Purification and Characterization of ACC Oxidase and Its Expression during Ripening in Apple Fruit

Dilley, David R.; Kuai, Jianping; Poneleit, Loelle; Zhu, Yali; Pekker, Y.; Wilson, Ian; Burmeister, Douglas M.; Gran, Christopher D.; Bowers, Alex J.

doi:10.1007/978-94-017-1003-9_9

Cited by 22 publications

(16 citation statements)

References 11 publications

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“…Among those residues, Shaw et al (1996) demonstrated that H 177 , D 179 , and H 234 are essential for enzyme activity and suggested that they may act as the putative Fe(II)‐binding site. Another cofactor, CO 2 has also been shown to be necessary for ACC oxidase activity (Dong et al 1992b) via a carbamate formation (Dilley et al 1993; Fernandez‐Maculet et al 1993; Yang et al 1993). The amino acid R 300 of Pa ‐ ACO may be involved in the carbamate formation according to the hypothesis of Lay et al (1996).…”

Section: Resultsmentioning

confidence: 99%

Molecular cloning and expression of a cDNA encoding 1‐aminocyclopropane‐1‐carboxylate (ACC) oxidase from apricot fruit (Prunus armeniaca)

Mbéguié-A-Mbéguié¹,

Chahine²,

Gomez³

et al. 1999

Physiologia Plantarum

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Little is known on gene expression during ripening of apricot fruit (Prunus armeniaca cv. Bergeron), in particular for the enzymes involved in ethylene biosynthesis. ACC oxidase (EC 1.4.3) catalyses the last step of the ethylene biosynthesis pathway in higher plants. Based on sequence conservation of ACC oxidases, a reverse transcriptase‐polymerase chain reaction (RT‐PCR) experiment was carried out to synthesize a homologous ACC oxidase probe from apricot fruit. This probe was further used to isolate a full length ACC oxidase cDNA, Pa‐ACO, from a ripe fruit cDNA library. Pa‐ACO is 1 236 bp long and contains a single open reading frame encoding a mature peptide of 319 amino acids with a calculated molecular mass of 36.17 kDa and a pI of 5.07. Immunoblot analysis allowed us to associate a 40 kDa protein to apricot fruit ACC oxidase. Pa‐ACO belongs to a multi‐gene family, is fruit specific and is transcriptionally regulated during ripening of apricot fruit.

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Section: Resultsmentioning

confidence: 99%

Molecular cloning and expression of a cDNA encoding 1‐aminocyclopropane‐1‐carboxylate (ACC) oxidase from apricot fruit (Prunus armeniaca)

Mbéguié-A-Mbéguié¹,

Chahine²,

Gomez³

et al. 1999

Physiologia Plantarum

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“…The addition of cobalt, an inhibitor of ACC oxidase (Lau & Yang 1976, Dilley et al 1993, to the nutrient solution of either iron-deficient or iron-sufficient El07 pea seedlings inhibited the development of root Fe(III)-chelate reducing activity ( Figure 2 and Table 1). Similarly, the Fe(III)-chelate reducing capacity of iron-deficient El07 pea plants was inhibited by AOA (Figure 3), which inhibits the activity of ACC synthase (Yang & Hoffman 1984).…”

Section: Discussionmentioning

confidence: 99%

“…The conversion of SAM to ACC is catalysed by the enzyme ACC synthase, whose activity is inhibited by a number of chemicals, including AOA lYang & Hoffman 1984). The conversion of ACC to Ethylene and root Fe(lll)-chelate reductase activity ethylene is catalysed by ACC oxidase, whose activity is dependent upon Fe 2+ and is competitively inhibited by Co z + ions (Dilley et al 1993). SAM is a common biosynthetic precursor of ethylene (Yang & Hoffman 1984), polyamines (Even-chet et al 1982) and nicotianamine (Shojima et al 1990).…”

Section: Introductionmentioning

confidence: 99%

Ethylene involvement in the over-expression of Fe(III)-chelate reductase by roots of E107 pea [Pisum sativum L. (brz, brz)] and chloronerva tomato (Lycopersicon esculentum L.) mutant genotypes

et al. 1996

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Recently, ethylene was reported to be involved in the regulation of Fe(lll)-chelate reducing capacity by cucumber (Cucumis sativus L.) roots. Here, we studied the effect of two ethylene inhibitnrs, aminooxyacetic acid (AOA) and cobalt, on the Fe(lll) reducing capacity in roots of mutant genotypes [El07 pea [Pisum sativum L. (brz, brz)] and chloronerva tomato (Lycopers&on esculentum L.] that exhibit high rates of Fe(lll)-chelate reduction and excessive iron accumulation. The ethylene inhihitors, AOA and cobalt, markedly inhibited Fe(lll)-chelate reducing capacity in roots of both genotypes. Over-expression of root Fe(lll) reductase activity by both mutants appears to be related to ethylene. Possibly, both mutants are genetically defective in their ability to regulate root ethylene production. The large inhibitory effect of both ethylene inhibitors on Fe(lll)-ehelate reducing capacity in roots of the mutant tomato genotype, chloronerva, disputes the contention that the nicotianamine-Fe(ll) complex is the repressior of the gene responsible for Fe(llI)-chelate reductase activity, as previously suggested by others. However, since nicotianamine shares the same biosynthetic precursor as ethylene, i.e. S-adenosyl methionine, nicotianamine may affect Fe(lll)-ehelate reductase activity in dicot and non-grass monoeot roots by influencing ethylene biosynthesis.

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“…This enzyme requires iron for activation and is inhibited competitively by Co 2 + (Dilley et al 1993). This enzyme requires iron for activation and is inhibited competitively by Co 2 + (Dilley et al 1993).…”

Section: Iron Requiredtbr Stimulation Of Root Fe( Lll)-chelate Reducmentioning

confidence: 99%

“…The conversion of S-adenosyl methionine (SAM) to ACC is catalysed by ACC synthase which is inhibited by AOA, as well as by other substances (Yang & Hoffman 1984). ACC oxidase requires iron for activation and is competitively inhibited by Co 2+ (Dilley et al 1993). ACC oxidase requires iron for activation and is competitively inhibited by Co 2+ (Dilley et al 1993).…”

Section: Introductionmentioning

confidence: 99%

Iron requirement for and effects of promoters and inhibitors of ethylene action on stimulation of Fe(III)-chelate reductase in roots of strategy I species

et al. 1996

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Stimulation of root Fe(lll) reductase activity by iron additions to iron-deficient growth media may be the result of iron activation of I-aminocyclopropane-l-carboxylic acid (ACC) oxidase required for ethylene biosynthesis. Two different ethylene inhibitors, aminooxyacetic acid (AOA) (20 pM; ACC synthase inhibitor) and cobalt (3 pM COCI2; ACC oxidase inhibitor), were used to study the effects of iron supply and cobalt inhibition on ethylene action in controlling the activity of Fe(lll)-chelate reductase in pea (Pisum sativum L.) roots. Supplying 20 ~M Fe(lll)-N,/V-ethylenebis[2-(2-hydroxypheyl)-glycine [Fe(III)-EDDHA] to either cobalt-treated, iron-deficient Sparkle (normal parent) or El07 (brz mutant genotype) pea seedlings reversed the negative effects of cobalt on root Fe(lll)-reductase activity. Re-supplying 20 ~M Fe(III)-EDDHA to iron-deficient, AOA-treated seedlings did not enhance root (Fe(lll)-reductase. Apparently, cobalt competes with iron for the active site in ACC oxidase during ethylene synthesis. Inhibition of root reductase activity by cobalt treatment lowered manganese, zinc, magnesium and potassium content of mutant El07 pea seedlings. In contrast, iron enhancement of root reductase activity in iron-deficient, cobalt-treated El07 seedlings resulted in higher seedling accumulations of manganese, zinc, magnesium and potassium. These results support the hypothesis that root cell plasma membrane reduetase activity plays a role in cation uptake by root cells.

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Purification and Characterization of ACC Oxidase and Its Expression during Ripening in Apple Fruit

Cited by 22 publications

References 11 publications

Molecular cloning and expression of a cDNA encoding 1‐aminocyclopropane‐1‐carboxylate (ACC) oxidase from apricot fruit (Prunus armeniaca)

Molecular cloning and expression of a cDNA encoding 1‐aminocyclopropane‐1‐carboxylate (ACC) oxidase from apricot fruit (Prunus armeniaca)

Ethylene involvement in the over-expression of Fe(III)-chelate reductase by roots of E107 pea [Pisum sativum L. (brz, brz)] and chloronerva tomato (Lycopersicon esculentum L.) mutant genotypes

Iron requirement for and effects of promoters and inhibitors of ethylene action on stimulation of Fe(III)-chelate reductase in roots of strategy I species

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