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1.
Physiol Plant ; 133(2): 288-97, 2008 Jun.
Article in English | MEDLINE | ID: mdl-18298412

ABSTRACT

To achieve a deeper knowledge on the function of HAL1 gene in tomato (Solanum lycopersicum) plants submitted to salt stress, in this study, we studied the growth and physiological responses to high salt stress of T3 transgenic plants (an azygous line without transgene and both homozygous and hemizygous lines for HAL1) proceeding from a primary transformant with a very high expression level of HAL1 gene. The homozygous plants for HAL1 gene did not increase their salt tolerance in spite of an earlier and higher reduction of the Na(+) accumulation in leaves, being moreover the Na(+) homeostasis maintained throughout the growth cycle. The greater ability of the homozygous line to regulate the Na(+) transport to the shoot to long term was even shown in low accumulation of Na(+) in fruits. By comparing the homozygous and hemizygous lines, a higher salt tolerance in the hemizygous line, with respect to the homozygous line, was observed on the basis of fruit yield. The Na(+) homeostasis and osmotic homeostasis were also different in homozygous and hemizygous lines. Indeed, the Na(+) accumulation rate in leaves was greater in hemizygous than in homozygous line after 35 days of 100 mM NaCl treatment and only at the end of growth cycle did the hemizygous line show leaf Na(+) levels similar to those found in the homozygous line. With respect to the osmotic homeostasis, the main difference between lines was the different contribution of inorganic and organic solutes to the leaf osmotic balance. Taken together, these results suggest that the greater Na(+) exclusion ability of the homozygous line overexpressing HAL1 induces a greater use of organic solutes for osmotic balance, which seems to have an energy cost and hence a growth penalty that reverts negatively on fruit yield.


Subject(s)
Adaptation, Physiological/drug effects , Homeostasis/drug effects , Plant Leaves/metabolism , Saccharomyces cerevisiae Proteins/metabolism , Sodium Chloride/pharmacology , Sodium/metabolism , Solanum lycopersicum/genetics , Carbohydrate Metabolism/drug effects , Fruit/drug effects , Fruit/metabolism , Homozygote , Intracellular Signaling Peptides and Proteins , Solanum lycopersicum/drug effects , Solanum lycopersicum/growth & development , Plant Leaves/drug effects , Plant Leaves/physiology , Plant Proteins/metabolism , Plant Roots/drug effects , Plant Roots/metabolism , Plants, Genetically Modified , Potassium/pharmacology , Sodium/pharmacology , Time Factors , Transgenes
2.
Plant J ; 40(4): 523-35, 2004 Nov.
Article in English | MEDLINE | ID: mdl-15500468

ABSTRACT

Disruption of the TRH1 potassium transporter impairs root hair development in Arabidopsis, and also affects root gravitropic behaviour. Rescue of these morphological defects by exogenous auxin indicates a link between TRH1 activity and auxin transport. In agreement with this hypothesis, the rate of auxin translocation from shoots to roots and efflux of [3H]IAA in isolated root segments were reduced in the trh1 mutant, but efflux of radiolabelled auxin was accelerated in yeast cells transformed with the TRH1 gene. In roots, Pro(TRH1):GUS expression was localized to the root cap cells which are known to be the sites of gravity perception and are central for the redistribution of auxin fluxes. Consistent with these findings, auxin-dependent DR5:GUS promoter-reporter construct was misexpressed in the trh1 mutant indicating that partial block of auxin transport through the root cap is associated with upstream accumulation of the phytohormone in protoxylem cells. When [K+] in the medium was reduced from 20 to 0.1 mm, wild type roots showed mild agravitropic phenotype and DR5:GUS misexpression in stelar cells. This pattern of response to low external [K+] was also affected by trh1 mutation. We conclude that the TRH1 carrier is an important part of auxin transport system in Arabidopsis roots.


Subject(s)
Arabidopsis Proteins/metabolism , Arabidopsis/metabolism , Cation Transport Proteins/metabolism , Indoleacetic Acids/metabolism , Plant Roots/metabolism , Potassium/metabolism , Arabidopsis/drug effects , Arabidopsis/genetics , Biological Transport, Active/genetics , Gene Expression Regulation, Plant , Genotype , Gravitropism/genetics , Indoleacetic Acids/pharmacology , Mutation , Organisms, Genetically Modified , Phenotype , Plant Roots/drug effects , Potassium/pharmacology , Saccharomyces cerevisiae/metabolism
3.
J Biol Chem ; 277(12): 10367-73, 2002 Mar 22.
Article in English | MEDLINE | ID: mdl-11741933

ABSTRACT

Some neurotransmitter-gated ion channels are very much more sensitive to general anesthetics than others, even when they are genetically and structurally related. The most striking example of this is the extreme sensitivity of heteromeric neuronal nicotinic acetylcholine receptors to inhalational general anesthetics compared with the marked insensitivity of the closely related homomeric neuronal nicotinic receptors. Here we investigate the role of the alpha subunit in determining the anesthetic sensitivity of these receptors by using alpha(3)/alpha(7) chimeric subunits that are able to form functional homomeric receptors. By comparing the sensitivities of a number of chimeras to the inhalational agent halothane we show that the short (13 amino acids) putative extracellular loop connecting the second and third transmembrane segments is a critical determinant of anesthetic sensitivity. In addition, using site-directed mutagenesis, we show that two particular amino acids in this loop play a dominant role. When mutations are made in this loop, there is a good correlation between increasing anesthetic sensitivity and decreasing acetylcholine sensitivity. We conclude that this extracellular loop probably does not participate directly in anesthetic binding, but rather determines receptor sensitivity indirectly by playing a critical role in transducing anesthetic binding into an effect on channel gating.


Subject(s)
Anesthetics, Inhalation/pharmacology , Neurons/metabolism , Receptors, Nicotinic/metabolism , Acetylcholine/pharmacology , Animals , Dose-Response Relationship, Drug , Female , Halothane/pharmacology , Mutagenesis, Site-Directed , Mutation , Neurons/drug effects , Oocytes/metabolism , Protein Binding , Protein Structure, Tertiary , Recombinant Fusion Proteins/metabolism , Time Factors , Xenopus , Xenopus laevis
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