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2. Induction of cyclic electron flow around photosystem 1 and state transition are correlated with salt tolerance in soybean
- Creator:
- Lu, K. X., Yang, Y., He, Y., and Jiang, D. A.
- Format:
- bez média and svazek
- Type:
- model:article and TEXT
- Subject:
- chlorophyll fluorescence induction, DBMIB, DCMU, electron flow inhibitors, light-harvesting complex, maximum photochemical efficiency, NaCl, phosphorylation, species differences, and Western blot
- Language:
- Multiple languages
- Description:
- We investigated the role of cyclic electron flow around photosystem 1 (CEF1) and state transition (ST) in two soybean cultivars that differed in salt tolerance. The CEF1 and maximum photochemical efficiency (Fv/Fm) were determined under control and NaCl (50 mM) stress and the NaCl-induced light-harvesting complex 2 (LHC2) phosphorylation in vitro was analysed in light and dark. NaCl induced the increase of CEF1 more greatly in wild soybean Glycine cyrtoloba (cv. ACC547) than in cultivated soybean Glycine max (cv. Melrose). The Fv/Fm was reduced less in G. cyrtoloba than in G. max after 10-d NaCl stress. In G. cyrtoloba, the increase of CEF1 was associated with enhancement of LHC2 phosphorylation in thylakoid membrane under both dark and light. However, in G. max the NaCl treatment decreased the LHC2 phosphorylation. Treatment with photosynthetic electron flow inhibitors (DCMU, DBMIB) inhibited LHC2 phosphorylation more in G. max than in G. cyrtoloba. Thus the NaCl-induced up-regulation in CEF1 and ST might contribute to salt resistance of G. cyrtoloba. and K. X. Lu ... [et al.].
- Rights:
- http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public
3. Modulation in vivo by nitrate salts of the activity and properties of phosphoenolpyruvate carboxylase in leaves of Alternanthera pungens (C4 plant) and A. sessilis (C3 species)
- Creator:
- Rajagopalan, A. V., Agarwal, R. M., and Raghavendra, A. S.
- Format:
- bez média and svazek
- Type:
- model:article and TEXT
- Subject:
- cycloheximide, glucose-6-phosphate, inorganic salts, L-malate, nitrate, phosphorylation, regulation, and sulphate
- Language:
- Multiple languages
- Description:
- Feeding K+ or Na+ nitrate salts in vivo enhanced the activity of phosphoenolpyruvate carboxylase (PEPC) in the leaf extracts of Alternanthera pungens (C4 plant) and A. sessilis (C3 species). The increase was more pronounced in A. pungens than in A. sessilis. Chloride salts increased the PEPC activity only marginally. However, the sulfate salts were either not effective or inhibitory. Feeding nitrate modulated the regulatory properties of PEPC in A. pungens, resulting in increased KI (malate) and decreased KA (glucose-6-P). The sensitivity of PEPC to malate, which gives a measure of phosphorylation status of the enzyme, indicated that feeding leaves with NO3- enhanced the phosphorylation status of the enzyme. The reduction in PEPC activity due to cycloheximide treatment suggested that increased synthesis of PEPC protein kinase may be one of the reasons for the enhancement in PEPC activity, after the nitrate feeding. We suggest that nitrate salts could be used as a tool to modulate and analyze the properties of PEPC in C3 and C4 plants. and A. V. Rajagopalan, R. M. Agarwal, A. S. Raghavendra.
- Rights:
- http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public
4. The PsbH protein of photosystem 2
- Creator:
- Komenda, J., Štys, D., and Lupínková, L.
- Format:
- bez média and svazek
- Type:
- model:article and TEXT
- Subject:
- chloroplast, cyanobacterium, D1 protein, phosphorylation, and photosynthesis
- Language:
- Multiple languages
- Description:
- 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.
- Rights:
- http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public
5. The relation between changes in non-photochemical quenching, low temperature fluorescence emission, and membrane ultrastructure upon binding of polyionic compounds and fragments of light-harvesting complex 2
- Creator:
- Štys, D., Šiffel, P., Hunalová, I., and Nebesářová, J.
- Format:
- bez média and svazek
- Type:
- model:article and TEXT
- Subject:
- decyldiamine, ethylenediamine, peptides, membrane fragments, phosphorylation, and Pisum sativum
- Language:
- Multiple languages
- Description:
- 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.].
- Rights:
- http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public
6. Thylakoid membrane protein kinase activity as a signal transduction pathway in chloroplasts
- Creator:
- Misra, A. N. and Biswal, A. K.
- Format:
- bez média and svazek
- Type:
- model:article and TEXT
- Subject:
- D1 protein, evolution, gene expression, light-harvesting complex 2, phosphorylation, and photosystems
- Language:
- Multiple languages
- Description:
- In plants external stimuli are perceived through a cascade of signals and signal transduction pathways. Protein phosphorylation and de-phosphorylation is one of the most important transduction paths for the perception of signals in plants. The highest concentrations of plant phospho-proteins are located in chloroplasts. This facilitates the protection of thylakoid membranes from stress-induced damage and augments adaptive strategies in plants. In this review, the protein kinases associated with phosphorylation of thylakoid membrane protein, and the adaptive changes in thylakoid membrane architecture and developmental cues are given. The presence of membrane bound kinases in thylakoid membranes have evolutionary implications for the signal transduction pathways and the photosynthetic gene expression for thylakoid membrane protein dynamics. and A. N. Misra, A. K. Biswal.
- Rights:
- http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public