High-irradiance (HI) stress induced changes in the photosynthetic energy storage (ES) of photosystems 1 (ESPS1) and 2 (ESPS2) were studied with 650 nm modulated radiation in intact sugar maple (Acer saccharum Marsh.) leaves. HI-treatment (420 W m-2, 1 h) caused an inhibition of about 40 % in ESPS2 and an enhancement of about 60 % in ESPS1. The rate of PS1 cyclic electron transport, measured with 705 nm modulated radiation, also increased in HI-treated leaves. There was a clear state 1- state 2 transition in HI-treated leaves. ESPS1 increased significantly and ESPS2 decreased drastically in leaves preadapted to state 1 after HI (600 W m-2, 30 min) treatment. Thus, the increase in PS1 activity observed immediately after HI-treatment in leaves preadapted to state 1 can be due to the coupling of LHC2 to PS1 during the HI-treatment. Further, the dissociation of LHC2 from PS2 during the HI-treatment resulted in apparently (about 15 %) greater inhibition than the "true" inhibition of PS2 activity. The presence of LHC2 with PS2 (state 1) at the time of HI-treatment caused no additional damage to PS2 or its coupling to PS1 offered no apparent HI-treatment. Further, the dissociation of LHC2 from PS2 during the HI-treatment resulted in apparently (about 15 %) greater inhibition than the "true" inhibition of PS2 activity. The presence of LHC2 with PS2 (state 1) at the time of HI-treatment caused no additional damage to PS2 or its coupling to PS1 offered no apparent protection to the photosynthetic apparatus. and K. Veeranjaneyulu, M. Charland, R. M. Leblanc.
NYB is chlorophyll-less barley mutant, which is controlled by a recessive nuclear gene. The mutation mechanism is revealed. The activities of enzymes transforming 5-aminolevulinic acid into protochlorophyllide were the same in both NYB and the wild type (WT), but the activity of the protochlorophyllide oxidoreductase (POR) in WT was much higher than that of NYB. Most of the photosystem 2 apoproteins were present in both WT and NYB, suggesting that the capability of protein synthesis was probably fully preserved in the mutant. Thus chlorophyll (Chl) biosynthesis in NYB was hampered at conversion form protochlorophyllide (Pchlide) into chlorophyllide. The open reading frame of porB gene in NYB was inserted with a 95 bp fragment, which included a stop codon. The NYB mutant is a very useful material for studies of Chl biosynthesis, chloroplast signalling, and structure of light-harvesting POR-Pchlide complex (LHPP). and Z.-L. Liu ... [et al.].
Chloroplast thylakoid contains several membrane-bound protein kinases that phosphorylate thylakoid polypeptides for the regulation of photosynthesis. Thylakoid protein phosphorylation is activated when the plastoquinone pool is reduced either by light-dependent electron flow through photosystem 2 (PS2) or by adding exogenous reductants such as durohydroquinone in the dark. The major phosphorylated proteins on thylakoid are components of light-harvesting complex 2 (LHC2) and a PS2 associated 9 kDa phosphoprotein. Radiation inactivation technique was employed to determine the functional masses of various kinases for protein phosphorylation in thylakoids. Under the photosynthetically active radiation (PAR), the apparent functional masses of thylakoid protein kinase systems (TPKXs) for catalyzing phosphorylation of LHC2 27 and 25 kDa polypeptides were 540±50 and 454±35 kDa as well as it was 448±23 kDa for PS2 9 kDa protein phosphorylation. Furthermore, the functional sizes of dark-regulated TPKXs for 25 and 9 kDa proteins were 318±25 and 160±8 kDa. The 9 kDa protein phosphorylation was independent of LHC2 polypeptides phosphorylation with regard to its TPKX functional mass. Target size analysis of protein phosphorylation mentioned above indicates that thylakoid contains a group of distinct protein kinase systems. A working model is accordingly proposed to interpret the interaction between these protein kinase systems. and S. C. Lee ... [et al.].
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.