Light-induced development of glycine oxidation by mitochondria from sunflower cotyledons

Arron, Geoffrey P.; Edwards, Gerald E.

doi:10.1016/0304-4211(80)90113-3

Cited by 29 publications

(13 citation statements)

References 21 publications

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“…However, it has been reported that light is a prerequisite for the biogenesis of the glycine decarboxylase (GDC) enzyme complex (Arron and Edwards 1980;Walker and Oliver 1986). To date this is the only evidence for a possible role of light in the regulation of the synthesis of a mitochondrial protein.…”

Section: Discussionmentioning

confidence: 97%

Mitochondrial gene expression during wheat leaf development

Topping

Leaver

1990

Planta

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The expression of specific mitochondrial, chloroplast and nuclear genes has been investigated in leaves of 7-d-old light-grown wheat (Triticum aestivum cv. Maris Dove). In the wheat leaf there is a spatial separation of a temporal sequence of development from the basal meristem to the distal mature, photosynthetically competent cells. This sequence of cellular differentiation is paralleled by a functional differentiation in which the energy supply changes from oxidative phosphorylation in the non-green meristematic cells to a combined dependence on oxidative and photophosphorylation in the photosynthesizing cells. The changes in copy number per cell and expression of mitochondrial genes have been investigated in successive sections of the wheat leaf using quantitative DNA-DNA and DNA-RNA filter and protein-binding techniques. The abundance of specific mitochondrial genes (cox II.cob andatp A) per cell was found to decrease between five- and tenfold within the basal (1 cm) section of the leaf and then remain constant to the distal tip. The relative abundances of specific mitochondrial transcripts (cox I,cox II,cob andatp A) were found to decrease in successive sections from the basal meristem to the distal tip (from a relative value of 100% to 5-40%). In contrast, transcripts of chloroplast genes and nuclear genes encoding chloroplast polypeptides (psb A,rbc L andrbc S) were found to increase steadily in progressive leaf sections (from a relative value of 0-2% to 100%). The steady-state level of the α-subunit of the mitochondrial F1 ATPase was found to remain constant along the length of the leaf. Possible sites at which the regulation of organellar gene expression is coordinated during the development of photosynthetic competence within the wheat leaf are discussed.

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Section: Discussionmentioning

confidence: 97%

Mitochondrial gene expression during wheat leaf development

Topping

Leaver

1990

Planta

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“…Vol. 107, 1995 light IArron andEdwards, 1980;Walker and Oliver, 19861). Similar changes have been demonstrated to occur in dicotyledons with photosynthetic activity increasing with leaf cell maturity (Tobin and Rogers, 1992).…”

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Developmental Regulation of Respiratory Activity in Pea Leaves

Lennon

Pratt²,

Leach³

et al. 1995

Plant Physiol.

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“…In etiolated leaves or nongreen tissues the amount of enzyme activity is low (1,3,6,22) and following illumination of etiolated leaves the amount ofenzyme activity increases about 10-fold (16,22). The increase in activity results from a de novo synthesis of new proteins and the increase in protein synthesis is largely regulated at the transcriptional level (9).…”

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confidence: 99%

Interaction between the Component Enzymes of the Glycine Decarboxylase Multienzyme Complex

Oliver

Neuburger²,

Bourguignon³

et al. 1990

Plant Physiol.

120

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The glycine decarboxylase multienzyme complex comprises about one-third of the soluble protein of the matrix of pea (Pisum sativum) leaf mitochondria where it exists at a concentration of approximately 130 milligrams protein/milliliter. Under these conditions the complex is stable with an approximate subunit ratio of 2 P-protein dimers:27 H-protein monomers:9 T-protein mono glycine cleavage system or glycine synthase) has been reported from the mitochondria of a broad range of plant and animal tissues (8) as well as the cytosol of a number of bacteria (10, 1 1), it is found at its highest level in the mitochondria of C3 plant leaves. Indeed, glycine formed by the photorespiratory C-2 pathway is the predominant substrate oxidized by these mitochondria in illuminated leaf tissue (17).The concentration of the complex in plant tissue is controlled by light. In etiolated leaves or nongreen tissues the amount of enzyme activity is low (1, 3, 6, 22) and following illumination of etiolated leaves the amount ofenzyme activity increases about 10-fold (16,22). The increase in activity results from a de novo synthesis of new proteins and the increase in protein synthesis is largely regulated at the transcriptional level (9). The time course for the increase in mRNA concentrations for the specific component proteins of the enzyme complex closely parallels the increase in enzyme activity in greening pea tissues (9,12,22).The glycine decarboxylase complex consists of four different component proteins (2, 21). The 100 kD P-protein binds the PLP that forms the initial Schiff base with the a-amino group of glycine. The a-carboxyl of glycine is lost as CO2 and the remaining methylamine moiety is passed to the lipoamide cofactor of the 13.9 kD H-protein. The lipoamide-bound methylamine group is shuttled to the 45 kD T-protein where the methylene carbon is transferred to THF to produce methylene THF and the amino nitrogen is released as NH3. The last step of the reaction involves the oxidation of the resulting dihydrolipoamide of the H-protein by the 59 kD L-protein with the sequential reduction of FAD and NAD+.Although substantial progress has been made in understanding the enzymology and molecular biology of the glycine decarboxylase complex from leaf tissue, little is known about the physical structure of the complex. We describe here a series of experiments designed to study this multienzyme complex and some of the unusual enzymological consequences of the unique interactions between the subunits. MATERIALS AND METHODSPea (Pisum sativum) leaf mitochondria were isolated from young plants by differential centrifugation and purified on Percoll-polyvinylpyrrolidone gradients (5

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Light-induced development of glycine oxidation by mitochondria from sunflower cotyledons

Cited by 29 publications

References 21 publications

Mitochondrial gene expression during wheat leaf development

Mitochondrial gene expression during wheat leaf development

Developmental Regulation of Respiratory Activity in Pea Leaves

Interaction between the Component Enzymes of the Glycine Decarboxylase Multienzyme Complex

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