Microbodies (Glyoxysomes and Peroxisomes) in Cucumber Cotyledons

Trelease, Richard N.; Becker, Wayne M.; Gruber, Peter J.; Newcomb, Eldon H.

doi:10.1104/pp.48.4.461

Cited by 165 publications

(68 citation statements)

References 39 publications

(36 reference statements)

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“…Enzyme profiles for two cucumber strains essentially agreed with those documented by Trelease et al (14) for cucumber cotyledon development. Isocitrate lyase activity (a glyoxysomal marker) rose in the dark during the first few days after planting, reaching a maximum at day 3, after which it declined.…”

Section: Resultssupporting

confidence: 77%

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Microbody Malate Dehydrogenase Isozyme in Cotyledons of Cucumis sativus L. during Development

Wainwright¹,

Ting²

1976

Plant Physiol.

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The properties of the microbody malate debydrogenase (EC 1.1.1.37) (MDH) isozyme from cotyledons of Cucumus sativus L. were compared during development. It is conduded that the isozyme remains unaltered, despite the transition from glyoxysomal to peroxisomal function that occurs during greening of the cotyledons. This condusion is based on electrophoretic behavior, chromatographic elution from DEAE-cellulose, molecular weight, kinetic behavior, and immunological identity. In most cases, the distinct properties of the other MDH isozymes in the tissue during development provide additional support for an unchanging microbody isozyme. A method for assaying specifically the microbody isozyme was developed; a diluted preparation was assayed spectrophotometrically before and after complete immunological precipitation. The turnover of the microbody MDH isozyme was investigated by a radioactive labeling study. There is incorporation into both glyoxysomal and peroxisomal MDH. Degradation rates do not correspond with either decline of glyoxysomal activity or the continuation of peroxisomal activity. Apparently, the microbody MDH isozyme is continually turned over throughout cotyledon development.The transition, during the development of epigeal cotyledons, from a primary function of fat metabolism (nongreen cotyledons) to one of photosynthesis (green cotyledons) has been correlated with a parallel transition in microbody function. In particular, the development of microbodies in cucumber cotyledons has been well documented by electron microscopy (14).This work has substantiated earlier findings on sunflower cotyledons (4, 10) that the microbodies are first associated with the lipid bodies (for lipid catabolism), whereas later they are associated with chloroplasts and contain peroxisomal enzymes (functioning in photorespiration) (13). A previous study on catalase indicated that during the transition, the three-band isozyme pattern on electrophoresis is supplemented by an additional nine bands (3). By contrast, evidence is presented here that the microbody MDH isozyme is not altered during the transition in microbody function. The isozyme is organelle-specific rather than being adapted to the particular metabolic pathway in which it is involved. In addition, radioactive labeling experiments have given some insight into the turnover (synthesis and degradation) of the isozyme during glyoxysomal and peroxisomal function. This work is more fully detailed in a thesis dissertation (15). MATERIALS AND METHODSPlant Material and Preparation of the Homogenates. Seeds of a Burpee hybrid and the Straight Eight variety (6033-5) of cucumber (Cucumis sativus L.) were grown in vermiculite in a dark chamber (30 C) for the first 4 days and then transferred to a growth chamber with a 12-hr light/dark regime, with corresponding temperatures of 26.5 C and 15.5 C, respectively.The washed cotyledons were homogenized in 2 volumes of cold grinding medium (0.1 M tris or K phosphate at pH 7.5, containing 1 mM EDTA and 1 mm DTF) at 4 C, either ...

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Section: Resultssupporting

confidence: 77%

“…There is good evidence for the degradation of glyoxysomes and de novo synthesis of peroxisomes during the functional transition (7). On the other hand, others have provided equally good evidence that there is a single, ongoing population of microbodies (2,14).…”

Section: Discussionmentioning

confidence: 95%

Microbody Malate Dehydrogenase Isozyme in Cotyledons of Cucumis sativus L. during Development

Wainwright¹,

Ting²

1976

Plant Physiol.

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“…During photomorphogenesis, as seedlings undergo the transition from heterotrophic to autotrophic growth, organelles involved in photosynthesis and related functions (such as photorespiration) need to develop and genes required in these processes need to be activated. It was suggested that, during such a transitional stage, glyoxysomes are converted into leaf peroxisomes by replacement of glyoxysome-specific enzymes with those characteristic of leaf-type peroxisomes (Trelease et al, 1971;Olsen and Harada, 1995). In this study, we observed in Arabidopsis seedlings peroxisome elongation after 0.5-h light exposure, constriction and fission of these organelles at 2 h, and a sheer increase in peroxisome abundance at 4 and 8 h (Fig.…”

Section: Discussionmentioning

confidence: 53%

Light Induces Peroxisome Proliferation in Arabidopsis Seedlings through the Photoreceptor Phytochrome A, the Transcription Factor HY5 HOMOLOG, and the Peroxisomal Protein PEROXIN11b

Desai

2008

Plant Physiology

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Peroxisomes are single membrane-delimited subcellular organelles that carry out numerous vital metabolic reactions in nearly all eukaryotes. Peroxisomes alter their morphology, abundance, and enzymatic constituents in response to environmental cues, yet little is known about the underlying mechanisms. In this work, we investigated the regulatory role of light in peroxisome proliferation in Arabidopsis (Arabidopsis thaliana). We provide evidence that light induces proliferation of peroxisomes in Arabidopsis seedlings and that the peroxisomal protein PEX11b plays an important role in mediating this process. The far-red light receptor phytochrome A (phyA) and the bZIP transcription factor HY5 HOMOLOG (HYH) are both required for the up-regulation of PEX11b in the light. We further demonstrate that the phyA and hyh mutants exhibit reduced peroxisome abundance, a phenotype that can be rescued by overexpressing PEX11b in these plants. The HYH protein is able to bind to the promoter of PEX11b, suggesting that the PEX11b gene is a direct target of HYH. We conclude that HYH and PEX11b constitute a novel branch of the phyA-mediated light signaling cascade, which promotes peroxisome proliferation during seedling photomorphogenesis.

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“…The effect of transfer to light at various stages of growth in the dark on glycolate oxidase, hydroxypyruvate reductase, catalase, and isocitrate lyase have been described in this material (32). In cucumber cotyledons too, changes in enzymes of the glyoxylate cycle and those of leaf peroxisomes have been measured during greening under light-dark cycles and after transfer to light after 5 days in darkness (35). Furthermore, it is known from the work of Van Poucke and his associates (36,37) that the development of glycolate oxidase and glyoxylate reductase in cotyledons of Sinapis seedlings is under the control of the phytochrome system as it is in the young developing leaves of Phaseolus (11, 23) and also, apparently, of wheat (8).…”

mentioning

confidence: 99%

“…leaves have been examined (7-11, 23, 24, 33, 34), and some information is available for the special case of cotyledons of fatty seedlings (14,17,22,32,(35)(36)(37). Particular interest attaches to those enzymes characteristic of microbodies, since during fat utilization one class of microbody, the glyoxysome, is present, whereas during greening, leaf peroxisomes appear.…”

mentioning

confidence: 99%

Development of Enzymes in the Cotyledons of Watermelon Seedlings

Kagawa

McGREGOR²,

Beevers³

1973

Plant Physiol.

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Microbodies (Glyoxysomes and Peroxisomes) in Cucumber Cotyledons

Abstract: The changes in activities of glyoxysomal and peroxisomal enzymes have been correlated with the fine structure of micro.

Cited by 165 publications

References 39 publications

Microbody Malate Dehydrogenase Isozyme in Cotyledons of Cucumis sativus L. during Development

Microbody Malate Dehydrogenase Isozyme in Cotyledons of Cucumis sativus L. during Development

Light Induces Peroxisome Proliferation in Arabidopsis Seedlings through the Photoreceptor Phytochrome A, the Transcription Factor HY5 HOMOLOG, and the Peroxisomal Protein PEROXIN11b

Development of Enzymes in the Cotyledons of Watermelon Seedlings

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