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Plant Physiology 99:1642-1649 (1992) © 1992 American Society of Plant Biologists
Subcellular Location of
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  M. Hansen, M. Lange, C. Friis, G. Dionisio, P. B. Holm, and E. Vincze Antisense-mediated suppression of C-hordein biosynthesis in the barley grain results in correlated changes in the transcriptome, protein profile, and amino acid composition J. Exp. Bot., November 1, 2007; 58(14): 3987 - 3995. [Abstract] [Full Text] [PDF]
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 L. Thiery, A.-S. Leprince, D. Lefebvre, M. A. Ghars, E. Debarbieux, and A. Savoure Phospholipase D Is a Negative Regulator of Proline Biosynthesis in Arabidopsis thaliana J. Biol. Chem., April 9, 2004; 279(15): 14812 - 14818. [Abstract] [Full Text] [PDF]
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 Y. Terao, S. Nakamori, and H. Takagi Gene Dosage Effect of L-Proline Biosynthetic Enzymes on L-Proline Accumulation and Freeze Tolerance in Saccharomyces cerevisiae Appl. Envir. Microbiol., November 1, 2003; 69(11): 6527 - 6532. [Abstract] [Full Text] [PDF]
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T. Fujita, A. Maggio, M. Garcia-Rios, C. Stauffacher, R. A. Bressan, and L. N. Csonka Identification of Regions of the Tomato gamma -Glutamyl Kinase That Are Involved in Allosteric Regulation by Proline J. Biol. Chem., April 11, 2003; 278(16): 14203 - 14210. [Abstract] [Full Text] [PDF]
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Y. Morita, S. Nakamori, and H. Takagi L-Proline Accumulation and Freeze Tolerance in Saccharomyces cerevisiae Are Caused by a Mutation in the PRO1 Gene Encoding {gamma}-Glutamyl Kinase Appl. Envir. Microbiol., January 1, 2003; 69(1): 212 - 219. [Abstract] [Full Text] [PDF]
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 M. Murahama, T. Yoshida, F. Hayashi, T. Ichino, Y. Sanada, and K. Wada Purification and Characterization of {Delta}1-Pyrroline-5-Carboxylate Reductase Isoenzymes, Indicating Differential Distribution in Spinach (Spinacia oleracea L.) Leaves Plant Cell Physiol., July 1, 2001; 42(7): 742 - 750. [Abstract] [Full Text] [PDF]
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 N. H. Roosens, R. Willem, Y. Li, I. Verbruggen, M. Biesemans, and M. Jacobs Proline Metabolism in the Wild-Type and in a Salt-Tolerant Mutant of Nicotiana plumbaginifolia Studied by 13C-Nuclear Magnetic Resonance Imaging Plant Physiology, December 1, 1999; 121(4): 1281 - 1290. [Abstract] [Full Text]
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 N. Brugière, F. Dubois, A. M. Limami, M. Lelandais, Y. Roux, R. S. Sangwan, and B. Hirel Glutamine Synthetase in the Phloem Plays a Major Role in Controlling Proline Production PLANT CELL, October 1, 1999; 11(10): 1995 - 2012. [Abstract] [Full Text]
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P. E. Verslues and R. E. Sharp Proline Accumulation in Maize (Zea mays L.) Primary Roots at Low Water Potentials. II. Metabolic Source of Increased Proline Deposition in the Elongation Zone Plant Physiology, April 1, 1999; 119(4): 1349 - 1360. [Abstract] [Full Text]
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T. Fujita, A. Maggio, M. Garcia-Rios, R. A. Bressan, and L. N. Csonka Comparative Analysis of the Regulation of Expression and Structures of Two Evolutionarily Divergent Genes for Delta 1-Pyrroline-5-Carboxylate Synthetase from Tomato Plant Physiology, October 1, 1998; 118(2): 661 - 674. [Abstract] [Full Text]
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S. Iyer and A. Caplan Products of Proline Catabolism Can Induce Osmotically Regulated Genes in Rice Plant Physiology, January 1, 1998; 116(1): 203 - 211. [Abstract] [Full Text]
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C.-s. Zhang, Q. Lu, and D. P. S. Verma Removal of Feedback Inhibition of Delta^1-Pyrroline-5-carboxylate Synthetase, a Bifunctional Enzyme Catalyzing the First Two Steps of Proline Biosynthesis in Plants J. Biol. Chem., September 1, 1995; 270(35): 20491 - 20496. [Abstract] [Full Text] [PDF]
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| ASPB Publications | PLANT PHYSIOLOGY | THE PLANT CELL | |
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1-Pyrroline-5-Carboxylate Reductase in Root/Nodule and Leaf of Soybean 
1-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 (AJ Delauney, DPS Verma [1990] 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 NaCl). 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.