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Volumn 264, Issue 1, 1999, Pages 161-167

Class II DNA photolyase from Arabidopsis thaliana contains FAD as a cofactor

Author keywords

Arabidopsis thaliana; Class II DNA photolyase; DNA repair; Enzymatic properties; Spectroscopic properties

Indexed keywords

DEOXYRIBODIPYRIMIDINE PHOTOLYASE; FLAVINE ADENINE NUCLEOTIDE;

EID: 0033567251     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00590.x     Document Type: Article
Times cited : (42)

References (53)
  • 1
    • 0025033353 scopus 로고
    • DNA photolyases: Physical properties, action mechanism and roles in dark repair
    • 1. Sancar, A. (1990) DNA photolyases: physical properties, action mechanism and roles in dark repair. Mutat. Res. 236, 147-160.
    • (1990) Mutat. Res. , vol.236 , pp. 147-160
    • Sancar, A.1
  • 2
    • 0028117141 scopus 로고
    • Structure and function of DNA photolyase
    • 2. Sancar, A. (1994) Structure and function of DNA photolyase. Biochemistry 33, 2-9.
    • (1994) Biochemistry , vol.33 , pp. 2-9
    • Sancar, A.1
  • 3
    • 0027439741 scopus 로고
    • A new photoreactivating enzyme that specifically repairs ultraviolet light-induced (6-4)photoproducts
    • 3. Todo, T., Takemori, H., Ryo, H., Ihara, M., Matsunaga, T., Nikaido, O., Sato, K. & Nomura, T. (1993) A new photoreactivating enzyme that specifically repairs ultraviolet light-induced (6-4)photoproducts. Nature 361, 371-374.
    • (1993) Nature , vol.361 , pp. 371-374
    • Todo, T.1    Takemori, H.2    Ryo, H.3    Ihara, M.4    Matsunaga, T.5    Nikaido, O.6    Sato, K.7    Nomura, T.8
  • 4
    • 0029874444 scopus 로고    scopus 로고
    • No end of history for photolyases
    • 4. Sancar, A. (1996) No end of history for photolyases. Science 272, 48-49.
    • (1996) Science , vol.272 , pp. 48-49
    • Sancar, A.1
  • 5
    • 0000832551 scopus 로고
    • Reactivation of ultraviolet-inactivated bacteriophage by visible light
    • 5. Dulbecco, R. (1949) Reactivation of ultraviolet-inactivated bacteriophage by visible light. Nature 163, 949-950.
    • (1949) Nature , vol.163 , pp. 949-950
    • Dulbecco, R.1
  • 6
    • 0021762610 scopus 로고
    • Escherichia coli DNA photolyase is a flavoprotein
    • 6. Sancar, A. & Sancar, G.B. (1984) Escherichia coli DNA photolyase is a flavoprotein. J. Mol. Biol. 172, 223-227.
    • (1984) J. Mol. Biol. , vol.172 , pp. 223-227
    • Sancar, A.1    Sancar, G.B.2
  • 7
    • 0024121590 scopus 로고
    • Identification of the second chromophore of Escherichia coli and yeast DNA photolyases as 5,10-methenyltetrahydrofolate
    • 7. Johnson, J.L., Hamm-Alvarez, S., Payne, G., Sancar, G.B., Rajagopalan, K.V. & Sancar, A. (1988) Identification of the second chromophore of Escherichia coli and yeast DNA photolyases as 5,10-methenyltetrahydrofolate. Proc. Natl Acad. Sci. USA 85, 2046-2050.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2046-2050
    • Johnson, J.L.1    Hamm-Alvarez, S.2    Payne, G.3    Sancar, G.B.4    Rajagopalan, K.V.5    Sancar, A.6
  • 8
    • 0019446467 scopus 로고
    • Photoreactivating enzyme from Streptomyces griseus-IV. On the nature of the chromophoric cofactor in Streptomyces griseus photoreactivating enzyme
    • 8. Eker, A.P., Dekker, R.H. & Berends, W. (1981) Photoreactivating enzyme from Streptomyces griseus-IV. On the nature of the chromophoric cofactor in Streptomyces griseus photoreactivating enzyme. Photochem. Photobiol. 33, 65-72.
    • (1981) Photochem. Photobiol. , vol.33 , pp. 65-72
    • Eker, A.P.1    Dekker, R.H.2    Berends, W.3
  • 9
    • 0029914630 scopus 로고    scopus 로고
    • Similarity among the Drosophila (6-4) photolyase, a human photolyase homolog, and the DNA photolyase-blue-light photoreceptor family
    • 9. Todo, T., Ryo, H., Yamamoto, K., Toh, H., Inui, T., Ayaki, H., Nomura, T. & Ikenaga, M. (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
  • 12
    • 0027493250 scopus 로고
    • HY4 gene of A. thaliana encodes a protein with characteristics of a blue-light photoreceptor
    • 12. Ahmad, M. & Cashmore, A.R. (1993) HY4 gene of A. thaliana encodes a protein with characteristics of a blue-light photoreceptor. Nature 366, 162-166.
    • (1993) Nature , vol.366 , pp. 162-166
    • Ahmad, M.1    Cashmore, A.R.2
  • 13
    • 0029857950 scopus 로고    scopus 로고
    • PHH1, a novel gene from Arabidopsis thaliana that encodes a protein similar to plant blue-light photoreceptors and microbial photolyases
    • 13. Hoffman, P.D., Batschauer, A. & Hays, J.B. (1996) PHH1, a novel gene from Arabidopsis thaliana that encodes a protein similar to plant blue-light photoreceptors and microbial photolyases. Mol. Gen. Genet. 253, 259-265.
    • (1996) Mol. Gen. Genet. , vol.253 , pp. 259-265
    • Hoffman, P.D.1    Batschauer, A.2    Hays, J.B.3
  • 14
    • 0001078531 scopus 로고    scopus 로고
    • CRY2: A second member of the Arabidopsis cryptochrome gene family
    • 14. Lin, C., Ahmad, M., Chan, J. & Cashmore, A.R. (1996) CRY2: a second member of the Arabidopsis cryptochrome gene family. Plant Physiol. 110, 1047.
    • (1996) Plant Physiol. , vol.110 , pp. 1047
    • Lin, C.1    Ahmad, M.2    Chan, J.3    Cashmore, A.R.4
  • 17
    • 0032533793 scopus 로고    scopus 로고
    • Characterization of photolyase/blue-light receptor homologs in mouse and human cells
    • 17. Kobayashi, K., Kanno, S., Smil, B., van der Horst, G.T.J., Takao, M. & Yasui, A. (1998) Characterization of photolyase/blue-light receptor homologs in mouse and human cells. Nucl. Acids Res. 26, 5086-5092.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 5086-5092
    • Kobayashi, K.1    Kanno, S.2    Smil, B.3    Van Der Horst, G.T.J.4    Takao, M.5    Yasui, A.6
  • 18
    • 0032567038 scopus 로고    scopus 로고
    • CRY, a Drosophila clock and light-regulated cryptochrome, is a major contributor to circadian rhythm resetting and photosensitivity
    • 18. Emery, P., So, W.V., Kaneko, M., Hall, J.C. & Rosbash, M. (1998) CRY, a Drosophila clock and light-regulated cryptochrome, is a major contributor to circadian rhythm resetting and photosensitivity. Cell 95, 669-679.
    • (1998) Cell , vol.95 , pp. 669-679
    • Emery, P.1    So, W.V.2    Kaneko, M.3    Hall, J.C.4    Rosbash, M.5
  • 19
    • 0029061519 scopus 로고
    • Putative blue-light photoreceptors from Arabidopsis thaliana and Sinapis alba with a high degree of sequence homology to DNA photolyase contain the two photolyase cofactors but lack DNA repair activity
    • 19. Malhotra, K., Kim, S.T., Batschauer, A., Dawut, L. & Sancar, A. (1995) Putative blue-light photoreceptors from Arabidopsis thaliana and Sinapis alba with a high degree of sequence homology to DNA photolyase contain the two photolyase cofactors but lack DNA repair activity. Biochemistry 34, 6892-6899.
    • (1995) Biochemistry , vol.34 , pp. 6892-6899
    • Malhotra, K.1    Kim, S.T.2    Batschauer, A.3    Dawut, L.4    Sancar, A.5
  • 20
    • 0027081004 scopus 로고
    • Visible light-inducible photolyase gene from the goldfish Carassius auratus
    • 20. Yasuhira, S. & Yasui, A. (1992) Visible light-inducible photolyase gene from the goldfish Carassius auratus. J. Biol. Chem. 267, 25644-25647.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25644-25647
    • Yasuhira, S.1    Yasui, A.2
  • 21
    • 0028559513 scopus 로고
    • A new class of DNA photolyases present in various organisms including aplacental mammals
    • 21. Yasui, A., Eker, A.P., Yasuhira, S., Yajima, H., Kobayashi, T., Takao, M. & Oikawa, A. (1994) A new class of DNA photolyases present in various organisms including aplacental mammals. EMBO J. 13, 6143-6151.
    • (1994) EMBO J. , vol.13 , pp. 6143-6151
    • Yasui, A.1    Eker, A.P.2    Yasuhira, S.3    Yajima, H.4    Kobayashi, T.5    Takao, M.6    Oikawa, A.7
  • 22
    • 0029919617 scopus 로고    scopus 로고
    • Photolyase of Myxococcus xanthus, a gram-negative eubacterium, is more similar to photolyases found in Archaea and 'higher' eukaryotes than to photolyases of other eubacteria
    • 22. O'Connor, K.A., McBride, M.J., West, M., Yu, H., Trinh, L., Yuan, K., Lee, T. & Zusman, D.R. (1996) Photolyase of Myxococcus xanthus, a Gram-negative eubacterium, is more similar to photolyases found in Archaea and 'higher' eukaryotes than to photolyases of other eubacteria. J. Biol. Chem. 271, 6252-6359.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6252-6359
    • O'Connor, K.A.1    McBride, M.J.2    West, M.3    Yu, H.4    Trinh, L.5    Yuan, K.6    Lee, T.7    Zusman, D.R.8
  • 23
    • 0001602284 scopus 로고    scopus 로고
    • Nucleotide sequence of an Arabidopsis cDNA At-phrll encoding a protein with high homology to the class II CPD photolyases present in higher eukaryotes
    • 23. Taylor, R., Tobin, A. & Bray, C. (1996) Nucleotide sequence of an Arabidopsis cDNA At-phrII encoding a protein with high homology to the class II CPD photolyases present in higher eukaryotes. Plant Physiol. 112, 862.
    • (1996) Plant Physiol. , vol.112 , pp. 862
    • Taylor, R.1    Tobin, A.2    Bray, C.3
  • 25
    • 0030831112 scopus 로고    scopus 로고
    • Molecular evolution of the photolyase-blue-light photoreceptor family
    • 25. Kanai, S., Kikuno, R., Toh, H., Ryo, H. & Todo, T. (1997) Molecular evolution of the photolyase-blue-light photoreceptor family. J. Mol. Evol. 45, 535-548.
    • (1997) J. Mol. Evol. , vol.45 , pp. 535-548
    • Kanai, S.1    Kikuno, R.2    Toh, H.3    Ryo, H.4    Todo, T.5
  • 26
    • 77952306859 scopus 로고
    • Preparation and properties of 5,10-methenyltetrahydrofolic acid and 10-formyltetrahydrofolic acid
    • 26. Rabinowitz, J.C. (1963) Preparation and properties of 5,10-methenyltetrahydrofolic acid and 10-formyltetrahydrofolic acid. Methods Enzymol. 6, 814-815.
    • (1963) Methods Enzymol. , vol.6 , pp. 814-815
    • Rabinowitz, J.C.1
  • 27
    • 0026024037 scopus 로고
    • Construction of Escherichia coli K12 phr deletion and insertion mutants by gene replacement
    • 27. Akasaka, S. & Yamamoto, K. (1991) Construction of Escherichia coli K12 phr deletion and insertion mutants by gene replacement. Mutat. Res. 254, 27-35.
    • (1991) Mutat. Res. , vol.254 , pp. 27-35
    • Akasaka, S.1    Yamamoto, K.2
  • 28
    • 0023875970 scopus 로고
    • Using mini-prep plasmid DNA for sequencing double stranded templates with sequenase
    • 28. Kraft, R., Tardiff, J., Krauter, K.S. & Leinwand, L.A. (1988) Using mini-prep plasmid DNA for sequencing double stranded templates with sequenase. Biotechniques 6, 544-547.
    • (1988) Biotechniques , vol.6 , pp. 544-547
    • Kraft, R.1    Tardiff, J.2    Krauter, K.S.3    Leinwand, L.A.4
  • 29
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • 29. Schagger, H. & von 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
    • Schagger, H.1    Von Jagow, G.2
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 30. Laemmli, U.K. (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
  • 31
    • 0016616415 scopus 로고
    • Eine störungsfreie Mikromethode zur Bestimmung des Proteingehalts in Gewebehomogenaten
    • 31. Popov, N., Schmitt, S. & Matthies, H. (1975) Eine störungsfreie Mikromethode zur Bestimmung des Proteingehalts in Gewebehomogenaten. Acta Biol. Germ. 34, 1441-1446.
    • (1975) Acta Biol. Germ. , vol.34 , pp. 1441-1446
    • Popov, N.1    Schmitt, S.2    Matthies, H.3
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 32. 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
  • 33
    • 0027215760 scopus 로고
    • Effect of sequence, adduct type, and opposing lesions on the binding and repair of ultraviolet photodamage by DNA photolyase and (A)BC exconuclease
    • 33. Svoboda, D.L., Smith, C.A., Taylor, J.S. & Sancar, A. (1993) Effect of sequence, adduct type, and opposing lesions on the binding and repair of ultraviolet photodamage by DNA photolyase and (A)BC exconuclease. J. Biol. Chem. 268, 10694-10700.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10694-10700
    • Svoboda, D.L.1    Smith, C.A.2    Taylor, J.S.3    Sancar, A.4
  • 34
    • 0033105505 scopus 로고    scopus 로고
    • Photodamaged DNA-RNA duplexes are poor substrates for photoreactivating DNA-repair enzymes
    • 34. Butenandt, J., Burgdorf, L. & Carell, T. (1999) Photodamaged DNA-RNA duplexes are poor substrates for photoreactivating DNA-repair enzymes. Angew. Chem. Int. Ed. Engl. 38, 708-711.
    • (1999) Angew. Chem. Int. Ed. Engl. , vol.38 , pp. 708-711
    • Butenandt, J.1    Burgdorf, L.2    Carell, T.3
  • 35
    • 0026654909 scopus 로고
    • Probing structural factors stabilizing antisense oligonucleotide duplexes: NMR studies of a DNA.DNA duplex containing a formacetal linkage
    • 35. Gao, X., Brown, F.K., Jeffs, P., Bischofberger, N., Lin, K.Y., Pipe. A.J. & Noble, S.A. (1992) Probing structural factors stabilizing antisense oligonucleotide duplexes: NMR studies of a DNA.DNA duplex containing a formacetal linkage. Biochemistry, 31, 6228-6236.
    • (1992) Biochemistry , vol.31 , pp. 6228-6236
    • Gao, X.1    Brown, F.K.2    Jeffs, P.3    Bischofberger, N.4    Lin, K.Y.5    Pipe, A.J.6    Noble, S.A.7
  • 36
    • 0000250379 scopus 로고
    • A comparison of DNA oligomer duplexes containing formacetal and phosphodiester linkers using molecular dynamics and quantum-mechanics
    • 36. Veal, J.M., Gao, X. & Brown, F.K. (1993) A comparison of DNA oligomer duplexes containing formacetal and phosphodiester linkers using molecular dynamics and quantum-mechanics. J. Am. Chem. Soc. 115, 7139-7145.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7139-7145
    • Veal, J.M.1    Gao, X.2    Brown, F.K.3
  • 37
    • 0031860433 scopus 로고    scopus 로고
    • Synthesis, crystal-structure and enzymatic evaluation of a DNA-photolesion isostere
    • 37. Butenandt, J., Eker, A.P.M. & Carell, T. (1998) Synthesis, crystal-structure and enzymatic evaluation of a DNA-photolesion isostere. Chem. Eur. J. 4, 642-654.
    • (1998) Chem. Eur. J. , vol.4 , pp. 642-654
    • Butenandt, J.1    Eker, A.P.M.2    Carell, T.3
  • 38
    • 0023643412 scopus 로고
    • The active form of Escherichia coli DNA photolyase contains a fully reduced flavin and not a flavin radical, both in vivo and in vitro
    • 38. Payne, G., Heelis, P.F., Rohrs, B.R. & Sancar, A. (1987) The active form of Escherichia coli DNA photolyase contains a fully reduced flavin and not a flavin radical, both in vivo and in vitro. Biochemistry 26, 7121-7127.
    • (1987) Biochemistry , vol.26 , pp. 7121-7127
    • Payne, G.1    Heelis, P.F.2    Rohrs, B.R.3    Sancar, A.4
  • 39
    • 0025100995 scopus 로고
    • Chromophore function and interaction in Escherichia coli DNA photolyase: Reconstitution of the apoenzyme with pterin and/or flavin derivatives
    • 39. Jorns, M.S., Wang, B.Y., Jordan, S.P. & Chanderkar, L.P. (1990) Chromophore function and interaction in Escherichia coli DNA photolyase: reconstitution of the apoenzyme with pterin and/or flavin derivatives. Biochemistry 29, 552-561.
    • (1990) Biochemistry , vol.29 , pp. 552-561
    • Jorns, M.S.1    Wang, B.Y.2    Jordan, S.P.3    Chanderkar, L.P.4
  • 40
    • 0027212725 scopus 로고
    • Evidence for lack of DNA photoreactivating enzyme in humans
    • 40. Li, Y.F., Kim, S.T. & Sancar, A. (1993) Evidence for lack of DNA photoreactivating enzyme in humans. Proc. Natl Acad. Sci. USA 90, 4389-4393.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4389-4393
    • Li, Y.F.1    Kim, S.T.2    Sancar, A.3
  • 41
    • 0019631509 scopus 로고
    • Reactivity of D-amino acid oxidase with 1,2-cyclohexanedione: Evidence for one arginine in the substrate-binding site
    • 41. Ferti, C., Curti, B., Pilone, S.M., Ronchi, S., Galliano, M. & Minchiotti, L. (1981) Reactivity of D-amino acid oxidase with 1,2-cyclohexanedione: evidence for one arginine in the substrate-binding site. Eur. J. Biochem. 119, 553-557.
    • (1981) Eur. J. Biochem. , vol.119 , pp. 553-557
    • Ferti, C.1    Curti, B.2    Pilone, S.M.3    Ronchi, S.4    Galliano, M.5    Minchiotti, L.6
  • 42
    • 0028812143 scopus 로고
    • Crystal-structure of DNA photolyase from E. coli
    • 42. Park, H.-W., Kim, S.T., Sancar, A. & Deisenhofer, J. (1995) Crystal-structure of DNA photolyase from E. coli. Science 268, 1866-1872.
    • (1995) Science , vol.268 , pp. 1866-1872
    • Park, H.-W.1    Kim, S.T.2    Sancar, A.3    Deisenhofer, J.4
  • 43
    • 0000986142 scopus 로고
    • Fluorescence of riboflavin and flavin adenine dinucleotide
    • 43. Weber, G. (1959) Fluorescence of riboflavin and flavin adenine dinucleotide. Biochem. J. 47, 114-121.
    • (1959) Biochem. J. , vol.47 , pp. 114-121
    • Weber, G.1
  • 44
    • 0026603410 scopus 로고
    • Specificity and kinetics of Rhodotorula gracilis D-amino acid oxidase
    • 44. Pollegioni, L., Falbo, A. & Pilone, M.S. (1992) Specificity and kinetics of Rhodotorula gracilis D-amino acid oxidase. Biochim. Biophys. Acta. 1120, 11-16.
    • (1992) Biochim. Biophys. Acta. , vol.1120 , pp. 11-16
    • Pollegioni, L.1    Falbo, A.2    Pilone, M.S.3
  • 45
    • 0025762543 scopus 로고
    • A study on apoenzyme from Rhodotorula gracilis D-amino acid oxidase
    • 45. Casalin, P., Pollegioni, L., Curti, B. & Pilone, M.S. (1991) A study on apoenzyme from Rhodotorula gracilis D-amino acid oxidase. Eur. J. Biochem. 197, 513-517.
    • (1991) Eur. J. Biochem. , vol.197 , pp. 513-517
    • Casalin, P.1    Pollegioni, L.2    Curti, B.3    Pilone, M.S.4
  • 46
    • 0019274551 scopus 로고
    • Analytical and preparative high-performance liquid chromatography separation of flavin and flavin analog coenzymes
    • 46. Light, D.R., Walsh, C. & Marletta, M.A. (1980) Analytical and preparative high-performance liquid chromatography separation of flavin and flavin analog coenzymes. Anal. Biochem. 109, 87-93.
    • (1980) Anal. Biochem. , vol.109 , pp. 87-93
    • Light, D.R.1    Walsh, C.2    Marletta, M.A.3
  • 47
    • 0000253486 scopus 로고
    • Photoreactivating enzyme from the green algae Scenedesmus acutus: Evidence for the presence of two different flavin chromophores
    • 47. Eker, A.P.M., Hessels, J.K.C. & van der Velde, J. (1988) Photoreactivating enzyme from the green algae Scenedesmus acutus: evidence for the presence of two different flavin chromophores. Biochemistry 27, 1758-1765.
    • (1988) Biochemistry , vol.27 , pp. 1758-1765
    • Eker, A.P.M.1    Hessels, J.K.C.2    Van Der Velde, J.3
  • 48
    • 0025272139 scopus 로고
    • DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans
    • 48. Eker, A.P.M., Kooiman, P., Hessels, J.K.C. & Yasui, A.J. (1990) DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans. J. Biol. Chem. 265, 8009-8015.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8009-8015
    • Eker, A.P.M.1    Kooiman, P.2    Hessels, J.K.C.3    Yasui, A.J.4
  • 49
    • 0024971180 scopus 로고
    • Purification and properties of Methanobacterium thermoautotrophicum DNA photolyase
    • 49. Kiener, A., Husain, I., Sancar, A. & Walsh, C. (1989) Purification and properties of Methanobacterium thermoautotrophicum DNA photolyase. J. Biol. Chem. 264, 13880-13887.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13880-13887
    • Kiener, A.1    Husain, I.2    Sancar, A.3    Walsh, C.4
  • 50
    • 0030580949 scopus 로고    scopus 로고
    • Purification and characterization of Drosophila melanogaster photolyase
    • 50. Kim, S.T., Malhotra, K., Ryo, H., Sancar, A. & Todo, T. (1996) Purification and characterization of Drosophila melanogaster photolyase. Mutat. Res. 363, 97-104.
    • (1996) Mutat. Res. , vol.363 , pp. 97-104
    • Kim, S.T.1    Malhotra, K.2    Ryo, H.3    Sancar, A.4    Todo, T.5
  • 51
    • 0024758607 scopus 로고
    • Expression of an Anacystis nidulans photolyase gene in Escherichia coli; functional complementation and modified action spectrum of photoreactivation
    • 51. Takao, M., Oikawa, A., Eker, A.P. & Yasui, A. (1989) Expression of an Anacystis nidulans photolyase gene in Escherichia coli; functional complementation and modified action spectrum of photoreactivation. Photochem. Photobiol. 50, 633-637.
    • (1989) Photochem. Photobiol. , vol.50 , pp. 633-637
    • Takao, M.1    Oikawa, A.2    Eker, A.P.3    Yasui, A.4
  • 52
    • 0000366414 scopus 로고
    • UV-B-inducible and temperature-sensitive photoreactivation of cyclobutane pyrimidine-dimers in Arabidopsis thaliana
    • 52. Pang, Q. & Hays, J.B. (1991) UV-B-inducible and temperature-sensitive photoreactivation of cyclobutane pyrimidine-dimers in Arabidopsis thaliana. Plant Physiol. 95, 536-543.
    • (1991) Plant Physiol. , vol.95 , pp. 536-543
    • Pang, Q.1    Hays, J.B.2
  • 53
    • 0015970511 scopus 로고
    • Action spectrum for enzymatic photoreactivation in maize
    • 53. Ikenaga, M. & Kondo, S. (1974) Action spectrum for enzymatic photoreactivation in maize. Photochem. Photobiol. 74, 109-113.
    • (1974) Photochem. Photobiol. , vol.74 , pp. 109-113
    • Ikenaga, M.1    Kondo, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.