    • 0014662507 scopus 로고
    • Genetic analysis of a mutant of Bacillus subtilis producing ultraviolet-sensitive spores
    • Munakata, N. 1969. Genetic analysis of a mutant of Bacillus subtilis producing ultraviolet-sensitive spores. Mol. Gen. Genet. 104:258-263.
    • (1969) Mol. Gen. Genet. , vol.104 , pp. 258-263
    • Munakata, N.1
  • 23
    • 0015369323 scopus 로고
    • Genetically controlled removal of "spore photoproduct" from deoxyribonucleic acid of ultraviolet-irradiated Bacillus subtilis spores
    • Munakata, N., and C. S. Rupert. 1972. Genetically controlled removal of "spore photoproduct" from deoxyribonucleic acid of ultraviolet-irradiated Bacillus subtilis spores. J. Bacteriol. 111:192-198.
    • (1972) J. Bacteriol. , vol.111 , pp. 192-198
    • Munakata, N.1    Rupert, C.S.2
  • 24
    • 0016211876 scopus 로고
    • Dark repair of DNA containing "spore photoproduct" in Bacillus subtilis
    • Munakata, N., and C. S. Rupert. 1974. Dark repair of DNA containing "spore photoproduct" in Bacillus subtilis. Mol. Gen. Genet. 130:239-250.
    • (1974) Mol. Gen. Genet. , vol.130 , pp. 239-250
    • Munakata, N.1    Rupert, C.S.2
  • 25
    • 0030610788 scopus 로고    scopus 로고
    • Analysis of spore photoproduct lyase operon (splAB) function using targeted deletion-insertion mutations spanning the Bacillus subtilis ptsHI and splAB operons
    • Nicholson, W. L., L. Chooback, and P. Fajardo-Cavazos. 1997. Analysis of spore photoproduct lyase operon (splAB) function using targeted deletion-insertion mutations spanning the Bacillus subtilis ptsHI and splAB operons. Mol. Gen. Genet. 255:587-594.
    • (1997) Mol. Gen. Genet. , vol.255 , pp. 587-594
    • Nicholson, W.L.1    Chooback, L.2    Fajardo-Cavazos, P.3
  • 26
    • 0000726568 scopus 로고    scopus 로고
    • DNA repair and the ultraviolet radiation resistance of bacterial spores: From the laboratory to the environment
    • S. Pandalai (ed.), Research Signpost, Trivandrum, India
    • Nicholson, W. L., and P. Fajardo-Cavazos. 1997. DNA repair and the ultraviolet radiation resistance of bacterial spores: from the laboratory to the environment. In S. Pandalai (ed.), Recent research developments in microbiology, vol. 1, p. 125-140. Research Signpost, Trivandrum, India.
    • (1997) Recent Research Developments in Microbiology , vol.1 , pp. 125-140
    • Nicholson, W.L.1    Fajardo-Cavazos, P.2
  • 27
    • 0026002937 scopus 로고
    • Ultraviolet irradiation of DNA complexed with α/β-type small, acid-soluble proteins from spores of Bacillus or Clostridium species makes spore photoproduct but not thymine dimers
    • Nicholson, W. L., B. Setlow, and P. Setlow. 1991. Ultraviolet irradiation of DNA complexed with α/β-type small, acid-soluble proteins from spores of Bacillus or Clostridium species makes spore photoproduct but not thymine dimers. Proc. Natl. Acad. Sci. USA 88:8288-8292.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8288-8292
    • Nicholson, W.L.1    Setlow, B.2    Setlow, P.3
  • 28
    • 0001864545 scopus 로고
    • Sporulation, germination, and outgrowth
    • C. R. Harwood and S. M. Cutting (ed.). John Wiley and Sons, Sussex, England
    • Nicholson, W. L., and P. Setlow. 1990. Sporulation, germination, and outgrowth, p. 391-450. In C. R. Harwood and S. M. Cutting (ed.). Molecular biological methods for Bacillus. John Wiley and Sons, Sussex, England.
    • (1990) Molecular Biological Methods for Bacillus , pp. 391-450
    • Nicholson, W.L.1    Setlow, P.2
  • 29
    • 0029800334 scopus 로고    scopus 로고
    • The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers
    • Nielsen, F. S., P. S. Andersen, and K. F. Jensen. 1996. The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers. J. Biol. Chem. 271:29359-29365.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29359-29365
    • Nielsen, F.S.1    Andersen, P.S.2    Jensen, K.F.3
  • 30
    • 0029918138 scopus 로고    scopus 로고
    • The anaerobic Escherichia coli ribonucleotide reductase: Subunit structure and iron-sulfur center
    • Ollagnier, S., E. Mulliez, J. Gaillard, R. Eliasson, M. Fontecave, and P. Reichard. 1996. The anaerobic Escherichia coli ribonucleotide reductase: subunit structure and iron-sulfur center. J. Biol. Chem. 271:9410-9416.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9410-9416
    • Ollagnier, S.1    Mulliez, E.2    Gaillard, J.3    Eliasson, R.4    Fontecave, M.5    Reichard, P.6
  • 31
    • 9844228508 scopus 로고    scopus 로고
    • Activation of the anaerobic ribonucleotide reductase from Escherichia coli. the essential role of the iron-sulfur center for S-adenosylmethionine reduction
    • Ollagnier, S., E. Mulliez, P. P. Schmidt, R. Eliasson, J. Gaillard, C. Deronzier, T. Bergman, A. Gräslund, P. Reichard, and M. Fontcave. 1997. Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction. J. Biol. Chem. 272:24216-24223.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24216-24223
    • Ollagnier, S.1    Mulliez, E.2    Schmidt, P.P.3    Eliasson, R.4    Gaillard, J.5    Deronzier, C.6    Bergman, T.7    Gräslund, A.8    Reichard, P.9    Fontcave, M.10
  • 32
    • 0028332201 scopus 로고
    • Temporal regulation and forespore-specific expression of the spore photoproduct lyase gene by sigma-G RNA polymerase during Bacillus subtilis sporulation
    • Pedraza-Reyes, M., F. Gutiérrez-Corona, and W. L. Nicholson. 1994. Temporal regulation and forespore-specific expression of the spore photoproduct lyase gene by sigma-G RNA polymerase during Bacillus subtilis sporulation. J. Bacteriol. 176:3983-3991.
    • (1994) J. Bacteriol. , vol.176 , pp. 3983-3991
    • Pedraza-Reyes, M.1    Gutiérrez-Corona, F.2    Nicholson, W.L.3
  • 33
    • 1842299883 scopus 로고    scopus 로고
    • Spore photoproduct lyase operon (splAB) regulation during Bacillus subtilis sporulation: Modulation of splB-lacZ fusion expression by P1 promoter mutations and by an in-frame deletion of splA
    • Pedraza-Reyes, M., F. Gutiérrez-Corona, and W. L. Nicholson. 1997. Spore photoproduct lyase operon (splAB) regulation during Bacillus subtilis sporulation: modulation of splB-lacZ fusion expression by P1 promoter mutations and by an in-frame deletion of splA. Curr. Microbiol. 34:133-137.
    • (1997) Curr. Microbiol. , vol.34 , pp. 133-137
    • Pedraza-Reyes, M.1    Gutiérrez-Corona, F.2    Nicholson, W.L.3
  • 34
    • 0031106730 scopus 로고    scopus 로고
    • The evolution of ribonucleotide reduction
    • Reichard, P. 1997. The evolution of ribonucleotide reduction. Trends Biochem. Sci. 22:81-85.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 81-85
    • Reichard, P.1
  • 36
    • 0028117141 scopus 로고
    • Structure and function of DNA photolyase
    • Sancar, A. 1994. Structure and function of DNA photolyase. Biochemistry 33:2-9.
    • (1994) Biochemistry , vol.33 , pp. 2-9
    • Sancar, A.1
  • 39
    • 0001274336 scopus 로고
    • Resistance of bacterial spores to ultraviolet light
    • Setlow, P. 1988. Resistance of bacterial spores to ultraviolet light. Comments Mol. Cell. Biophys. 5:253-264.
    • (1988) Comments Mol. Cell. Biophys. , vol.5 , pp. 253-264
    • Setlow, P.1
  • 40
    • 0026749802 scopus 로고
    • I will survive: Protecting and repairing spore DNA
    • Setlow, P. 1992. I will survive: protecting and repairing spore DNA. J. Bacteriol. 174:2737-2741.
    • (1992) J. Bacteriol. , vol.174 , pp. 2737-2741
    • Setlow, P.1
  • 41
    • 0026556134 scopus 로고
    • DNA in dormant spores of Bacillus species is in an A-like conformation
    • Setlow, P. 1992. DNA in dormant spores of Bacillus species is in an A-like conformation. Mol. Microbiol. 6:563-567.
    • (1992) Mol. Microbiol. , vol.6 , pp. 563-567
    • Setlow, P.1
  • 42
    • 0003095260 scopus 로고
    • DNA structure, spore formation, and spore properties
    • P. J. Piggot, C. P. Moran, Jr., and P. Youngman (ed.), American Society for Microbiology, Washington, D.C.
    • Setlow, P. 1994. DNA structure, spore formation, and spore properties. p. 181-194. In P. J. Piggot, C. P. Moran, Jr., and P. Youngman (ed.), Regulation of bacterial differentiation. American Society for Microbiology, Washington, D.C.
    • (1994) Regulation of Bacterial Differentiation , pp. 181-194
    • Setlow, P.1
  • 43
    • 0028868465 scopus 로고
    • Mechanisms for the prevention of damage to DNA in spores of Bacillus species
    • Setlow, P. 1995. Mechanisms for the prevention of damage to DNA in spores of Bacillus species. Annu. Rev. Microbiol. 49:29-54.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 29-54
    • Setlow, P.1
  • 44
    • 0014962511 scopus 로고
    • Biochemical studies of bacterial sporulation and germination. XXII. Energy metabolism in early stages of germination of Bacillus megaterium spores
    • Setlow, P., and A. Kornberg. 1970. Biochemical studies of bacterial sporulation and germination. XXII. Energy metabolism in early stages of germination of Bacillus megaterium spores. J. Biol. Chem. 245:3637-3644.
    • (1970) J. Biol. Chem. , vol.245 , pp. 3637-3644
    • Setlow, P.1    Kornberg, A.2
  • 45
    • 0001147947 scopus 로고
    • Studies on the mechanism of radiation inactivation of microorganisms. III. Inactivation of germinating spores of Bacillus cereus
    • Stuy, J. H. 1956. Studies on the mechanism of radiation inactivation of microorganisms. III. Inactivation of germinating spores of Bacillus cereus. Biochim. Biophys. Acta 22:241-246.
    • (1956) Biochim. Biophys. Acta , vol.22 , pp. 241-246
    • Stuy, J.H.1
  • 46
    • 0027978277 scopus 로고
    • High-pressure liquid chromatography assay for quantitatively monitoring spore photoproduct repair mediated by spore photoproduct lyase during germination of UV-irradiated Bacillus subtilis spores
    • Sun, Y., K. Palasingam, and W. L. Nicholson. 1994. High-pressure liquid chromatography assay for quantitatively monitoring spore photoproduct repair mediated by spore photoproduct lyase during germination of UV-irradiated Bacillus subtilis spores. Anal. Biochem. 221:61-65.
    • (1994) Anal. Biochem. , vol.221 , pp. 61-65
    • Sun, Y.1    Palasingam, K.2    Nicholson, W.L.3
  • 47
    • 0027471199 scopus 로고
    • Overexpression in Escherichia coli and affinity purification of chick kidney ferredoxin
    • Tang, C., and H. L. Henry. 1993. Overexpression in Escherichia coli and affinity purification of chick kidney ferredoxin. J. Biol. Chem. 268:5069-5076.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5069-5076
    • Tang, C.1    Henry, H.L.2
  • 48
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer, M. M., H. Ahern, D. Xing, R. P. Cunningham, and J. A. Tainer. 1995. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 14:4108-4120.
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 49
    • 0029914630 scopus 로고    scopus 로고
    • Similarity among the Drosophila (6-4) photolyase, a human photolyase homolog, and the DNA photolyase-blue-light photoreceptor family
    • Todo, T., H. Ryo, K. Yamamoto, H. Toh, T. Inui, H. Ayaki, T. Nomura, and M. Ikenaga. 1996. Similarity among the Drosophila (6-4) photolyase, a human photolyase homolog, and the DNA photolyase-blue-light photoreceptor family. Science 272:109-112.
    • (1996) Science , vol.272 , pp. 109-112
    • Todo, T.1    Ryo, H.2    Yamamoto, K.3    Toh, H.4    Inui, T.5    Ayaki, H.6    Nomura, T.7    Ikenaga, M.8
  • 50
    • 0017424519 scopus 로고
    • Evidence for the monomerization of spore photoproduct to two thymines by the light-independent "spore repair" process in Bacillus subtilis
    • Wang, T.-C.V., and C. S. Rupert. 1977. Evidence for the monomerization of spore photoproduct to two thymines by the light-independent "spore repair" process in Bacillus subtilis. Photochem. Photobiol. 25:123-127.
    • (1977) Photochem. Photobiol. , vol.25 , pp. 123-127
    • Wang, T.-C.V.1    Rupert, C.S.2


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