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Abstract. Long-term drought stress on photosystem II (PSII) was studied in pea (Pisum sativum L.) seedlings. Drought stress (reduction of water content by 35-80%) led to a considerable depletion of the PSII core, and the remaining PSII complex appeared to be functional and reorganized, with a unit size (LHCP/PSII core) twofold greater than that of well-irrigated plants. By immunoblotting analysis of the PSII proteins from grana and stroma lamellae, the enhanced degradation of CP43 and D1 proteins was observed in water-stressed plants. Also, water stress caused increased phosphorylation of the PSII core and increased D1 protein synthesis. Water-stress-mediated increase in D1 synthesis did not occur when plants were exposed to photoinhibitory light. The depletion of the PSII core was essentially reversed when water-stressed plants grown at low visible irradiance were watered. We suggest that the syndrome caused by the effect of long-term water stress on photosynthesis is a combination of at least two events: a reduction in the number of active PSII centres caused by a physical destabilization of the PSII core and a PSII reorganization with enhanced D1 turnover to counteract the core depletion. Key words: D1 protein (turnover, modification) - DroughtHigh irradiance -Photosystem II (core phosphorylation) -Pisum sativum (drought stress) -Stress syndrome

A biosensor for the detection of triazine- and phenylurea-type herbicides was constructed using isolated Photosystem II (PS II) complexes as a biosensing element. PSII isolated from the thermophilic cyanobacterium Synechococcus elongatus was immobilized on the surface of a screen-printed sensor composed of a graphite working electrode and Ag/AgCl reference electrode deposited on a polymeric substrate. The biosensor was mounted in a flow microcell with illumination. The principle of the detection was based on the fact that herbicides selectively block PSII electron transport activity in a concentration-dependent manner. Changes of the activity were registered amperometrically as the rate of photoreduction of an artificial electron acceptor. The setup resulted in a reusable herbicide biosensor with a good stability (half-life of 24 h) and limit of detection of approximately 10(-9) M for diuron, atrazine and simazine.

Mitochondrial processing peptidases are heterodimeric enzymes (α/βMPP) that play an essential role in mitochondrial biogenesis by recognizing and cleaving the targeting presequences of nuclear-encoded mitochondrial proteins. The two subunits are paralogues that probably evolved by duplication of a gene for a monomeric metallopeptidase from the endosymbiotic ancestor of mitochondria. Here, we characterize the MPP-like proteins from two important human parasites that contain highly reduced versions of mitochondria, the mitosomes of Giardia intestinalis and the hydrogenosomes of Trichomonas vaginalis. Our biochemical characterization of recombinant proteins showed that, contrary to a recent report, the Trichomonas processing peptidase functions efficiently as an α/β heterodimer. By contrast, and so far uniquely among eukaryotes, the Giardia processing peptidase functions as a monomer comprising a single βMPP-like catalytic subunit. The structure and surface charge distribution of the Giardia processing peptidase predicted from a 3-D protein model appear to have co-evolved with the properties of Giardia mitosomal targeting sequences, which, unlike classic mitochondrial targeting signals, are typically short and impoverished in positively charged residues. The majority of hydrogenosomal presequences resemble those of mitosomes, but longer, positively charged mitochondrial-type presequences were also identified, consistent with the retention of the Trichomonas αMPP-like subunit. Our computational and experimental/functional analyses reveal that the divergent processing peptidases of Giardia mitosomes and Trichomonas hydrogenosomes evolved from the same ancestral heterodimeric α/βMPP metallopeptidase as did the classic mitochondrial enzyme. The unique monomeric structure of the Giardia enzyme, and the co-evolving properties of the Giardia enzyme and substrate, provide a compelling example of the power of reductive evolution to shape parasite biology.