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D1 Protein (d1 + protein)
Selected AbstractsThe function of D1-H332 in Photosystem II electron transport studied by thermoluminescence and chlorophyll fluorescence in site-directed mutants of Synechocystis 6803FEBS JOURNAL, Issue 17 2004Yagut Allahverdiyeva The His332 residue of the D1 protein has been identified as the likely ligand of the catalytic Mn ions in the water oxidizing complex (Ferreira, K.N., Iverson, T.M., Maghlaoui, K., Barber, J. & Iwata, S. (2004) Science 303, 1831,1838). However, its function has not been fully clarified. Here we used thermoluminescence and flash-induced chlorophyll fluorescence measurements to characterize the effect of the D1-H333E, D1-H332D and D1-H332S mutations on the electron transport of Photosystem II in intact cells of the cyanobacterium Synechocystis 6803. Although the mutants are not photoautotrophic they all show flash-induced thermoluminescence and chlorophyll fluorescence, which originate from the S2QA, and S2QB, recombinations demonstrating that charge stabilization takes place in the water oxidizing complex. However, the conversion of S2 to higher S states is inhibited and the energetic stability of the S2QA, charge pair is increased by 75, 50 and 7 mV in the D1-H332D, D1-H332E and D1-H332S mutants, respectively. This is most probably caused by a decrease of Em(S2/S1). Concomitantly, the rate of electron donation from Mn to Tyr-Z, during the S1 to S2 transition is slowed down, relative to the wild type, 350- and 60-fold in the D1-H332E and D1-H332D mutants, respectively, but remains essentially unaffected in D1-H332S. A further effect of the D1-H332E and D1-H332D mutations is the retardation of the QA to QB electron transfer step as an indirect consequence of the donor side modification. Our data show that although the His residue in the D1-332 position can be substituted by other metal binding residues for binding photo-oxidisable Mn it is required for controlling the functional redox energetics of the Mn cluster. [source] PTHrP Signaling Targets Cyclin D1 and Induces Osteoblastic Cell Growth Arrest,JOURNAL OF BONE AND MINERAL RESEARCH, Issue 6 2005Nabanita S Datta PhD Abstract PTHrP control of the MC3T3-E1 cell cycle machinery showed that, during differentiation, PTHrP induced G1 growth arrest. Cyclin D1 was a critical mediator as a downstream effector of cAMP, PKC, and MAPK signaling, and the process was PKA-independent. The involvement of JunB has been found critical for PTHrP effects. Introduction: PTH-related protein (PTHrP) has been implicated in the control of bone cell turnover, but the mechanisms underlying its effect on osteoblast proliferation and differentiation have not been clearly defined. The mechanisms by which PTHrP impacts cell cycle proteins and the role of signaling pathways in differentiated osteoblasts were studied. Materials and Methods: To elucidate the role of PTHrP, flow cytometric analyses were performed using MC3T3-E1 and primary mouse calvarial cells. Relative protein abundance (Western blot), physical association of partners (immunoprecipitation), and kinase activities (in vitro kinase assays using either GST-Rb or H1-histone as substrates) of cell cycle-associated proteins in vehicle and PTHrP-treated 7-day differentiated cells were determined. ELISA and/or Northern blot analyses were done to evaluate JunB and cyclin D1 expression. SiRNA-mediated gene silencing experiments were performed to silence JunB protein. Finally, inhibitors of cAMP, protein kinase A (PKA), protein kinase C (PKC), and mitogen-activated protein kinase (MAPK) were used to determine involvement of different signaling pathways. Results: PTHrP inhibited cyclin D1 protein expression 7-fold in a dose- and time-dependent manner and increased the level of p16 protein in differentiated osteoblasts. Additionally, PTHrP reduced cyclin D1-CDK4/CDK6 and CDK1 kinase activities. Forskolin, a cAMP agonist, mimicked PTHrP action, and the PKC inhibitor, GF109203X, slightly blocked downregulation of cyclin D1, implying involvement of both cAMP and PKC. U0126, a MAPK inhibitor, alone decreased cyclin D1 protein, suggesting that the basal cyclin D1 protein is MAPK dependent. H-89, a PKA inhibitor, did not alter the effect of PTHrP on cyclin D1, suggesting a PKA-independent mechanism. Finally, expression of JunB, an activating protein-1 transcription factor, was significantly upregulated, and silencing JunB (siRNA) partially reversed the cyclin D1 response, implying involvement of JunB in the PTHrP-mediated growth arrest of MC3T3-E1 cells. Conclusion: PTHrP upregulates JunB and reduces cyclin D1 expression while inducing G1 cell cycle arrest in differentiated osteoblasts. Such regulation could be an important determinant of the life span and bone-forming activity of osteoblasts. [source] psbA mutation (Asn266 to Thr) in Senecio vulgaris L. confers resistance to several PS II-inhibiting herbicidesPEST MANAGEMENT SCIENCE (FORMERLY: PESTICIDE SCIENCE), Issue 9 2006Kee Woong Park Abstract DNA sequence analysis of the psbA gene encoding the D1 protein of photosystem II (PS II), the target site of PS II-inhibiting herbicides, identified a point mutation (Asn266 to Thr) in a bromoxynil-resistant Senecio vulgaris L. population collected from peppermint fields in Oregon. Although this mutation has been previously reported in Synechocystis, this is the first report of this particular point mutation in a higher plant exhibiting resistance to PS II-inhibiting herbicides. The resistant population displayed high-level resistance to bromoxynil and terbacil (R/S ratio 10.1 and 9.3, respectively) and low-level resistance to metribuzin and hexazinone (R/S ratio 4.2 and 2.6, respectively) when compared with the susceptible population. However, the population was not resistant to the triazine herbicides atrazine and simazine or to the urea herbicide diuron. A chlorophyll fluorescence assay confirmed the resistance levels and patterns of cross-resistance of the whole-plant studies. The resistant S. vulgaris plants produced fewer seeds. Differences in cross-resistance patterns to PS II-inhibiting herbicides and the difference in fitness cost could be exploited in a weed management program. Copyright © 2006 Society of Chemical Industry [source] Rubisco expression in rice leaves is related to genotypic variation of photosynthesis under elevated growth CO2 and temperaturePLANT CELL & ENVIRONMENT, Issue 12 2003R. W. GESCH ABSTRACT Genetic modifications of agronomic crops will likely be necessary to cope with global climate change. This study tested the hypotheses that genotypic differences in rice (Oryza sativa L.) leaf photosynthesis at elevated [CO2] and temperature are related to protein and gene expression of Rubisco, and that high growth temperatures under elevated [CO2] negatively affect photosystem II (PSII) photochemical efficiency. Two rice cultivars representing an indica (cv. IR72) and japonica type (cv. M103) were grown in 350 (ambient) and 700 (elevated) µmol CO2 mol,1 at 28/18, 34/24 and 40/30 °C sinusoidal maximum/minimum, day/night temperatures in outdoor, sunlit, environment-controlled chambers. Leaf photosynthesis of IR72 favoured higher growth temperatures more than M103. Rubisco total activity and protein content were negatively affected in both genotypes by high temperatures and elevated CO2. However, at moderate to high growth temperatures, IR72 leaves averaged 71 and 39% more rbcS transcripts than M103 under ambient and elevated CO2, respectively, and likewise had greater Rubisco activity and protein content. Expression of psbA (D1 protein of PSII) in IR72 leaves increased with temperature, whereas it remained constant for M103, except for a 20% decline at 40/30 °C under elevated CO2. Even at the highest growth temperatures, PSII photochemical efficiency was not impaired in either genotype grown under either ambient or elevated CO2. Genotypic differences exist in rice for carboxylation responses to elevated CO2 and high temperatures, which may be useful in developing genotypes suited to cope with global climate changes. [source] Effect of a nonhost-selective toxin from Alternaria alternata on chloroplast-electron transfer activity in Eupatorium adenophorumPLANT PATHOLOGY, Issue 5 2005S. Chen AAC-toxin, a putative nonhost-selective phytotoxin, was obtained from Alternaria alternata causing a brown leaf spot disease of Crofton weed (Eupatorium adenophorum). The effect of AAC-toxin on the electron transfer reaction of chloroplasts showed that the activity of photosystem II, but not photosystem I, was completely inhibited by the toxin. AAC-toxin affected the following chlorophyll fluorescence parameters: coefficient of photochemical quenching (qP), the half-time value of fluorescence rise, and the O,J,I,P fluorescence induction kinetics curve, but not the ratio values of Fv/Fm (the quantum yield of photosystem II) and the half-time value of fluorescence quenching. It was concluded that the toxin inhibited electron transfer from QA to QB (primary and secondary quinine acceptors of photosystem II) in photosystem II by competing with QB for the binding site in D1 protein on the thylakoid membrane. [source] | |||||||||||||