Membrane association and some characteristics of the ethylene forming enzyme from etiolated pea seedlings

Mattoo, Autar K.; Achilea, O.; Fuchs, Yoram; Chalutz, E.

doi:10.1016/s0006-291x(82)80041-7

Cited by 26 publications

(11 citation statements)

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“…Since the ethylene-forming enzyme seems to be membrane associated (20,29) and ethylene is known to cause changes in membrane permeability (1), it is possible that increased conversion of ACC to ethylene in ethylene-treated tissue may be mediated through a change in the membrane milieu of this enzyme.…”

Section: Discussionmentioning

confidence: 99%

Enhancement by Ethylene of Cellulysin-Induced Ethylene Production by Tobacco Leaf Discs

Chalutz¹,

Mattoo²,

Solomos³

et al. 1984

Plant Physiol.

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Cellulysin-induced ethylene production in tobacco (Nicotiana tabacum L.) leaf discs was enhanced several-fold by prior exposure of the leaf tissue to ethylene. This enhancement in the response of the tissue to Cellulysin increased rapidly during 4 and 8 hours of pretreatment with ethylene and resulted from greater conversion of methionine to ethylene. On treatment with Cellulysin, the content of 1-aminocyclopropane-lcarboxylic acid (ACC) in leaf discs not pretreated with ethylene markedly increased while that of the ethylene-pretreated tissue was only slightly higher than in the tissue incubated in the absence of Cellulysin. Ethylenetreated tissue, however, converted ACC to ethylene at a faster rate than air controls. These data indicate that ethylene stimulates Cellulysininduced ethylene production by stimulating the conversion of ACC to ethylene. Data are also presented on a possible relation of this phenomenon to ethylene produced by the tobacco leaf upon interaction with its pathogen, Alternaria alternata.Ethylene is produced by higher plants as well as microorganisms and its role as a plant hormone is well established (1,15,16). In most diseased plants, ethylene production is stimulated and the involvement of ethylene in pathogenesis has been suggested (6,21,25). Ethylene may be involved in disease resistance by induction of enzymes or by formation of antifungal compounds (8,10,11,21,28), while it may also promote sensitivity of higher plants to external stimuli by accelerating senescence (1). Little is known about the mechanism of production and roles of ethylene during the interaction of host and parasite. There is also no clear knowledge of the contribution of host or pathogen to ethylene produced during disease or of the site of ethylene production (21). However, an early event in the interaction between the host and its pathogen is the secretion, by the pathogen, of cell-wall degrading enzymes (5) Tobacco leaves were pretreated in air or ethylene in 3.8-L desiccators. Each leaf was divided in half by cutting along its mid-rib and each half was placed on filter paper, moistened with water, in individual desiccators. A vial containing filter paper soaked with 2 ml of 0.25 M mercuric perchlorate was placed in the 'air control' desiccator to absorb traces of ethylene. Similarly, in some experiments, whole, potted tobacco plants were pretreated with ethylene. Four plants were placed inside a 2-ply (3 mil), 45-L polyethylene bag for 16 h with the desired ethylene concentration. Unless otherwise indicated, three leaf discs (1 cm in diameter, weighing 50 mg) were incubated in 25-ml Erlenmeyer flasks with 0.5 ml of the basal medium containing 700 mM sorbitol, 10 mm Mes (pH 6.0), 10 mm CaC12, 50 gg/ml streptomycin sulfate, and 50 units/ml penicillin G in the absence or presence of Cellulysin (Calbiochem) (4). Cellulysin was desalted before use by ultrafiltration with an Amicon PM-10 membrane (3). Ethylene was allowed to accumulate for I h and quantified by GC (17). Between each sampling, flasks were flu...

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Section: Discussionmentioning

confidence: 99%

Enhancement by Ethylene of Cellulysin-Induced Ethylene Production by Tobacco Leaf Discs

Chalutz¹,

Mattoo²,

Solomos³

et al. 1984

Plant Physiol.

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“…(i) Although ethylene is produced freely from both green leaves and green fruits, the enzyme itself has up to now been able to be prepared only from etiolated seedling, fruit, or flower tissues (4)(5)(6)(7)(8). In green leaves the enzymatic activity is lost on grinding (8).…”

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confidence: 99%

“…(ii) The many interactions of the ACC-oxidizing system with light (9-12), cytokinins (13), carbon dioxide (10)(11)(12)14), EDTA (7), catalase (7), and reagents for free radicals and sulfhydryl groups (7,15,16) In view of these complications, it seemed wiser, before making further attempts at purification, to explore known enzyme systems considered likely to carry out the reaction. For such an exploration some guidance that limits the field is needed.…”

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confidence: 99%

“…For such an exploration some guidance that limits the field is needed. An important lead was furnished by the growing number of indications that the formation of ethylene is in some way connected with cell membranes (7,(15)(16)(17)(18); indeed Legge et al concluded flatly that "a step in ethylene biosynthesis may be membrane-associated" (18). The requirement for oxygen (and not mere proton transfer) in the conversion of ACC to ethylene indicates the participation of an oxidase or free radicals, or both.…”

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confidence: 99%

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Lipid peroxidation forms ethylene from 1-aminocyclopropane-1-carboxylic acid and may operate in leaf senescence

Bousquet

Thimann

1984

Proc. Natl. Acad. Sci. U.S.A.

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An enzyme system is described which oxidizes 1-aminocyclopropane-l-carboxylic acid (ACC) to ethylene under physiological conditions. It comprises linoleic acid, pyridoxal phosphate, manganese, and lipoxygenase (linoleate:oxygen oxidoreductase, EC 1.13.11.12). It requires oxygen and is specific for manganese; it can operate but only with greatly reduced yield in the absence of pyridoxal phosphate.An enzyme with the same properties was prepared from microsomal membranes of the seedling shoots of peas. Both have similar reactions to a variety of inhibitors and other reagents. The properties also resemble those of at least two of the in vivo systems recorded ih the literature. Intact green oat leaves also contain a similar system. Because there is a growing body of evidence that ethylene formation is associated with cell membranes and because the yields of ethylene from the complete system are much higher than those recorded for' other enzymes, it may be identical with the in vivo system acting in senescent leaves.

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“…The results presented in table 1 show that EFE [3,12]. Moreover, soiubilisation of the membranes with a non-ionic detergent preserves the activity at the same level (table 1).…”

Section: Flowers Of Carnationmentioning

confidence: 92%

On the role of membrane integrity in the conversion of 1‐aminocyclopropane 1‐carboxylic acid to ethylene in carnation petals

Borochov

Adam

1984

FEBS Letters

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The reaction converting 1-aminocyclopropane l-carboxylic acid (ACC) to ethylene in plants is independent of cell or membrane integrity. Both intact and detergent-solubilised membrane fractions can readily convert ACC to ethylene. The reaction catalysed by the solubilised enzyme is inhibited by 1OOpM 2,Cdinitrophenol.ATP, even at very low concentrations, totally inhibits the reaction. The results would appear to invalidate a previously hypothesised model for this reaction.

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Membrane association and some characteristics of the ethylene forming enzyme from etiolated pea seedlings

Cited by 26 publications

References 20 publications

Enhancement by Ethylene of Cellulysin-Induced Ethylene Production by Tobacco Leaf Discs

Enhancement by Ethylene of Cellulysin-Induced Ethylene Production by Tobacco Leaf Discs

Lipid peroxidation forms ethylene from 1-aminocyclopropane-1-carboxylic acid and may operate in leaf senescence

On the role of membrane integrity in the conversion of 1‐aminocyclopropane 1‐carboxylic acid to ethylene in carnation petals

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