Systemic Calcium Wave Propagation in Physcomitrella patens.

The adaptation to dehydration and rehydration cycles represents a key step in the evolution of photosynthetic organisms and requires the development of mechanisms by which to sense external stimuli and translate them into signaling components. In this study, we used genetically encoded fluorescent sensors to detect specific transient increases in the Ca2+ concentration in the moss Physcomitrella patens upon dehydration and rehydration treatment. Observation of the entire plant in a single time-series acquisition revealed that various cell types exhibited different sensitivities to osmotic stress and that Ca2+ waves originated from the basal part of the gametophore and were directionally propagated towards the top of the plant. Under similar conditions, the vascular plant Arabidopsis thaliana exhibited Ca2+ waves that propagated at a higher speed than those of P. patens. Our results suggest that systemic Ca2+ propagation occurs in plants even in the absence of vascular tissue, even though the rates can be different.

The co-chaperone p23 controls root development through the modulation of auxin distribution in the Arabidopsis root meristem.

Homologues of the p23 co-chaperone of HSP90 are present in all eukaryotes, suggesting conserved functions for this protein throughout evolution. Although p23 has been extensively studied in animal systems, little is known about its function in plants. In the present study, the functional characterization of the two isoforms of p23 in Arabidopsis thaliana is reported, suggesting a key role of p23 in the regulation of root development. Arabidopsis p23 mutants, for either form, show a short root length phenotype with a reduced meristem length. In the root meristem a low auxin level associated with a smaller auxin gradient was observed. A decrease in the expression levels of PIN FORMED PROTEIN (PIN)1, PIN3, and PIN7, contextually to an inefficient polar localization of PIN1, was detected. Collectively these results suggest that both Arabidopsis p23 isoforms are required for root growth, in particular in the maintenance of the root meristem, where the proteins are located.

WHIRLY2 plays a key role in mitochondria morphology, dynamics, and functionality in Arabidopsis thaliana.

WHIRLY2 is a single-stranded DNA binding protein associated with mitochondrial nucleoids. In the why 2-1 mutant of Arabidopsis thaliana, a major proportion of leaf mitochondria has an aberrant structure characterized by disorganized nucleoids, reduced abundance of cristae, and a low matrix density despite the fact that the macroscopic phenotype during vegetative growth is not different from wild type. These features coincide with an impairment of the functionality and dynamics of mitochondria that have been characterized in detail in wild-type and why 2-1 mutant cell cultures. In contrast to the development of the vegetative parts, seed germination is compromised in the why 2-1 mutant. In line with that, the expression level of why 2 in seeds of wild-type plants is higher than that of why 3, whereas in adult plant no difference is found. Intriguingly, in early stages of shoots development of the why 2-1 mutant, although not in seeds, the expression level of why 3 is enhanced. These results suggest that WHIRLY3 is a potential candidate to compensate for the lack of WHIRLY2 in the why 2-1 mutant. Such compensation is possible only if the two proteins are localized in the same organelle. Indeed, in organello protein transport experiments using intact mitochondria and chloroplasts revealed that WHIRLY3 can be dually targeted into both, chloroplasts and mitochondria. Together, these data indicate that the alterations of mitochondria nucleoids are tightly linked to alterations of mitochondria morphology and functionality. This is even more evident in those phases of plant life when mitochondrial activity is particularly high, such as seed germination. Moreover, our results indicate that the differential expression of why 2 and why 3 predetermines the functional replacement of WHIRLY2 by WHIRLY3, which is restricted though to the vegetative parts of the plant.

Phosphorylation of p23-1 cochaperone by protein kinase CK2 affects root development in Arabidopsis.

Root growth is a fundamental process in plants and assures nutrient and water uptake required for efficient photosynthesis and metabolism. Postembryonic development of roots is controlled by the functionality of the meristem. Several hormones and signaling molecules regulate the size of the meristem, and among them, auxins play a major role. Protein kinase CK2, along with the chaperone protein HSP90, has been found to be involved in the regulation of auxin transport. Here, we show that p23-1, a cochaperone of HSP90, is phosphorylated by CK2 in Arabidopsis. We identified Ser201 as the major CK2 target site in p23-1 and demonstrated that phosphorylation of this site is necessary for normal root development. Moreover, we shed light on the nature of CK2 in Arabidopsis, showing that the three catalytic isoforms, CK2 αA, αB and αC, are proteins of approximately 40 kDa. Our results increase knowledge of the connection among HSP90, p23-1 and CK2 in Arabidopsis, suggesting the existence of a possible common root development mechanism controlled by these signaling molecules.