Pyrroline-5-Carboxylate Reductase Is in Pea (<i>Pisum sativum</i> L.) Leaf Chloroplasts

Rayapati, P. J.; Stewart, Cecil R.; Hack, Ethan

doi:10.1104/pp.91.2.581

Cited by 68 publications

(45 citation statements)

References 23 publications

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“…Subcellular Location of P5CR in Soybean Root/Nodule and Leaf Tissues P5CR activity has been localized in chloroplasts in tobacco and pea (27,29). Analysis of the amino acid sequence of soybean P5CR deduced from the cDNA clone did not reveal any putative transit peptide, consistent with the location of this enzyme in the cytoplasm.…”

Section: Imentioning

confidence: 78%

“…This is consistent with studies on barley and tobacco (27). In pea, however, this enzyme is primarily located in chloroplasts of leaves (29). The presence of an immunoreactive peptide against the P5CR antibody in the chloroplastic fraction of soybean (Fig.…”

Section: Imentioning

confidence: 95%

“…P5CR activity has been detected in the chloroplast fraction of tobacco (27) and pea (29) leaves. In soybean, however, P5CR activity has been identified primarily in cytosol of root nodules (6,16).…”

mentioning

confidence: 99%

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Subcellular Location of Δ¹-Pyrroline-5-Carboxylate Reductase in Root/Nodule and Leaf of Soybean

Szöke

Miao²,

Hong³

et al. 1992

Plant Physiol.

131

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The expression of A'-pyrroline-5-carboxylate reductase (P5CR) gene was found to be higher in soybean root nodules than in leaves and roots, and its expression in roots appeared to be osmoregulated Mol Gen Genet 221: 299-305).P5CR was purified to homogeneity as a monomeric protein of 29 kilodaltons by overexpression of a soybean P5CR cDNA clone in Escherichia coli. The pH optimum of the purified P5CR was altered by increasing the salt concentration, and maximum enzyme activity was attainable at a lower pH under high salt (0.2-1 molar NaCI). Kinetic studies of the purified enzyme suggested that nicotinamide adenine dinucleotide phosphate' inhibited P5CR activity, whereas nicotinamide adenine dinucleotide+ did not. Subcellular fractionation and antibodies raised against purified soybean P5CR were used to investigate location of the enzyme in different parts of soybean as well as in leaves of transgenic tobacco plants synthesizing soybean P5CR. P5CR activity was present in cytoplasm of soybean roots and nodules as well as in leaves, but in leaves, about 15% of the activity was detected in the plastid fraction. The location of P5CR was further confirmed by western blot assay of the proteins from cytosol and plastid fractions of different parts of the plant. Expression of soybean nodule cytosolic P5CR in transgenic tobacco under the control of cauliflower mosaic virus 35S promoter led to the accumulation of this protein exclusively in the cytoplasm, suggesting that the chloroplastic activity may be due to the presence of a plastid form of the enzyme. The different locations of P5CR in root and leaf suggested that proline may be synthesized in different subcellular compartments in root and leaf. Proline concentration was not significantly increased in transgenic plants exhibiting high level P5CR activity, indicating that reduction of P5C is not a rate-limiting step in proline production.Proline accumulation is one of the adaptations of plants to salinity and water deficit (4,22,34). The proline biosynthetic pathway in plants and its regulation in response to osmotic stress is, however, not well understood. A precise determination of the proline pathway and its compartmentalization in different tissues is essential not only for understanding the regulation of proline production, but also for establishing the role of this amino acid in conferring tolerance to salt and drought stresses. The proline pathway in plants has been proposed to be analogous to that in bacteria (7, 21), although proline can also be made from omithine (1).

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Section: Imentioning

confidence: 78%

Section: Imentioning

confidence: 95%

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Subcellular Location of Δ¹-Pyrroline-5-Carboxylate Reductase in Root/Nodule and Leaf of Soybean

Szöke

Miao²,

Hong³

et al. 1992

Plant Physiol.

131

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“…Soybean nodule (18) and yeast (5) P5CRs have also been reported to be cytosolic proteins. However, chloroplast-localized P5CR activities have been reported for both greened and etiolated pea tissues (26).…”

Section: Effect Of Salt Stress On Levels Of P5cr Mrna and Protein Andmentioning

confidence: 99%

“…There are reports of kinetically distinguishable P5CR isozymes (18) and both cytosolic (18) and chloroplastic (26) forms of P5CR in plants.…”

mentioning

confidence: 99%

Molecular Cloning and Evidence for Osmoregulation of the Δ¹-Pyrroline-5-Carboxylate Reductase (proC) Gene in Pea (Pisum sativum L.)

Williamson¹,

Slocum²

1992

Plant Physiol.

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Enhanced drought tolerance with artificial microRNA‐mediated StProDH1 gene silencing in potato

Zhang

Zhu

et al. 2020

Crop Science

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Proline is a multifunctional molecule, which especially is associated with response to abiotic stress. The proline dehydrogenase (ProDH) is the rate-limiting enzyme in the process of proline catabolism. In the present study, two potato ProDH genes, StProDH1 and StProDH2, were cloned from potato (Solanum tuberosum L.) cultivar 'Favorita'. Gene expression analysis indicated that these two genes exhibited tissue-specific expression and responded differently to various stress conditions, and that the StProDH1 plays a predominant role in most of these conditions. An artificial microRNA expression vector, under the control of CaMV 35S promoter, was constructed to generate transgenic potato plants by Agrobacterium-mediated transformation, thereby silencing the StProDH1 gene. The result showed that the artificial microRNA caused a decline in StProDH1 expression, which was accompanied by a concomitant increase in proline content in transgenic plants under drought stress. The transgenic potato plants showed normal phenotypes under drought stress, while the non-transgenic plants appeared withered. Results of physiological parameters assays showed that malondialdehyde, relative water content, and chlorophyll content in the transgenic potato plants were higher than that of non-transgenic plants. Upon rehydration after two weeks of drought, proline and soluble sugar contents of the transgenic potato plants were significantly higher than those of non-transgenic plants. These results combined demonstrate that the StProDH1 is a key player in the process of potato response to drought stress.Abbreviations: amiRNA, artificial microRNA; MDA, malondialdehyde; MS, Murashige and Skoog; NT, non-transgenic; OAT, ornithine ð-aminotransferase; P5C, pyrroline-5-carboxylate; P5CDH, P5C dehydrogenase; P5CR, pyrroline-5-carboxylate reductase; P5CS, pyrroline-5-carboxylate synthetase; ProDH, proline dehydrogenase; RWC, relative water content.

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Pyrroline-5-Carboxylate Reductase Is in Pea (Pisum sativum L.) Leaf Chloroplasts

Cited by 68 publications

References 23 publications

Subcellular Location of Δ¹-Pyrroline-5-Carboxylate Reductase in Root/Nodule and Leaf of Soybean

Subcellular Location of Δ¹-Pyrroline-5-Carboxylate Reductase in Root/Nodule and Leaf of Soybean

Molecular Cloning and Evidence for Osmoregulation of the Δ¹-Pyrroline-5-Carboxylate Reductase (proC) Gene in Pea (Pisum sativum L.)

Enhanced drought tolerance with artificial microRNA‐mediated StProDH1 gene silencing in potato

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Pyrroline-5-Carboxylate Reductase Is in Pea (Pisum sativum L.) Leaf Chloroplasts

Cited by 68 publications

References 23 publications

Subcellular Location of Δ1-Pyrroline-5-Carboxylate Reductase in Root/Nodule and Leaf of Soybean

Subcellular Location of Δ1-Pyrroline-5-Carboxylate Reductase in Root/Nodule and Leaf of Soybean

Molecular Cloning and Evidence for Osmoregulation of the Δ1-Pyrroline-5-Carboxylate Reductase (proC) Gene in Pea (Pisum sativum L.)

Enhanced drought tolerance with artificial microRNA‐mediated StProDH1 gene silencing in potato

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Subcellular Location of Δ¹-Pyrroline-5-Carboxylate Reductase in Root/Nodule and Leaf of Soybean

Subcellular Location of Δ¹-Pyrroline-5-Carboxylate Reductase in Root/Nodule and Leaf of Soybean

Molecular Cloning and Evidence for Osmoregulation of the Δ¹-Pyrroline-5-Carboxylate Reductase (proC) Gene in Pea (Pisum sativum L.)