glycine max/proline

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RNA-Seq profiling of a defective seed coat mutation in Glycine max reveals differential expression of proline-rich and other cell wall protein transcripts.

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The plant cell wall performs a number of essential functions including providing shape to many different cell types and serving as a defense against potential pathogens. The net pattern mutation creates breaks in the seed coat of soybean (Glycine max) because of ruptured cell walls. Using RNA-Seq,

Differential Expression of Two Soybean (Glycine max L.) Proline-Rich Protein Genes after Wounding.

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We have investigated the wound-induced expression of two members of the soybean (Glycine max L.) proline-rich cell wall protein gene family and show that SbPRP1 and SbPRP2 exhibit unique patterns of expression after physical damage. SbPRP1 mRNA can be detected in the hook of soybean seedlings within

Arsenic-induced genotoxic responses and their amelioration by diphenylene iodonium, 24-epibrassinolide and proline in Glycine max L.

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Presence of the toxic metalloid, "arsenic (As)" is ubiquitous in the environment especially in the soil and water. Its excess availability in the soil retards growth and metabolism of plants via (a) slowing down the cell division/elongation, (b) overproduction of reactive oxygen species (ROS), (c)

Accumulation of extracellular proteins bearing unique proline-rich motifs in intercellular spaces of the legume nodule parenchyma.

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Nodulins encoding repetitive proline-rich cell wall proteins (PRPs) are induced during early interactions with rhizobia, suggesting a massive restructuring of the plant extracellular matrix during infection and nodulation. However, the proteins corresponding to these gene products have not been

Isolation and characterization of a proline-rich cell wall protein from soybean seedlings.

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We have purified a cell wall protein from extracts of soybean (Glycine max) that was previously shown to be immunologically related to p33, a wound-induced carrot cell wall protein (Tierney ML, Wiechert J, Pluymers D [1988] Mol Gen Genet 211: 393-399). Amino acid composition analysis reveals that

Proline metabolism in N2-fixing root nodules: energy transfer and regulation of purine synthesis.

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N2-fixing root nodules of soybean (Glycine max L. Merr.) convert atmospheric N2 to ammonia(um) in an energy-intensive enzymatic reaction. These nodules synthesize large quantities of purines because nitrogen fixed by bacteria contained within this tissue is transferred to the shoots in the form of

A G-Box-Binding Protein from Soybean Binds to the E1 Auxin-Response Element in the Soybean GH3 Promoter and Contains a Proline-Rich Repression Domain.

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The E1 promoter fragment (-249 to -203) is one of three auxin-response elements (AuxREs) in the soybean (Glycine max L.) GH3 promoter (Z.-B. Liu, T. Ulmasov, X. Shi, G. Hagen, T.J. Guilfoyle [1994] Plant Cell 6: 645-657). Results presented here further characterize and delimit the AuxRE within the

A defective seed coat pattern (Net) is correlated with the post-transcriptional abundance of soluble proline-rich cell wall proteins.

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The pigmented seed coats of several soybean (Glycine max (L.) Merr.) plant introductions and isolines have unusual defects that result in cracking of the mature seed coat exposing the endosperm and cotyledons. It has previously been shown that the T (tawny) locus that controls the color of trichomes

Oxidation of proline by plant mitochondria.

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Mitochondria isolated from etiolated shoots of corn (Zea mays), wheat (Triticum aestivum), barley (Hordeum vulgare), soybean (Glycine max L. Merr.), and mung bean (Phaseolus aureus) exhibited a proline-dependent O(2) uptake subject to respiratory control. ADP/O ratios with proline as substrate were

Proline fed to intact soybean plants influences acetylene reducing activity and content and metabolism of proline in bacteroids.

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Supplying l-proline to the root system of intact soybean (Glycine max [L.] Merr.) plants stimulated acetylene reducing activity to the same extent as did supplying succinate. Feeding l-proline also caused an increase in bacteroid proline dehydrogenase activity that was highly correlated with the

Effect of drought stress at supraoptimal temperature on polyamine concentrations in transgenic soybean with increased proline levels.

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The effect of drought stress at supraoptimal temperature on free proline and polyamine levels was compared in wild type and transgenic soybean (Glycine max cv. Ibis) plants having increased proline levels. Since glutamate and arginine are precursors of both proline and polyamines, it was assumed

Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (L-proline)-type II structure.

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Late embryogenesis abundant (LEA) proteins are members of a large group of hydrophilic, glycine-rich proteins found in plants, algae, fungi, and bacteria known collectively as hydrophilins that are preferentially expressed in response to dehydration or hyperosmotic stress. Group 2 LEA (dehydrins or

Characterization of a proline-rich cell wall protein gene family of soybean. A comparative analysis.

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Further characterization of a proline-rich cell wall protein gene family from soybean (Glycine max (L.) Merr) has been accomplished by the isolation and sequence analysis of two additional genes, SbPRP2 and SbPRP3, which encode mRNAs of 1050 and 650 nucleotides in length, respectively. Like the

The effect of sodium chloride on solute potential and proline accumulation in soybean leaves.

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Two cultivars of soybean (Glycine max [L.] Merr.) were grown in solution with up to 100 millimolar NaCl. Leaf solute potential was -1.1 to -1.2 megapascals in both cultivars without NaCl. At 100 millimolar NaCl leaf solute potential was -3.1 to -3.5 megapascals in Bragg and -1.7 megapascals in

Peptidyl proline hydroxylation and the growth of a soybean cell culture.

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Peptidyl proline hydroxylase inhibitors block the growth of cultured soybean (Glycine max) cells and bring about the disappearance of the major salt-extractable hydroxyproline-rich protein, the 33 kilodalton repetitive proline-rich protein (RPRP2). Three polypeptides of 28, 20, and 14 kilodalton

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