Peroxisomal thiolase mRNA is induced during mango fruit ripening

Bojorquez, Guadalupe; Gómez-Lim, Miguel Á.

doi:10.1007/bf00042067

Cited by 31 publications

(5 citation statements)

References 27 publications

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“…In higher plants, these fatty acids metabolism reactions occur mostly in the peroxisomes. The identiied mango thiolase in this study is in close agreement with peroxisomal thiolase isolated by Bojorquez and Gomez-Lim [57] from ripening mango fruits with 430 amino acid residues and a molecular weight of 45,743 Da. The changes in the fatty acids may be associated with the production of aromatic volatile during mango ripening.…”

Section: Ethylene Synthesis and Aromatic Volatilessupporting

confidence: 89%

Comparative Proteomic Analysis on Fruit Ripening Processes in Two Varieties of Tropical Mango (Mangifera indica)

et al. 2019

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Section: Ethylene Synthesis and Aromatic Volatilessupporting

confidence: 89%

Comparative Proteomic Analysis on Fruit Ripening Processes in Two Varieties of Tropical Mango (Mangifera indica)

et al. 2019

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“…Alignment of the amino-terminal sequence of pumpkin thiolase with those of other microbody proteins that are synthesized as larger precursors. PTH10, pumpkin thiolase; CTHIO, cucumber thiolase [25]; MFTHIO, mango fruit thiolase [3]; RPTHIO, rat peroxisomal thiolase A [13]; WMGMDH, watermelon glyoxysoreal malate dehydrogenase [7]; PGCS, pumpkin glyoxysomal citrate synthase [15]. Conserved amino acids are showed in bold letters.…”

Section: Changes In the Levels O/'the Mrna For Thiolase And The Encodmentioning

confidence: 99%

cDNA cloning and expression of a gene for 3-ketoacyl-CoA thiolase in pumpkin cotyledons

et al. 1996

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A cDNA clone for 3-ketoacyl-CoA thiolase (EC 2.3.1.16) was isolated from a lambda gt11 cDNA library constructed from the poly(A)+ RNA of etiolated pumpkin cotyledons. The cDNA insert contained 1682 nucleotides and encoded 461 amino acid residues. A study of the expression in vitro of the cDNA and analysis of the amino-terminal sequence of the protein indicated that pumpkin thiolase is synthesized as a precursor which has a cleavable amino-terminal presequence of 33 amino acids. The amino-terminal presequence was highly homologous to typical amino-terminal signals that target proteins to microbodies. Immunoblot analysis showed that the amount of thiolase increased markedly during germination but decreased dramatically during the light-inducible transition of microbodies from glyoxysomes to leaf peroxisomes. By contrast, the amount of mRNA increased temporarily during the early stage of germination. In senescing cotyledons, the levels of the thiolase mRNA and protein increased again with the reverse transition of microbodies from leaf peroxisomes to glyoxysomes, but the pattern of accumulation of the protein was slightly different from that of malate synthase. These results indicate that expression of the thiolase is regulated in a similar manner to that of other glyoxysomal enzymes, such as malate synthase and citrate synthase, during seed germination and post-germination growth. By contrast, during senescence, expression of the thiolase is regulated in a different manner from that of other glyoxysomal enzymes.

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“…The catalytic and molecular properties of the two former components have been studied intensively (Frevert and Kindl 1980a;Miernyk and Trelease 1981;Gerhardt 1985;Kirsch et al 1986;Behrends et al 1988;GuÈ hnemann-SchaÈ fer et al 1994;Preisig-MuÈ ller et al 1994; GuÈ hnemann-SchaÈ fer and Kindl 1995;Hooks et al 1996;Hayashi et al 1998Hayashi et al , 1999. Available information on the glyoxysomal thiolase predominantly refers to the isolation of cDNA clones encoding the thiolase, to thiolase biosynthesis and related aspects (Preisig-MuÈ ller and Kindl 1993;Bojorquez and Gomez-Lim 1995;Olesen and Brandt 1995;Kato et al 1996;Olesen et al 1997). Information regarding the catalytic properties of the glyoxysomal thiolase is scarce.…”

Section: Introductionmentioning

confidence: 98%

Glyoxysomal acetoacetyl-CoA thiolase and 3-oxoacyl-CoA thiolase from sunflower cotyledons

Oeljeklaus

Fischer

Gerhardt

2002

Planta

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Following chromatography on hydroxyapatite, the elution profile of the thiolase activity of the glyoxysomal fraction from sunflower (Helianthus annuus L.) cotyledons exhibited two peaks when the enzyme activity was assayed with acetoacetyl-CoA as substrate. Only one of these two activity peaks was detectable when a long-chain thiolase substrate was used in the activity assay. The proteins (thiolase I and thiolase II) underlying the two activity peaks detected with acetoacetyl-CoA were of glyoxysomal origin. They were purified using glyoxysomal matrices as starting material, and biochemically characterized. Thiolase I is an acetoacetyl-CoA thiolase (EC 2.3.1.9) exhibiting activity only towards acetoacetyl-CoA (Km = 11 microM). Its contribution to the total glyoxysomal thiolytic activity towards acetoacetyl-CoA amounted to about 15%. Thiolase II is a 3-oxoacyl-CoA thiolase (EC 2.3.1.16). The activity of the enzyme towards 3-oxoacyl-CoAs increased with increasing chain length of the substrate. Thiolase II exhibited a Km value of 27 microM with acetoacetyl-CoA as substrate. and Km values between 3 and 7 microM with substrates having a carbon chain length from 6 to 16 carbon atoms. The thiolase activity of the glyoxysomes towards acetoacetyl-CoA and 3-oxopalmitoyl-CoA exceeded the glyoxysomal butyryl-CoA and palmitoyl-CoA beta-oxidation rates, respectively, by about 10-fold at all substrate concentrations employed (1-15 microM).

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Peroxisomal thiolase mRNA is induced during mango fruit ripening

Cited by 31 publications

References 27 publications

Comparative Proteomic Analysis on Fruit Ripening Processes in Two Varieties of Tropical Mango (Mangifera indica)

Comparative Proteomic Analysis on Fruit Ripening Processes in Two Varieties of Tropical Mango (Mangifera indica)

cDNA cloning and expression of a gene for 3-ketoacyl-CoA thiolase in pumpkin cotyledons

Glyoxysomal acetoacetyl-CoA thiolase and 3-oxoacyl-CoA thiolase from sunflower cotyledons

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