Thermophilic unicellular cyanobacterium Synechococcus elongatus Näg. var. thermalis Geitl. strain Kovrov 1972/8 was cultivated in continuous flow reactor to simulate conditions occurring in nature in regions with low iron concentration. Two degrees of iron deprivation were established: (a) low iron (LI) conditions (9.0 µM Fe) when cells still maintained maximal growth rate but already exhibited changes in photosynthetic apparatus, and (b) iron deficient (ID) conditions (0.9 µM Fe) when cell growth rate decreased and extensive morphological and functional changes were observed. A decrease in the cellular content of phycobilin antenna was observed in both ID and LI cells and an increase of carotenoid concentration only in the ID culture. Morphologically, ID cells showed a decrease in the amount of phycobilins and in the number of thylakoid membranes. This suggests that S. elongatus responds to decrease in iron availability by substitution of the phycobilisomes by antennae containing chlorophyll (Chl) and carotenoids. Photochemical activity of photosystem (PS) 2, determined as Fv/Fm ratio was similar in high iron (HI) and LI cultures and approximately five times lower in ID culture. On the other hand, the activity of the whole electron transport chain showed the opposite tendency: the relative rates of the CO2-dependent oxygen evolution in HI : LI : ID cultures were approximately 1 : 2 : 4. Thus in nutrient stress the photosynthetic apparatus preserved its activity despite the decrease in the amount of both Chl-binding complexes and thylakoid membranes. and J. Benešová ... [et al.].
The PsbH protein of cyanobacterium Synechocystis sp. PCC 6803 was expressed as a fusion protein with glutathione-S transferase (GST) in E. coli grown on a mineral medium enriched in 15N isotope. After enzymatic cleavage of the fusion protein, the 1H-15N-HSQC spectrum of PsbH protein in presence of the detergent β-D-octyl-glucopyranoside (OG) was recorded on a Bruker DRX 500 MHz NMR spectrometer equipped with a 5 mm TXI cryoprobe to enhance the sensitivity and resolution. Non-labelled protein was used for secondary structure estimation by deconvolution from circular dichroism (CD) spectra. Experimental results were compared with our results from a structural model of PsbH using a restraint-based comparative modelling approach combined with molecular dynamics and energetic modelling. We found that PsbH shows 34-38% α-helical structure (Thr36-Ser60), a maximum of around 15% of β-sheet, and 12-19% of β-turn. and D. Štys ... [et al.].
The PsbH protein belongs to a group of small protein subunits of the photosystem 2 (PS2) complex and genes encoding PsbH homologues have been so far found in all studied oxygenic phototrophs. This single helix membrane protein is important for the proper function of the PS2 acceptor side and for stable assembly of PS2. Its hypothetical function as an analogue of the H subunit of the bacterial reaction centre as well as a putative role of its phosphorylation is evaluated. and J. Komenda, D. Štys, L. Lupínková.
Experiments were performed to distinguish some of the proposed mechanisms by which thylakoid membranes regulate the performance of photosynthetic apparatus in relation to non-photochemical quenching, qN. Aliphatic diamines were used as uncouplers of transmembrane H+ gradient as they can be transported across the membrane at the expense of hydrogen cations. Diamines did not induce changes in low-temperature fluorescence emission but induced different changes in membrane ultrastructure. Positively charged peptides did not affect membrane ultrastructure but blocked qN. In addition, they caused an increase of low temperature fluorescence emission between 710 and 720 nm. For control peptide, the maximal fluorescence increase was found at 715 nm. Fragments of light-harvesting complex 2 in their phosphorylated and non-phosphorylated form shifted the position of this increase. We believe that peptides bind to membrane surface and reduce the mobility of membrane components whose migration is needed for observation of qN. Phosphorylated and non-phosphophorylated LHC2 fragments bind to different binding sites for corresponding forms of the protein. and D. Štys ... [et al.].