메뉴 건너뛰기




Volumn 8, Issue 2, 1996, Pages 183-190

Cloning of Chalcone-Flavanone isomerase cDNA from Pueraria lobata and its overexpression in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; LOBATA; PHASEOLUS VULGARIS; PUERARIA; PUERARIA MONTANA VAR. LOBATA;

EID: 0030250197     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1996.0091     Document Type: Article
Times cited : (13)

References (40)
  • 1
    • 0021237824 scopus 로고
    • Transcription of plant defence genes in response to UV light or fungal elicitor
    • 1. Chappell, J., and Hahlbrock, K. (1982) Transcription of plant defence genes in response to UV light or fungal elicitor. Nature (London) 311, 76-79.
    • (1982) Nature (London) , vol.311 , pp. 76-79
    • Chappell, J.1    Hahlbrock, K.2
  • 2
    • 0001576084 scopus 로고
    • The phytoalexins response: Elicitation, signalling and control of host gene expression
    • 2. Dixon, R. A. (1986) The phytoalexins response: Elicitation, signalling and control of host gene expression. Biol. Rev. 61, 239-291.
    • (1986) Biol. Rev. , vol.61 , pp. 239-291
    • Dixon, R.A.1
  • 3
    • 0022470295 scopus 로고
    • A plant flavone, luteolin, induces expression of Rhizobium meliloti nodulation genes
    • 3. Peters, N. K., Frost, J. W., and Long, S. R. (1986) A plant flavone, luteolin, induces expression of Rhizobium meliloti nodulation genes. Science 233, 977-980.
    • (1986) Science , vol.233 , pp. 977-980
    • Peters, N.K.1    Frost, J.W.2    Long, S.R.3
  • 4
    • 0021764607 scopus 로고
    • Induction of chalcone isomerase in elicitor-treated bean cells. Comparison of rates of synthesis and appearence of immunodetectable enzyme
    • 4. Robbins, M. P., and Dixon, R. A. (1984) Induction of chalcone isomerase in elicitor-treated bean cells. Comparison of rates of synthesis and appearence of immunodetectable enzyme. Eur. J. Biochem. 145, 195-202.
    • (1984) Eur. J. Biochem. , vol.145 , pp. 195-202
    • Robbins, M.P.1    Dixon, R.A.2
  • 5
    • 0001083755 scopus 로고
    • Elicitor-mediated induction of chalcone isomerase in Phaseolus vulgaris cell suspension cultures
    • 5. Dixon, R. A., Gerrish, C., Lamb, C. J., and Robbins, M. P. (1983) Elicitor-mediated induction of chalcone isomerase in Phaseolus vulgaris cell suspension cultures. Planta 159, 561-569.
    • (1983) Planta , vol.159 , pp. 561-569
    • Dixon, R.A.1    Gerrish, C.2    Lamb, C.J.3    Robbins, M.P.4
  • 6
    • 0014810955 scopus 로고
    • Stereochemistry of the enzymatic cyclization of 4,2′,4′-trihydroxychalcone to 7,4′-dihydroxyflavanone by isomerases from mung bean seedlings
    • 6. Hahlbrock, K., Zilg, H., and Grisebach, H. (1970) Stereochemistry of the enzymatic cyclization of 4,2′,4′-trihydroxychalcone to 7,4′-dihydroxyflavanone by isomerases from mung bean seedlings. Eur. J. Biochem. 15, 13-18.
    • (1970) Eur. J. Biochem. , vol.15 , pp. 13-18
    • Hahlbrock, K.1    Zilg, H.2    Grisebach, H.3
  • 7
    • 0000110117 scopus 로고
    • Co-ordinated synthesis of phytoalexin biosynthetic enzymes in biologically-stressed cells of bean (Phaseolus vulgaris L.)
    • 7. Cramer, C. L., Bell, J. N., Ryder, T. B., Bailey, J. A., Schuch, W., Boldwell, G. P., Robbins, M. P., Dixon, R. A., and Lamb, C. J. (1985) Co-ordinated synthesis of phytoalexin biosynthetic enzymes in biologically-stressed cells of bean (Phaseolus vulgaris L.). EMBO J. 4, 285-289.
    • (1985) EMBO J. , vol.4 , pp. 285-289
    • Cramer, C.L.1    Bell, J.N.2    Ryder, T.B.3    Bailey, J.A.4    Schuch, W.5    Boldwell, G.P.6    Robbins, M.P.7    Dixon, R.A.8    Lamb, C.J.9
  • 8
    • 85000979631 scopus 로고
    • Chalcone isomerase cDNA cloning and mRNA induction by fungal elicitor, wounding and infection
    • 8. Mehdy, M. C., and Lamb, C. J. (1987) Chalcone isomerase cDNA cloning and mRNA induction by fungal elicitor, wounding and infection. EMBO J. 6, 1527-1533.
    • (1987) EMBO J. , vol.6 , pp. 1527-1533
    • Mehdy, M.C.1    Lamb, C.J.2
  • 9
    • 0024288251 scopus 로고
    • Purification and characterization of chalcone isomerase from soybeans
    • 9. Bednar, R. A., and Hadcock, J. R. (1988) Purification and characterization of chalcone isomerase from soybeans. J. Biol. Chem. 263, 9582-9588.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9582-9588
    • Bednar, R.A.1    Hadcock, J.R.2
  • 10
    • 0024978434 scopus 로고
    • Chemical modification of chalcone isomerase by mercurials and tetrathionate. Evidence for a single cysteine residue in the active site
    • 10. Bednar, R. A., Fried, W. B., Lock, Y. W., and Pramanik, B. (1989) Chemical modification of chalcone isomerase by mercurials and tetrathionate. Evidence for a single cysteine residue in the active site. J. Biol. Chem. 264, 14272-14276.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14272-14276
    • Bednar, R.A.1    Fried, W.B.2    Lock, Y.W.3    Pramanik, B.4
  • 11
    • 0003045533 scopus 로고
    • Mechanism of action of chalcone isomerase
    • 11. Boland, M. J., and Wong, E. (1979) Mechanism of action of chalcone isomerase. Bioorg. Chem. 8, 1-8.
    • (1979) Bioorg. Chem. , vol.8 , pp. 1-8
    • Boland, M.J.1    Wong, E.2
  • 13
    • 0025172926 scopus 로고
    • Chemical modification of chalcone isomerase by diethyl pyrocarbonate: Histidine residues are not essential for catalysis
    • 13. Bednar, R. A., and Adeniran, A. (1990) Chemical modification of chalcone isomerase by diethyl pyrocarbonate: Histidine residues are not essential for catalysis. Arch. Biochem. Biophys. 282, 393-398.
    • (1990) Arch. Biochem. Biophys. , vol.282 , pp. 393-398
    • Bednar, R.A.1    Adeniran, A.2
  • 14
    • 0026184759 scopus 로고
    • Introduction of unnatural amino acids into chalcone isomerase
    • 14. Bednar, R. A., McCafferey, and Shan, K. (1991) Introduction of unnatural amino acids into chalcone isomerase. Bioconjugate Chem. 2, 211-216.
    • (1991) Bioconjugate Chem. , vol.2 , pp. 211-216
    • Bednar, R.A.1    McCafferey2    Shan, K.3
  • 15
    • 0028156015 scopus 로고
    • Isolation and characterization of a maize gene encoding chalcone flavanone isomerase
    • 15. Grotewold, E., and Peterson, T. (1994) Isolation and characterization of a maize gene encoding chalcone flavanone isomerase. Mol Gen. Genet. 242, 1-8.
    • (1994) Mol Gen. Genet. , vol.242 , pp. 1-8
    • Grotewold, E.1    Peterson, T.2
  • 17
    • 0028388172 scopus 로고
    • Isolation of chalcone synthase and chalcone isomerase cDNAs from alfalfa (Medicago sativa L.): Highest transcript levels occur in young roots and root tips
    • 17. McKhann, H. I., and Hirsh, A. M. (1994) Isolation of chalcone synthase and chalcone isomerase cDNAs from alfalfa (Medicago sativa L.): Highest transcript levels occur in young roots and root tips. Plant Mol. Biol. 24, 767-777.
    • (1994) Plant Mol. Biol. , vol.24 , pp. 767-777
    • McKhann, H.I.1    Hirsh, A.M.2
  • 18
    • 0024003334 scopus 로고
    • Cloning of the two chalcone flavanone isomerase genes from Petunia hybrida: Coordinate, light-regulated and differential expression of flavonoid genes
    • 18. van Tunen, A. J., Koes, R. E., Spelt, C. E., van der Krol, A. R., Stuitje, A. R., and Mol, J. N. M. (1988) Cloning of the two chalcone flavanone isomerase genes from Petunia hybrida: Coordinate, light-regulated and differential expression of flavonoid genes. EMBO J. 7, 1257-1263.
    • (1988) EMBO J. , vol.7 , pp. 1257-1263
    • Van Tunen, A.J.1    Koes, R.E.2    Spelt, C.E.3    Van Der Krol, A.R.4    Stuitje, A.R.5    Mol, J.N.M.6
  • 19
    • 0001637464 scopus 로고
    • Regulation of chalcone flavanone isomerase (CHI) gene expression in Petunia hybrida: The use of alternative promoters in corolla anthers and pollen
    • 19. van Tunen, A. J., Hartman, S. A., Mur, L. A., and Mol, J. N. M. (1989) Regulation of chalcone flavanone isomerase (CHI) gene expression in Petunia hybrida: The use of alternative promoters in corolla anthers and pollen. Plant Mol. Biol. 12, 539-551.
    • (1989) Plant Mol. Biol. , vol.12 , pp. 539-551
    • Van Tunen, A.J.1    Hartman, S.A.2    Mur, L.A.3    Mol, J.N.M.4
  • 20
    • 0026090822 scopus 로고
    • Sequence analysis of a chalcone isomerase cDNA of Phaseolus vulgaris L
    • 20. Blyden, E. R., Doerner, P. W., Lamb, C. J., and Dixon, A. R. (1991) Sequence analysis of a chalcone isomerase cDNA of Phaseolus vulgaris L. Plant Mol. Biol. 16, 167-169.
    • (1991) Plant Mol. Biol. , vol.16 , pp. 167-169
    • Blyden, E.R.1    Doerner, P.W.2    Lamb, C.J.3    Dixon, A.R.4
  • 21
    • 0028407336 scopus 로고
    • A cDNA encoding chalcone isomerase from aged pea epicotyls
    • 21. Wood, A. J., and Davies, E. (1994) A cDNA encoding chalcone isomerase from aged pea epicotyls. Plant Physiol. 104, 1465-1466.
    • (1994) Plant Physiol. , vol.104 , pp. 1465-1466
    • Wood, A.J.1    Davies, E.2
  • 22
    • 0028386531 scopus 로고
    • Cloning and molecuar analysis of structural genes involved in flavonoid and stilbene biosynthesis in grape (Vitis vinifera L.)
    • 22. Sparvoli, F., Martin, C., Scienza, A., Gavazzi, G., and Tonelli, C. (1994) Cloning and molecuar analysis of structural genes involved in flavonoid and stilbene biosynthesis in grape (Vitis vinifera L.). Plant Mol. Biol. 24, 743-755.
    • (1994) Plant Mol. Biol. , vol.24 , pp. 743-755
    • Sparvoli, F.1    Martin, C.2    Scienza, A.3    Gavazzi, G.4    Tonelli, C.5
  • 23
    • 0001544155 scopus 로고
    • Deoxychalcone synthase from cell suspension cultures of Pueraria lobata
    • 23. Hakamatsuka, T., Noguchi, H., Ebizuka, Y., and Sankawa, U. (1988) Deoxychalcone synthase from cell suspension cultures of Pueraria lobata. Chem. Pharm. Bull. 36, 4225-4228.
    • (1988) Chem. Pharm. Bull. , vol.36 , pp. 4225-4228
    • Hakamatsuka, T.1    Noguchi, H.2    Ebizuka, Y.3    Sankawa, U.4
  • 24
    • 85011154768 scopus 로고
    • Isoflavone synthase from cell suspension cultures of Pueraria lobata
    • 24. Hakamatsuka, T., Noguchi, H., Ebizuka, Y., and Sankawa, U. (1989) Isoflavone synthase from cell suspension cultures of Pueraria lobata. Chem. Pharm. Bull. 37, 249-252.
    • (1989) Chem. Pharm. Bull. , vol.37 , pp. 249-252
    • Hakamatsuka, T.1    Noguchi, H.2    Ebizuka, Y.3    Sankawa, U.4
  • 25
    • 0025163193 scopus 로고
    • Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis
    • 25. Hashim, M. F., Hakamatsuka, T., Ebizuka, Y., and Sankawa, U. (1990) Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis. FEBS Lett. 271, 219-222.
    • (1990) FEBS Lett. , vol.271 , pp. 219-222
    • Hashim, M.F.1    Hakamatsuka, T.2    Ebizuka, Y.3    Sankawa, U.4
  • 26
    • 0025100554 scopus 로고
    • Isoflavone synthase from cell suspension cultures of Pueraria lobata
    • 26. Hakamatsuka, T., Noguchi, H., Ebizuka, Y., and Sankawa, U. (1990) Isoflavone synthase from cell suspension cultures of Pueraria lobata. Chem. Pharm. Bull. 38, 1942-1945.
    • (1990) Chem. Pharm. Bull. , vol.38 , pp. 1942-1945
    • Hakamatsuka, T.1    Noguchi, H.2    Ebizuka, Y.3    Sankawa, U.4
  • 27
    • 0025884986 scopus 로고
    • P-450-dependent oxidative rearrangeement in isoflavone biosynthesis: Reconstitution of P-450 and NADPH:P-450 reductase
    • 27. Hakamatsuka, T., Hashim, M. F., Ebizuka, Y., and Sankawa, U. (1991) P-450-dependent oxidative rearrangeement in isoflavone biosynthesis: Reconstitution of P-450 and NADPH:P-450 reductase. Tetrahedron 47, 5969-5978.
    • (1991) Tetrahedron , vol.47 , pp. 5969-5978
    • Hakamatsuka, T.1    Hashim, M.F.2    Ebizuka, Y.3    Sankawa, U.4
  • 28
    • 0001308550 scopus 로고
    • Isoflavone dimers from yeast extract-treated cell suspension cultures of Pueraria lobata
    • 28. Hakamatsuka, T., Shinkai, K., Noguchi, H., Ebizuka, Y., and Sankawa, U. (1992) Isoflavone dimers from yeast extract-treated cell suspension cultures of Pueraria lobata. Z. Naturforsh. 47c, 177-182.
    • (1992) Z. Naturforsh. , vol.47 C , pp. 177-182
    • Hakamatsuka, T.1    Shinkai, K.2    Noguchi, H.3    Ebizuka, Y.4    Sankawa, U.5
  • 29
    • 0010267370 scopus 로고
    • Recent progress in studies of the biosynthesis of isoflavonoids: Oxidative aryl migration during the formation of the isoflavone skeltone
    • 29. Hakamatsuka, T., and Sankawa, U. (1993) Recent progress in studies of the biosynthesis of isoflavonoids: Oxidative aryl migration during the formation of the isoflavone skeltone. J. Plant Res. 3, 129-144.
    • (1993) J. Plant Res. , vol.3 , pp. 129-144
    • Hakamatsuka, T.1    Sankawa, U.2
  • 30
    • 0025901113 scopus 로고
    • Isolation, sequence and bacterilal expression of a cDNA for chalcone synthase from the cultured cells of Pueraria lobata
    • 30. Nakajima, O., Akiyama, T., Hakamatsuka, T., Shibuya, M., Noguchi, H., Ebizuka, Y., and Sankawa, U. (1991) Isolation, sequence and bacterilal expression of a cDNA for chalcone synthase from the cultured cells of Pueraria lobata. Chem. Pharm. Bull. 39, 1911-1913.
    • (1991) Chem. Pharm. Bull. , vol.39 , pp. 1911-1913
    • Nakajima, O.1    Akiyama, T.2    Hakamatsuka, T.3    Shibuya, M.4    Noguchi, H.5    Ebizuka, Y.6    Sankawa, U.7
  • 32
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • 32. Chirgwin, J. M., Przybyla, A. E., MacDonald, R. J., and Rutter, W. J. (1979) Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18, 5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 34. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0016435597 scopus 로고
    • Purification and kinetic properties of chalcone-flavanone isomerase from soya bean
    • 35. Boland, M., and Wong, E. (1975) Purification and kinetic properties of chalcone-flavanone isomerase from soya bean. Eur. J. Biochem. 50, 383-389.
    • (1975) Eur. J. Biochem. , vol.50 , pp. 383-389
    • Boland, M.1    Wong, E.2
  • 36
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • 36. Frohman, M. A., Dush, M. K., and Martin, G. R. (1988) Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer. Proc. Natl. Acad. Sci. USA 85, 8998-9002.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 37
    • 0023659729 scopus 로고
    • All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II
    • 37. Maki, M., Takano, E., Mori, H., Sato, A., Murachi, T., and Hatanaka, M. (1987) All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II. FEBS Lett. 223, 174-180.
    • (1987) FEBS Lett. , vol.223 , pp. 174-180
    • Maki, M.1    Takano, E.2    Mori, H.3    Sato, A.4    Murachi, T.5    Hatanaka, M.6
  • 38
    • 0025283867 scopus 로고
    • Use of T7 polymerase to direct expression of cloned genes
    • 38. Studier, F. W., Roseberg, A. H., and Dunn, J. J. (1990) Use of T7 polymerase to direct expression of cloned genes. Methods Enzymol. 185, 60-89.
    • (1990) Methods Enzymol. , vol.185 , pp. 60-89
    • Studier, F.W.1    Roseberg, A.H.2    Dunn, J.J.3
  • 39
    • 0011978171 scopus 로고
    • Comparison of chalcone-flavanone isomerase heteroenzymes and isoenzymes
    • 39. Hahlbrock, K., Wong, E., Schul, L., and Grisebach, H. (1970) Comparison of chalcone-flavanone isomerase heteroenzymes and isoenzymes. Phytochemistry 9, 949-958.
    • (1970) Phytochemistry , vol.9 , pp. 949-958
    • Hahlbrock, K.1    Wong, E.2    Schul, L.3    Grisebach, H.4
  • 40
    • 0002155695 scopus 로고
    • Purification and properties of chalcone isomerase from cell suspension cultures of Phaseolus vulgaris
    • 40. Dixon, R. A., Dey, P. M., and Whitehead, I. M. (1982) Purification and properties of chalcone isomerase from cell suspension cultures of Phaseolus vulgaris. Biochim. Biophys. Acta 715, 25-33.
    • (1982) Biochim. Biophys. Acta , vol.715 , pp. 25-33
    • Dixon, R.A.1    Dey, P.M.2    Whitehead, I.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.