Identification of a glycine transporter from pea leaf mitochondria

Walker, Griffin H.; Sarojini, G.; Oliver, David J.

doi:10.1016/0006-291x(82)90601-5

Cited by 42 publications

(14 citation statements)

References 8 publications

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“…Addition of formate to crude mitochondria reduced both '4CO2 release and NH3 production from [1-'4C]glycine (Table III). (27). In the present study, glycine accumulation over a range of concentrations up to 100 mm glycine was linear in the presence of the glycine decarboxylase inhibitor INH (Fig.…”

Section: Resultssupporting

confidence: 63%

Effects of Glycolate Pathway Intermediates on Glycine Decarboxylation and Serine Synthesis in Pea (Pisum sativum L.)

Shingles¹,

Woodrow²,

Grodzinski³

1984

Plant Physiol.

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ABSTRACIGlycine decarboxylation and serine synthesis were studied in pea (Pisum sativum L.) leaf discs, in metabolically active intact chloroplasts, and in mitochondria isolated both partially by differential centrifugation (i.e. 'crude') and by further purification on a Percoll gradient. Glycolate, glyoxylate, and formate reduced glycine decarboxylase activity ('4C02 and NH3 release) in the crude green-colored mitochondrial fractions, and in the leaf discs without markedly altering serine synthesis from 11-'4q glycine. Glycolate acted because it was converted to glyoxylate which behaves as a noncompetitive inhibitor (K, = 5.1 ± 0.5 millimolar) on the mitochondrial glycine decarboxylation reaction in both crude and Percollpurified mitochondria. In contrast, formate facilitates glycine to serine conversion by a route which does not involve glycine breakdown in the crude mitochondrial fraction and leaf discs. Formate does not alter the conversion of two molecules of glycine to one C02, one NH3, and one serine molecule in the Percoll-purified mitochondria. In chloroplasts which were unable to break glycine down to CO2 and NH3, serine was labeled equally from I'4Clformate and 1-'4Cjglycine. The maximum rate of serine synthesis observed in chloroplasts is similar to that in isolated metabolically active mitochondria. Formate does not appear to be able to substitute for the one-carbon unit produced during mitochondrial glycine breakdown but can facilitate serine synthesis from glycine in a chloroplast reaction which is probably a secondary one in vivo.

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Section: Resultssupporting

confidence: 63%

Effects of Glycolate Pathway Intermediates on Glycine Decarboxylation and Serine Synthesis in Pea (Pisum sativum L.)

Shingles¹,

Woodrow²,

Grodzinski³

1984

Plant Physiol.

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“…To elucidate the effects of S-nitrosylation/S-glutathionylation on GDC activity, we treated mitochondria with GSNO and monitored the GDC activity (Walker et al, 1982;Walker and Oliver, 1986). Following 14 CO 2 release from [1-14 C]Gly (i.e.…”

Section: Inhibition Of Gly Decarboxylase Activity By Gsnomentioning

confidence: 99%

Regulation of Plant Glycine Decarboxylase byS-Nitrosylation and Glutathionylation

et al. 2010

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Mitochondria play an essential role in nitric oxide (NO) signal transduction in plants. Using the biotin-switch method in conjunction with nano-liquid chromatography and mass spectrometry, we identified 11 candidate proteins that were S-nitrosylated and/or glutathionylated in mitochondria of Arabidopsis (Arabidopsis thaliana) leaves. These included glycine decarboxylase complex (GDC), a key enzyme of the photorespiratory C 2 cycle in C3 plants. GDC activity was inhibited by S-nitrosoglutathione due to S-nitrosylation/S-glutathionylation of several cysteine residues. Gas-exchange measurements demonstrated that the bacterial elicitor harpin, a strong inducer of reactive oxygen species and NO, inhibits GDC activity. Furthermore, an inhibitor of GDC, aminoacetonitrile, was able to mimic mitochondrial depolarization, hydrogen peroxide production, and cell death in response to stress or harpin treatment of cultured Arabidopsis cells. These findings indicate that the mitochondrial photorespiratory system is involved in the regulation of NO signal transduction in Arabidopsis.

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“…Plant leaf mitochondria, for example, rapidly exchange glycine and L-senne to support the photorespiratory conversion of glycine to seine (19,27 for the phosphate transporter has been obtained from Arabidopsis (our unpublished data). Several organic acid transporters have been solubilized from mitoplasts, partially purified, and incorporated into liposomes.…”

mentioning

confidence: 93%

“…Plant leaf mitochondria, for example, rapidly exchange glycine and L-senne to support the photorespiratory conversion of glycine to seine (19,27). Plant mitochondria also contain a unique oxaloacetate transporter that interacts with NAD+-dependent malate dehydrogenase in the cytosol and matrix to shuttle reducing equivalents across the inner mitochondrial membrane (20).…”

mentioning

confidence: 99%

Isolation and Characterization of the Tricarboxylate Transporter from Pea Mitochondria

McIntosh¹,

Oliver²

1992

Plant Physiol.

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The tricarboxylate transporter was solubilized from pea (Pisum sativum) mitochondria with Triton X-1 14, partially purified over a hydroxylapatite column, and reconstituted in phospholipid vesicles.The proteoliposomes exchanged external [14C] (7,9,17,30).Although mitochondrial transporters are found in both plants and animals, there are some differences in the types of transporters present. Plant leaf mitochondria, for example, rapidly exchange glycine and L-senne to support the photorespiratory conversion of glycine to seine (19,27 for the phosphate transporter has been obtained from Arabidopsis (our unpublished data). Several organic acid transporters have been solubilized from mitoplasts, partially purified, and incorporated into liposomes. The monocarboxylate, dicarboxylate (24), glutamate/aspartate (25), and aketoglutarate (10) transporters have been isolated from plant mitochondria and incorporated into proteoliposomes for detailed study. However, sequence information for the organic acid transporters is not yet available from either plants or animals.The tricarboxylate transporter from animal mitochondria has been studied in considerable detail (6,16,(21)(22)(23). This transporter from rat (4) and bovine (6) mitochondria has been isolated and purified 1000-and 400-fold, respectively. The preparation from rat liver showed a protein with an apparent molecular mass of 30 kD, whereas the preparation from bovine liver had a predominant 37-to 38-kD protein on SDS-PAGE gels. No conclusive proof is available that either band is the mammalian tricarboxylate transporter. Both transporters exchanged citrate, isocitrate, malate, malonate, and phosphoenolpyruvate. In this paper, we report the solubilization, partial purification, reconstitution, and analysis of the tricarboxylate transporter from pea (Pisum sativum L.) mitochondria. buffer B containing 6 mg of cardiolipin mL-1 was added and the sample was incubated for 30 min. Solubilized membranes were then centrifuged for 35 min at 37,000g and the supernatant was removed. This crude Triton X-1 14 extract was then chromatographed on cold dry hydroxylapatite (0.5 g per column, 0.5 mL of crude extract per column). Elution was done with buffer B and the first 1.0 mL off each column was collected and pooled. MATERIALS AND METHODS Preparation of ProteoliposomesDried azolectin was resuspended in buffer C (120 mm Hepes, 50 mm KCl, 1 mm EDTA, pH 7.5) under N2 gas at 120 mg/mL and bath sonicated (Laboratory Supplies Co.) at room temperature until the solution was translucent. Six microliters of a 1-M solution of the organic to be loaded into the proteoliposome (citrate, malate, etc.) was added to 540 ,uL of liposomes and then 460 ,L (6.5 ,ug of protein) of the hydroxylapatite eluate (or 200 ML of the crude Triton X-114 extract containing about 4 mg of protein and 260 ,uL of buffer B) was added. The sample was vortexed and frozen at -800C.Immediately prior to the assay, the proteoliposomes were thawed for 15 min in a room-temperature water bath, cooled on ice for 5 mi...

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Identification of a glycine transporter from pea leaf mitochondria

Cited by 42 publications

References 8 publications

Effects of Glycolate Pathway Intermediates on Glycine Decarboxylation and Serine Synthesis in Pea (Pisum sativum L.)

Effects of Glycolate Pathway Intermediates on Glycine Decarboxylation and Serine Synthesis in Pea (Pisum sativum L.)

Regulation of Plant Glycine Decarboxylase byS-Nitrosylation and Glutathionylation

Isolation and Characterization of the Tricarboxylate Transporter from Pea Mitochondria

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