Spatiotemporal heterogeneity of photosystem II function during acclimation to zinc exposure and mineral nutrition changes in the hyperaccumulator Noccaea caerulescens.

We investigated changes in mineral nutrient uptake and translocation and photosystem II (PSII) functionality, in the hyperaccumulator Noccaea caerulescens after exposure to 800 μM Zn in hydroponic culture. Exposure to Zn inhibited the uptake of K, Mn, Cu, Ca, and Mg, while the uptake of Fe and Zn enhanced. Yet, Ca and Mg aboveground tissue concentrations remain unchanged while Cu increased significantly.

Cadmium-zinc accumulation and photosystem II responses of Noccaea caerulescens to Cd and Zn exposure.

A population of the metallophyte Noccaea (Thlaspi) caerulescens originating from a Zn-enriched area at Røros Copper Mine (Norway) was studied. N. caerulescens tolerance to accumulate Cd and Zn was evaluated in hydroponic experiments by chlorophyll fluorescence imaging analysis.

Regulatory mechanisms after short- and long-term perturbed lysine biosynthesis in the aspartate pathway: the need for isogenes in Arabidopsis thaliana.

The aspartate-derived amino acid pathway in plants is an intensively studied metabolic pathway, because of the biosynthesis of the four essential amino acids lysine, threonine, isoleucine and methionine. The pathway is mainly controlled by the key regulatory enzymes aspartate kinase (AK; EC 2.7.

Transcriptional and biochemical regulation of a novel Arabidopsis thaliana bifunctional aspartate kinase-homoserine dehydrogenase gene isolated by functional complementation of a yeast hom6 mutant.

An aspartate kinase-homoserine dehydrogenase (AK-HSDH) cDNA of Arabidopsis thaliana has been cloned by functional complementation of a Saccharomyces cerevisiae strain mutated in its homoserine dehydrogenase (HSDH) gene (hom6). Two of the three isolated clones were also able to complement a mutant yeast aspartate kinase (AK) gene (hom3). Sequence analysis showed that the identified gene (akthr2), located on chromosome 4, is different from the previously cloned A.