Effect of phytochrome on development of catalase activity and isoenzyme pattern in mustard (Sinapis alba L.) seedlings

Drumm, H.; Schöpfer, Peter

doi:10.1007/bf00388268

Cited by 47 publications

(35 citation statements)

References 31 publications

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“…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.…”

contrasting

confidence: 65%

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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contrasting

confidence: 65%

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

Wainwright¹,

Ting²

1976

Plant Physiol.

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“…Vol. 112, 1996 mustard (Drumm and Schopfer, 1974). Small families of catalase genes have been described for castor bean (Suzuki et al, 1994), N. plumbaginifolia (Willekens et al, 1994a(Willekens et al, , 1994b, and maize (Scandalios, 1987(Scandalios, , 1990.…”

mentioning

confidence: 99%

Catalase Is Encoded by a Multigene Family in Arabidopsis thaliana (L.) Heynh

et al. 1996

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The catalase multigene family in Arabidopsis includes three genes encoding individual subunits that associate to form at least six isozymes that are readily resolved by nondenaturing gel electrophoresis. CATl and CAT3map to chromosome 1 , and CAT2maps to chromosome 4. The nucleotide sequences of the three coding regions are 70 to 72% identical. The amino acid sequences of the three catalase subunits are 75 to 84% identical and 87 to 94% similar, considering conservative substitutions. Both the individual isozymes and the individual subunit mRNAs show distinct patterns of spatial (organ-specific) expression. Six isozymes are detected in flowers and leaves and two are seen in roots. Similarly, mRNA abundance of the three genes varies among organs. All three mRNAs are highly expressed in bolts, and CAT2 and CAT3 are highly expressed in leaves.

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“…In each case the authors addressed the problem of the number of microbody types involved in their systems, but could not draw definitive conclusions based on the data. Drumm and Schopfer (3) believe their comparison of the time course of catalase activity with time courses of glyoxysomal and peroxisomal enzymes in dark-grown and far red-irradiated watermelon cotyledons provides further circumstantial evidence favoring the microbody transformation hypothesis.…”

Section: Discussionmentioning

confidence: 99%

“…Their data are most consistent with the concept ot succession within existing particles (models 2 and 3). Definitive data are not available to determine whether peroxisomal enzymes are located in nonfunctional particles at the time of glyoxysomal metabolism (model 2) or in the same particles that house glyoxysomal enzymes (model 3).…”

Section: Discussionmentioning

confidence: 99%

Cytochemical Demonstration of Malate Synthase and Glycolate Oxidase in Microbodies of Cucumber Cotyledons

Burke

Trelease²

1975

Plant Physiol.

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The cytochemical localizations of malate synthase (glyoxysomal marker) Microbodies are a class of morphologically similar subcellular organelles commonly found in plant and animal tissues (11, 26). They are bounded by a single delimiting membrane and contain a coarsely granular or fibrillar matrix. On a metabolic basis, plant microbodies have been divided into peroxisomes and glyoxysomes. Peroxisomes house enzymes involved in the metabolism of glycolate, a product of photosynthesis (22), whereas glyoxysomes, common to endosperm or cotyledons of fatty seedlings, contain enzymes of the glyoxylate cycle (21, 26).Germinating fatty seedlings represent an excellent system for studying biogenesis and organization of microbodies. Activities of glyoxylate cycle enzymes increase steadily in microbodies (glyoxysomes) after the onset of germination, then decline rapidly I This work was supported by National Science Foundation Grant GB-43636 and Arizona State University Graduate Fellowship.as triglyceride reserves are depleted. Coincident with the lipid degradation, the cotyledons expand and become photosynthetically competent, and the microbodies gain enzyme activities characteristic of leaf peroxisomes (6,13,17,24,25). In these systems a change in metabolism occurs during postgerminative growth that directly involves enzymes contained within microbody particles. The evidence is not compelling whether cotyledonary glyoxysomes are degraded and replaced by a new population of microbodies that function as leaf peroxisomes or whether there is simply a change in enzymatic complement of the organelle, with the glyoxysomes persisting as functional peroxisomes.A direct approach for determining whether one or two microbody types are present at the time of the transition is to localize cytologically the appropriate marker enzymes. This is now possible with the use of two recently introduced electron cytochemical stains: malate synthase for glyoxysomes (23) and glycolate oxidase for peroxisomes (18). The cytochemical evidence given in this paper shows that both enzymes are housed within one type of microbody in cucumber cotyledons grown under conditions permitting high levels of both glyoxysomal and peroxisomal enzyme activities. MATERIALS AND METHODSCucumber seeds (Cucumis sativus L. cv. Improved Long Green) were surface-sterilized in 1 % hypochlorite (Clorox) for 10 min and planted in moistened vermiculite overlying soil. The seedlings were grown in the dark (constant 25 C) for 4 days following planting, subjected to 4 hr of continuous fluorescent and incandescent light (29 C), returned to the dark for 48

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Effect of phytochrome on development of catalase activity and isoenzyme pattern in mustard (Sinapis alba L.) seedlings

Cited by 47 publications

References 31 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

Catalase Is Encoded by a Multigene Family in Arabidopsis thaliana (L.) Heynh

Cytochemical Demonstration of Malate Synthase and Glycolate Oxidase in Microbodies of Cucumber Cotyledons

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