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Volumn 33, Issue 1, 2004, Pages 25-33

Cloning, expression, and purification of glyoxysomal 3-oxoacyl-CoA thiolase from sunflower cotyledons

Author keywords

Expression; Glyoxysomal thiolase; Purification; Sunflower

Indexed keywords

BACTERIA (MICROORGANISMS); CUCUMIS; CUCUMIS SATIVUS; HELIANTHUS; HELIANTHUS ANNUUS;

EID: 0348227644     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2003.08.022     Document Type: Article
Times cited : (7)

References (29)
  • 1
    • 0026757898 scopus 로고
    • Phylogenetic analysis of the thiolase family. Implications for the evolutionary origin of peroxisomes
    • J.C. Igual, C. Gonzalez-Bosch, J. Dopazo, J.E. Perez-Ortin, Phylogenetic analysis of the thiolase family. Implications for the evolutionary origin of peroxisomes, J. Mol. Evol. 35 (1992) 147-155.
    • (1992) J. Mol. Evol. , vol.35 , pp. 147-155
    • Igual, J.C.1    Gonzalez-Bosch, C.2    Dopazo, J.3    Perez-Ortin, J.E.4
  • 2
    • 0018968504 scopus 로고
    • Purification of glyoxysomal acetyl-CoA acyltransferase
    • J. Frevert, H. Kindl, Purification of glyoxysomal acetyl-CoA acyltransferase, Hoppe Seylers Z Physiol. Chem. 361 (1980) 537-542.
    • (1980) Hoppe Seylers Z Physiol. Chem. , vol.361 , pp. 537-542
    • Frevert, J.1    Kindl, H.2
  • 3
    • 0026478927 scopus 로고
    • Fatty acid degradation in plants
    • B. Gerhardt, Fatty acid degradation in plants, Progr. Lipid Res. 31 (1992) 417-446.
    • (1992) Progr. Lipid Res. , vol.31 , pp. 417-446
    • Gerhardt, B.1
  • 4
    • 0002310038 scopus 로고
    • β-Oxidation of fatty acids by specific organelles
    • P.K. Stumpf (Ed.), Academic Press, London
    • H. Kindl, β-Oxidation of fatty acids by specific organelles, in: P.K. Stumpf (Ed.), The Biochemistry of Plants: A Comprehensive Treatise, Academic Press, London, 1987, pp. 31-52.
    • (1987) The Biochemistry of Plants: A Comprehensive Treatise , pp. 31-52
    • Kindl, H.1
  • 5
    • 0027360304 scopus 로고
    • Effects of glucose starvation on the oxidation of fatty acids by maize root tip mitochondria and peroxisomes: Evidence for mitochondrial fatty acid β-oxidation and acyl-CoA dehydrogenase activity in a higher plant
    • M. Dieuaide, I. Couee, A. Pradet, P. Raymond, Effects of glucose starvation on the oxidation of fatty acids by maize root tip mitochondria and peroxisomes: evidence for mitochondrial fatty acid β-oxidation and acyl-CoA dehydrogenase activity in a higher plant, Biochem. J. 296 (1993) 199-207.
    • (1993) Biochem. J. , vol.296 , pp. 199-207
    • Dieuaide, M.1    Couee, I.2    Pradet, A.3    Raymond, P.4
  • 7
    • 0036138649 scopus 로고    scopus 로고
    • Pathways of straight and branched chain fatty acid catabolism in higher plants
    • I.A. Graham, P.J. Eastmond, Pathways of straight and branched chain fatty acid catabolism in higher plants, Progr. Lipid Res. 41 (2002) 156-181.
    • (2002) Progr. Lipid Res. , vol.41 , pp. 156-181
    • Graham, I.A.1    Eastmond, P.J.2
  • 8
    • 0020002339 scopus 로고
    • Mitochondrial and peroxisomal, β-oxidation of fatty acids in rat liver
    • H. Kindl, P.B. Lazarow (Eds.), Peroxisomes and Glyoxysomes
    • G.P. Mannaerts, L.J. Debeer, Mitochondrial and peroxisomal, β-oxidation of fatty acids in rat liver in: H. Kindl, P.B. Lazarow (Eds.), Peroxisomes and Glyoxysomes, Ann. NY Acad. Sci. 386 (1986) 30-39.
    • (1986) Ann. NY Acad. Sci. , vol.386 , pp. 30-39
    • Mannaerts, G.P.1    Debeer, L.J.2
  • 9
    • 0019349080 scopus 로고
    • Peroxisomes and glyoxysomes
    • N.E. Tolbert, Peroxisomes and glyoxysomes, Ann. Rev. Biochem. 50 (1981) 133-157.
    • (1981) Ann. Rev. Biochem. , vol.50 , pp. 133-157
    • Tolbert, N.E.1
  • 10
    • 0001592899 scopus 로고
    • Metabolic production of sucrose from fat
    • H. Beevers, Metabolic production of sucrose from fat, Nature 191 (1961) 433-436.
    • (1961) Nature , vol.191 , pp. 433-436
    • Beevers, H.1
  • 11
    • 0014670328 scopus 로고
    • Mitochondria and glyoxysomes from castor bean endosperm. Enzyme constituents and catalytic capacity
    • T.G. Cooper, H. Beevers, Mitochondria and glyoxysomes from castor bean endosperm. Enzyme constituents and catalytic capacity, J. Biol. Chem. 244 (1969) 3507-3513.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3507-3513
    • Cooper, T.G.1    Beevers, H.2
  • 12
    • 0014670256 scopus 로고
    • β-Oxidation in glyoxysomes from castor bean endosperm
    • T.G. Cooper, H. Beevers, β-Oxidation in glyoxysomes from castor bean endosperm, J. Biol. Chem. 244 (1969) 3514-3520.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3514-3520
    • Cooper, T.G.1    Beevers, H.2
  • 13
    • 0036483489 scopus 로고    scopus 로고
    • Glyoxysomal acetoacetyl-CoA thiolase and 3-oxoacyl-CoA thiolase from sunflower cotyledons
    • S. Oeljeklaus, K. Fischer, B. Gerhardt, Glyoxysomal acetoacetyl-CoA thiolase and 3-oxoacyl-CoA thiolase from sunflower cotyledons, Planta 214 (2002) 597-607.
    • (2002) Planta , vol.214 , pp. 597-607
    • Oeljeklaus, S.1    Fischer, K.2    Gerhardt, B.3
  • 14
    • 0029416813 scopus 로고
    • [β]-Oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: A century of continued progress
    • W.-H. Kunau, V. Dommes, H. Schulz, [β]-Oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: a century of continued progress, Progr. Lipid Res. 34 (1995) 267-342.
    • (1995) Progr. Lipid Res. , vol.34 , pp. 267-342
    • Kunau, W.-H.1    Dommes, V.2    Schulz, H.3
  • 15
    • 0032004229 scopus 로고    scopus 로고
    • 2,4-Dichlorophenoxybutyric acid-resistant mutants of Arabidopsis have defects in glyoxysomal fatty acid β-oxidation
    • M. Hayashi, K. Toriyama, M. Kondo, M. Nishimura, 2,4- Dichlorophenoxybutyric acid-resistant mutants of Arabidopsis have defects in glyoxysomal fatty acid β-oxidation, Plant Cell 10 (1998) 183-195.
    • (1998) Plant Cell , vol.10 , pp. 183-195
    • Hayashi, M.1    Toriyama, K.2    Kondo, M.3    Nishimura, M.4
  • 16
    • 0027587066 scopus 로고
    • Thiolase mRNA translated in vitro yields a peptide with a putative N-terminal presequence
    • R. Preisig-Muller, H. Kindl, Thiolase mRNA translated in vitro yields a peptide with a putative N-terminal presequence, Plant Mol. Biol. 22 (1993) 59-66.
    • (1993) Plant Mol. Biol. , vol.22 , pp. 59-66
    • Preisig-Muller, R.1    Kindl, H.2
  • 17
    • 0029346871 scopus 로고
    • Peroxisomal thiolase mRNA is induced during mango fruit ripening
    • G. Bojorquez, M.A. Gomez-Lim, Peroxisomal thiolase mRNA is induced during mango fruit ripening, Plant Mol. Biol. 28 (1995) 811-820.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 811-820
    • Bojorquez, G.1    Gomez-Lim, M.A.2
  • 18
    • 0030199279 scopus 로고    scopus 로고
    • cDNA cloning and expression of a gene for 3-ketoacyl-CoA thiolase in pumpkin cotyledons
    • A. Kato, M. Hayashi, Y. Takeuchi, M. Nishimura, cDNA cloning and expression of a gene for 3-ketoacyl-CoA thiolase in pumpkin cotyledons, Plant Mol. Biol. 31 (1996) 843-852.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 843-852
    • Kato, A.1    Hayashi, M.2    Takeuchi, Y.3    Nishimura, M.4
  • 19
    • 0030854991 scopus 로고    scopus 로고
    • The glyoxysomal 3-ketoacyl-CoA thiolase precursor from Brassica napus has enzymatic activity when synthesized in Escherichia coli
    • C. Olesen, K.K. Thomsen, I. Svendsen, A. Brandt, The glyoxysomal 3-ketoacyl-CoA thiolase precursor from Brassica napus has enzymatic activity when synthesized in Escherichia coli, FEBS Lett. 412 (1997) 138-140.
    • (1997) FEBS Lett. , vol.412 , pp. 138-140
    • Olesen, C.1    Thomsen, K.K.2    Svendsen, I.3    Brandt, A.4
  • 20
    • 0034782175 scopus 로고    scopus 로고
    • Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid β-oxidation and breakdown of triacylglycerol in lipid bodies of Arabidopsis seedlings
    • V. Germain, E.L. Rylott, T.R. Larson, S.M. Sherson, N. Bechtold, J.P. Carde, J.H. Bryce, I.A. Graham, S.M. Smith, Requirement for 3-ketoacyl-CoA thiolase-2 in peroxisome development, fatty acid β-oxidation and breakdown of triacylglycerol in lipid bodies of Arabidopsis seedlings, Plant J. 28 (2001) 1-12.
    • (2001) Plant J. , vol.28 , pp. 1-12
    • Germain, V.1    Rylott, E.L.2    Larson, T.R.3    Sherson, S.M.4    Bechtold, N.5    Carde, J.P.6    Bryce, J.H.7    Graham, I.A.8    Smith, S.M.9
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0001372764 scopus 로고    scopus 로고
    • A full length cDNA encoding 3-ketoacyl-CoA thiolase from Brassica napus (Accesssion No. X93015) (PGR 95-137)
    • C. Olesen, A. Brandt, A full length cDNA encoding 3-ketoacyl-CoA thiolase from Brassica napus (Accesssion No. X93015) (PGR 95-137), Plant Physiol. 110 (1996) 714.
    • (1996) Plant Physiol. , vol.110 , pp. 714
    • Olesen, C.1    Brandt, A.2
  • 23
    • 0025248867 scopus 로고
    • The reaction of acetyldithio-CoA, a readily enolized analog of acetyl- CoA with thiolase from Zoogloea ramigera
    • V. Anderson, B. Bahnson, I. Wlassics, C. Walsh, The reaction of acetyldithio-CoA, a readily enolized analog of acetyl- CoA with thiolase from Zoogloea ramigera, J. Biol. Chem. 265 (1990) 6255-6261.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6255-6261
    • Anderson, V.1    Bahnson, B.2    Wlassics, I.3    Walsh, C.4
  • 24
    • 0026746281 scopus 로고
    • Biosynthetic thiolase from Zoogloea ramigera. Mutagenesis of the putative active-site base Cys-378 to Ser-378 changes the partitioning of the acetyl S-enzyme intermediate
    • S. Williams, M. Palmer, O. Peoples, C. Walsh, A. Sinskey, S. Masamune, Biosynthetic thiolase from Zoogloea ramigera. Mutagenesis of the putative active-site base Cys-378 to Ser-378 changes the partitioning of the acetyl S-enzyme intermediate, J. Biol. Chem. 267 (1992) 16041-16043.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16041-16043
    • Williams, S.1    Palmer, M.2    Peoples, O.3    Walsh, C.4    Sinskey, A.5    Masamune, S.6
  • 25
    • 0031592777 scopus 로고    scopus 로고
    • The 1.8 a crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: Implications for substrate binding and reaction mechanism
    • M. Mathieu, Y. Modis, J.P. Zeelen, C.K. Engel, R.A. Abagyan, A. Ahlberg, B. Rasmussen, V.S. Lamzin, W.H. Kunau, R.K. Wierenga, The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism, J. Mol. Biol. 273 (1997) 714-728.
    • (1997) J. Mol. Biol. , vol.273 , pp. 714-728
    • Mathieu, M.1    Modis, Y.2    Zeelen, J.P.3    Engel, C.K.4    Abagyan, R.A.5    Ahlberg, A.6    Rasmussen, B.7    Lamzin, V.S.8    Kunau, W.H.9    Wierenga, R.K.10
  • 27
    • 0023548002 scopus 로고
    • Identification of a peroxisomal targeting signal at the carboxy terminus of firefly luciferase
    • S. Gould, G. Keller, S. Subramani, Identification of a peroxisomal targeting signal at the carboxy terminus of firefly luciferase, J. Cell Biol. 105 (1987) 2923-2931.
    • (1987) J. Cell Biol. , vol.105 , pp. 2923-2931
    • Gould, S.1    Keller, G.2    Subramani, S.3
  • 28
    • 0026526811 scopus 로고
    • Targeting of proteins into the peroxisomal matrix
    • S. Subramani, Targeting of proteins into the peroxisomal matrix, J. Membr. Biol. 125 (1992) 99-106.
    • (1992) J. Membr. Biol. , vol.125 , pp. 99-106
    • Subramani, S.1
  • 29
    • 0025941962 scopus 로고
    • A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase
    • B.W. Swinkels, S.J. Gould, A.G. Bodnar, R.A. Rachubinski, S. Subramani, A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase, EMBO J. 10 (1991) 3255-3262.
    • (1991) EMBO J. , vol.10 , pp. 3255-3262
    • Swinkels, B.W.1    Gould, S.J.2    Bodnar, A.G.3    Rachubinski, R.A.4    Subramani, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.