Home About us Contact
|
Home About us Contact | ||
|
|
||
Arabidopsis Cells (arabidopsi + cell)
Selected AbstractsA protein phosphatase 2A from Fagus sylvatica is regulated by GA3 and okadaic acid in seeds and related to the transition from dormancy to germinationPHYSIOLOGIA PLANTARUM, Issue 1 2006Mary Paz González-García Several gibberellic acid (GA3)-induced cDNA fragments encoding putative serine/threonine protein phosphatase (PP) 2A catalytic subunits were obtained by means of differential reverse transcriptase-PCR approach. The full-length clone, named FsPP2A1, isolated from a beechnut cDNA library, exhibited all the features of and homology to members of the PP2A family. By transient expression of FsPP2A1 in tobacco and Arabidopsis cells as a green fluorescent fusion protein, we have obtained evidence supporting the subcellular localization of this protein in both the cytosol and the nucleus. Analysis of FsPP2A1 expression during seed stratification shows that these transcripts increase in the presence of GA3, a treatment proved to be efficient in breaking the dormancy of Fagus sylvatica seeds, but they are almost undetectable in dormant seeds or when dormancy is maintained after treatment with either abscisic acid or the gibberellin biosynthesis inhibitor paclobutrazol. The PP inhibitor okadaic acid (OKA) has a clear effect in decreasing both seed germination and FsPP2A1 expression. Furthermore, FsPP2A1 is specifically expressed in seed tissues, not being detected in other vegetative tissues examined. These results show the regulation of this PP by GA3 and OKA in these seeds. Its relationship with the processes taking place during the transition from dormancy to germination is also discussed. [source] pH and carbon supply control the expression of phosphoenolpyruvate carboxylase kinase genes in Arabidopsis thalianaPLANT CELL & ENVIRONMENT, Issue 12 2008ZHI-HUI CHEN ABSTRACT Phosphoenolpyruvate carboxylase (PEPC) is thought to play many roles in C3 plants including the provision of biosynthetic precursors and control of pH during N assimilation. Its activity is controlled via phosphorylation catalysed by PEPC kinases, which are encoded by PPCK genes. We examined PPCK expression in response to changes in the supply of N or C, and to changes in intracellular pH, using cultured Arabidopsis cells and seedlings. The results show that expression of both PPCK1 and PPCK2 is increased by C availability, but does not respond to N availability. Expression of the two PPCK genes and the phosphorylation state of PEPC are increased in response to increasing intracellular pH. Elevated pH also reduces the repression of PPCK gene expression by Pi. Expression of phosphoenolpyruvate carboxykinase (PEPCK), which catalyses the decarboxylation of oxaloacetate, is decreased in response to increasing intracellular pH. pH homeostasis may be mediated at least partly by reciprocal changes in the expression of PPCK genes and PEPCK. [source] NO signalling in cytokinin-induced programmed cell deathPLANT CELL & ENVIRONMENT, Issue 9 2005FRANCESCO CARIMI ABSTRACT Cell death can be induced by cytokinin 6-benzylaminopurine (BA) at high dosage in suspension-cultured Arabidopsis cells. Herein, we provide evidence that BA induces nitric oxide (NO) synthesis in a dose-dependent manner. A reduction in cell death can be observed when the cytokinin is supplemented with the NO scavenger 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (cPTIO) or the nitric oxide synthase (NOS) inhibitors: 2-aminoethyl-isothiourea (AET) and NG. -monomethyl- l -arginine ( l -NMMA), which suggests that NO is produced via a NOS and is a signalling component of this form of programmed cell death. In BA-treated cells, mitochondrial functionality is altered via inhibition of respiration. This inhibition can be prevented by addition of either cPTIO or AET implying that NO acts at the mitochondrial level. [source] Identification of a novel family of 70 kDa microtubule-associated proteins in Arabidopsis cellsTHE PLANT JOURNAL, Issue 4 2005Andrey V. Korolev Summary Most plant microtubule-associated proteins (MAPs) have homologues across the phylogenetic spectrum. To find potential plant-specific MAPs that will have evaded bioinformatic searches we devised a low stringency method for isolating proteins from an Arabidopsis cell suspension on endogenous taxol-microtubules. By tryptic peptide mass fingerprinting we identified 55 proteins that were enriched on taxol-microtubules. Amongst a range of known MAPs, such as kinesins, MAP65 isoforms and MOR1, we detected ,unknown' 70 kDa proteins that belong to a family of five closely related Arabidopsis proteins having no known homologues amongst non-plant organisms. To verify that AtMAP70-1 associates with microtubules in vivo, it was expressed as a GFP fusion. This confirmed that the protein decorates all four microtubule arrays in both transiently infected Arabidopsis and stably transformed tobacco BY-2 suspension cells. Microtubule-directed drugs perturbed the localization of AtMAP70-1 but cytochalasin D did not. AtMAP70-1 contains four predicted coiled-coil domains and truncation studies identified a central domain that targets the fusion protein to microtubules in vivo. This study therefore introduces a novel family of plant-specific proteins that interact with microtubules. [source] Transport of cytokinins mediated by purine transporters of the PUP family expressed in phloem, hydathodes, and pollen of ArabidopsisTHE PLANT JOURNAL, Issue 1 2003Lukas Bürkle Summary Nucleobases and derivatives like cytokinins and caffeine are translocated in the plant vascular system. Transport studies in cultured Arabidopsis cells indicate that adenine and cytokinin are transported by a common H+ -coupled high-affinity purine transport system. Transport properties are similar to that of Arabidopsis purine transporters AtPUP1 and 2. When expressed in yeast, AtPUP1 and 2 mediate energy-dependent high-affinity adenine uptake, whereas AtPUP3 activity was not detectable. Similar to the results from cell cultures, purine permeases (PUP) mediated uptake of adenine can be inhibited by cytokinins, indicating that cytokinins are transport substrates. Direct measurements demonstrate that AtPUP1 is capable of mediating uptake of radiolabeled trans -zeatin. Cytokinin uptake is strongly inhibited by adenine and isopentenyladenine but is poorly inhibited by 6-chloropurine. A number of physiological cytokinins including trans- and cis- zeatin are also efficient competitors for AtPUP2-mediated adenine uptake, suggesting that AtPUP2 is also able to mediate cytokinin transport. Furthermore, AtPUP1 mediates transport of caffeine and ribosylated purine derivatives in yeast. Promoter,reporter gene studies point towards AtPUP1 expression in the epithem of hydathodes and the stigma surface of siliques, suggesting a role in retrieval of cytokinins from xylem sap to prevent loss during guttation. The AtPUP2 promoter drives GUS reporter gene activity in the phloem of Arabidopsis leaves, indicating a role in long-distance transport of adenine and cytokinins. Promoter activity of AtPUP3 was only found in pollen. In summary, three closely related PUPs are differentially expressed in Arabidopsis and at least two PUPs have properties similar to the adenine and cytokinin transport system identified in Arabidopsis cell cultures. [source] | ||||||||||