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Drought stress has a considerable impact on the ecosystem and agriculture. Continuous water deficit induces early leaf senescence in plants. During this process, chloroplasts are degraded and photosynthesis drastically drops. The objective of this investigation was to look into the regulation of nitrogen and carbon metabolism during water deficit. Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) and the total protein contents inform us of the sink-source relation in plants. Glutamine synthetase (GS, EC 6.3.1.2) isoenzymes are good markers of plastid status (GS2) and the nitrogen metabolism (GS1). Tolerant and sensitive wheat (Triticum aestivum L.) genotypes were tested, which are widely used in agriculture. The amount of protein, Rubisco and GS isoforms in leaves were measured during the grain filling period, as indicative traits that ultimately determine the onset and stage of senescence. The symptoms of senescence first appeared on the oldest and finally on the youngest leaves. Drought stress disrupted the sequentiality of senescence in the sensitive varieties. An untimely senescence appeared in flag leaves, earlier than in the older leaves. Total protein and Rubisco contents decreased and the GS2 isoenzyme declined considerably in the youngest leaves. In the tolerant varieties, however, these physiological parameters did not change under drought, only the sequential senescence of leaf levels accelerated in some cases compared to the control, well-watered plants. Our results revealed that GS is a good indicator of drought stress, which can be applied for the characterization of wheat cultivars in terms of drought stress tolerance., (Copyright © 2013 Elsevier Masson SAS. All rights reserved.)

Nitric oxide (NO) is one of the key elements in the complex signalling pathway leading to stomatal closure by inducing reversible protein phosphorylation and Ca(2+) release from intracellular stores. As photosynthesis in guard cells also contributes to stomatal function, the aim of this study was to explore the potential role of NO as a photosynthetic regulator. This work provides the first description of the reversible inhibition of the effect of NO on guard cell photosynthetic electron transport. Pulse amplitude modulation (PAM) chlorophyll fluorescence measurements on individual stomata of peeled abaxial epidermal strips indicated that exogenously applied 450nM NO rapidly increases the relative fluorescence yield, followed by a slow and constant decline. It was found that NO instantly decreases photochemical fluorescence quenching coefficients (qP and qL), the operating quantum efficiency of photosystem II (ΦPSII), and non-photochemical quenching (NPQ) to close to zero with different kinetics. NO caused a decrease in NPQ, which is followed by a slow and continuous rise. The removal of NO from the medium surrounding the epidermal strips using a rapid liquid perfusion system showed that the effect of NO on qP and ΦPSII, and thus on the linear electron transport rate through PSII (ETR), is reversible, and the constant rise in NPQ disappears, resulting in a near steady-state value. The reversible inhibition by NO of the ETR could be restored by bicarbonate, a compound known to compete with NO for one of the two coordination sites of the non-haem iron (II) in the QAFe(2+)QB complex.

Sodium nitroprusside (SNP) is a widely used nitric oxide (NO) donor chemical, although it has been reported to release cyanide as well as NO during its photolysis. The aim of this work was to examine this potential side effect of SNP. Chlorophyll fluorescence experiments with pea leaves showed that SNP modifies photosynthetic electron transport. The SNP-induced changes were only partially restored in the presence of a NO-specific scavenger. Moreover, a stoichiometric KCN treatment mimicked the outcome caused by the joint application of the NO donor and NO scavenger. These results confirm the cyanide release of SNP and show that both of its photolytic products reduce the photochemical activity of photosystem II in vivo., (Copyright 2010 Elsevier GmbH. All rights reserved.)

The role of nitric oxide (NO) in photosynthesis is poorly understood as indicated by a number of studies in this field with often conflicting results. As various NO donors may be the primary source of discrepancies, the aim of this study was to apply a set of NO donors and its scavengers, and examine the effect of exogenous NO on photosynthetic electron transport in vivo as determined by chlorophyll fluorescence of pea (Pisum sativum) leaves. Sodium nitroprusside-induced changes were shown to be mediated partly by cyanide, and S-nitroso-N-acetylpenicillinamine provided low yields of NO. However, the effects of S-nitrosoglutathione are inferred exclusively by NO, which made it an ideal choice for this study. Q(A)(-) reoxidation kinetics show that NO slows down electron transfer between Q(A) and Q(B), and inhibits charge recombination reactions of Q(A)(-) with the S(2) state of the water-oxidizing complex in photosystem II. Consistent with these results, chlorophyll fluorescence induction suggests that NO also inhibits steady-state photochemical and nonphotochemical quenching processes. NO also appears to modulate reaction-center-associated nonphotochemical quenching.

Structural analysis of K+ channel pores suggests that the selectivity filter of the pore is an inherent sensor for extracellular K+ (Ko+); channels seem to be inactivated at low Ko+ because of a destabilization of the conducting state and a collapse of the pore. In the present study, the effect of depleting Ko+ on the activity of a plant K+ channel, KAT1, from Arabidopsis thaliana was investigated. This channel is thought to be insensitive to Ko+. The channel was therefore expressed in mammalian HEK293 cells and measured with patch clamp technology in the whole cell configuration. The effect of Ko+ depletion on channel activity was monitored from the tail currents before, during, and after washing Ko+ from the medium. The data show that a depletion of Ko+ results in a decrease in channel conductance, irrespective of whether K+ is simply removed or replaced by either Na+ or Li+. Quantitative analysis suggests that the channel has two binding sites for K+ with the dissociation constant in the order of 20 microM. This high sensitivity of the channel to Ko+ could serve as a safety mechanism, which inactivates the channel at low Ko+ and, in this way, prevents leakage of K+ from the cells via this type of channel.