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arabidopsis pedemontana/proliini

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ArtikkelitKliiniset tutkimuksetPatentit
Sivu 1 alkaen 639 tuloksia

Proline accumulation and salt-stress-induced gene expression in a salt-hypersensitive mutant of Arabidopsis.

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The sos1 mutant of Arabidopsis thaliana is more than 20 times more sensitive to NaCl stress than wild type Arabidopsis. Because proline (Pro) is generally thought to have an important role in plant salt tolerance, the sos1 mutant and the wild type were compared with respect to their capacity to

Cell wall-associated ROOT HAIR SPECIFIC 10, a proline-rich receptor-like kinase, is a negative modulator of Arabidopsis root hair growth.

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Plant cell growth is restricted by the cell wall, and cell wall dynamics act as signals for the cytoplasmic and nuclear events of cell growth. Among various receptor kinases, ROOT HAIR SPECIFIC 10 (RHS10) belongs to a poorly known receptor kinase subfamily with a proline-rich extracellular domain.

Overexpression of NtHAL3 genes confers increased levels of proline biosynthesis and the enhancement of salt tolerance in cultured tobacco cells.

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The Hal3 protein of Saccharomyces cerevisiae inhibits the activity of PPZ1 type-1 protein phosphatases and functions as a regulator of salt tolerance and cell cycle control. In plants, two HAL3 homologue genes in Arabidopsis thaliana, AtHAL3a and AtHAl3b, have been isolated and the function of

Combinatorial control of Arabidopsis proline dehydrogenase transcription by specific heterodimerisation of bZIP transcription factors.

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Proline metabolism has been implicated in plant responses to abiotic stresses. The Arabidopsis thaliana proline dehydrogenase (ProDH) is catalysing the first step in proline degradation. Transcriptional activation of ProDH by hypo-osmolarity is mediated by an ACTCAT cis element, a typical binding

GhHyPRP4, a cotton gene encoding putative hybrid proline-rich protein, is preferentially expressed in leaves and involved in plant response to cold stress.

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Plant hybrid proline-rich proteins (HyPRPs) usually consist of an N-terminal signal peptide, a central proline-rich domain, and a conserved eight-cysteine motif C-terminal domain. In this study, one gene (designated as GhHyPRP4) encoding putative HyPRP was isolated from cotton cDNA library. Northern
Plant roots respond to environmental stresses or the exogenous plant hormone abscisic acid (ABA) by undergoing marked physiological and morphological changes. We show here that PERK4, a gene that encodes a member of the Arabidopsis thaliana proline-rich extensin-like receptor kinase family, plays an

Environmental and developmental signals modulate proline homeostasis: evidence for a negative transcriptional regulator.

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In many plants, osmotic stress induces a rapid accumulation of proline through de novo synthesis from glutamate. This response is thought to play a pivotal role in osmotic stress tolerance [Kishor, P. B. K., Hong, Z., Miao, G.-H., Hu, C.-A. A. and Verma, D. P. S. (1995) Plant Physiol. 108,

proline content alterative 17 (pca17) is involved in glucose response through sulfate metabolism-mediated pathway.

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Sulfate metabolism and glucose (Glc) signaling are important processes required for plant growth, development, and environmental responses. However, whether sulfate metabolism is involved in Arabidopsis response to Glc stress remains largely unclear. Recently, we have found that proline content

Analogs of the CLV3 peptide: synthesis and structure-activity relationships focused on proline residues.

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CLAVATA3 (CLV3) is a plant peptide hormone in which the proline residues are post-translationally hydroxylated and glycosylated. CLV3 plays a key role in controlling the stem cell mass in the shoot meristem of Arabidopsis thaliana. In a previous report, we identified a dodecapeptide (MCLV3) from
A novel, highly hydrophobic, glycine- and proline-rich peptide was characterized in the ovary of the desert locust, Schistocerca gregaria. The peptide was detected as one of the major peaks in a chromatographic separation of an acidic methanolic extract of 50 mature ovaries. Electrospray mass

A mitochondrial prolyl aminopeptidase PAP2 releases N-terminal proline and regulates proline homeostasis during stress response

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Most mitochondrial proteins are synthesised in the cytosol and targeted into the organelle via N-terminal targeting peptides that are cleaved upon import. The free targeting peptide is subsequently processed in a stepwise manner, with single amino acids released as final products. Here, we have

Molecular characterization of the gene coding for GPRP, a class of proteins rich in glycine and proline interacting with membranes in Arabidopsis thaliana.

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The gene coding for a new class of proteins rich in glycine and proline (GPRP) was cloned in Arabidopsis thaliana. In the protein sequence, five amino acids - glycine, proline, alanine, tyrosine and histidine - account for 79.4% of the total composition. The protein has two different glycine-rich

Synthesis of the proline analogue [2,3-3H]azetidine-2-carboxylic acid. Uptake and incorporation in Arabidopsis thaliana and Escherichia coli.

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Azetidine-2-carboxylic acid, the 4-membered ring noranalogue of proline, is regularly used in the study of proline metabolism as well as the study of protein conformation. We prepared D,L-[2,3-3H]azetidine-2-carboxylic acid with an optimized 10% yield from commercially available

Quantification of water stress-induced osmotic adjustment and proline accumulation for Arabidopsis thaliana molecular genetic studies.

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For the genetic potential of model systems such as Arabidopsis thaliana to be most effectively used to understand drought resistance, reliable and rapid protocols are needed for laboratory study of phenotypes relevant to stress responses in the field. Osmotic adjustment, the amount of additional

Phospholipase D is a negative regulator of proline biosynthesis in Arabidopsis thaliana.

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Accumulation of proline has been observed in a large number of plant species in response to drought and salt stresses, suggesting a key role of this amino acid in plant stress adaptation. Upstream components of the proline biosynthesis signal transduction pathways are still poorly defined. We
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