DOCSLIB.ORG

Analysis of Hydrogen Peroxide–Independent Expression of the High-Light–Inducible ELIP2 Gene with the Aid of the ELIP2 Promoter–Luciferase Fusion{

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Analysis of Hydrogen Peroxide–Independent Expression of the High-Light–Inducible ELIP2 Gene with the Aid of the ELIP2 Promoter–Luciferase Fusion{ Photochemistry and Photobiology, 2003, 77(6): 668–674 Analysis of Hydrogen Peroxide–independent Expression of the High-light–inducible ELIP2 Gene with the Aid of the ELIP2 Promoter–Luciferase Fusion{ Mitsuhiro Kimura1,2,3, Katsushi Manabe3, Tomoko Abe2, Shigeo Yoshida2, Minami Matsui1 and Yoshiharu Y. Yamamoto*1,2 1Plant Function Exploration Team, RIKEN Genomic Sciences Center, Tsurumi-Ku, Yokohama, Kanagawa, Japan; 2Plant Functions Laboratory, RIKEN, Hirosawa, Wako, Saitama, Japan and 3Graduate School of Integrated Science, Yokohama City University, Kanazawa-Ku, Yokohama, Kanagawa, Japan Received 4 December 2002; accepted 20 March 2003 ABSTRACT However, an intense and unmanageable amount of light (high light) spells danger for the plant. Under high-light conditions, Intense and excessive light triggers the evolution of reactive electrons leak from excited chlorophylls as well as from the oxygen species in chloroplasts, and these have the potential to photosynthetic electron transport system (ETS), resulting in the cause damage. However, plants are able to respond to light generation of oxygen and lipid radicals. These damage proteins, stress and protect the chloroplasts by various means, including lipids, pigments, DNA and all other components of the chloroplast transcriptional regulation at the nucleus. Activation of light (1). However, higher plants have developed several strategies to stress–responsive genes is mediated via hydrogen peroxide– protect the chloroplasts from high light. These include reduction of dependent and –independent pathways. In this study, we antenna size, downregulation of Photosystem II, photorespiration, characterized the Early-Light–Inducible Protein 2 (ELIP2) development of radical scavengers and induction of nonphoto- promoter–luciferase gene fusion (ELIP2::LUC), which re- chemical quenching to reduce the excitation energy transferred sponds only to the hydrogen peroxide–independent pathway. from the antenna to the reaction centers (1–3). Some of these high- Our results show that ELIP2::LUC is expressed under light responses are controlled at the level of gene expression. nonstressful conditions in green tissue containing juvenile Several nuclear genes have been reported to be activated by high and developing chloroplasts. Upon light stress, expression was light, including Early-Light–Inducible Protein (ELIP) (4), genes activated in leaves with mature as well as developing encoding active oxygen scavengers (5), actin, LEA, metallothio- chloroplasts. In contrast to another high-light–inducible gene, nein (6), a putative transcription factor (7) and others with APX2, which responds to the hydrogen peroxide–dependent unknown functions (6,8). Recently, microarray analysis has pathway, the activation of ELIP2::LUC was cell autonomous. revealed about 100 high-light–inducible genes of Arabidopsis The activation was suppressed by application of 3-(3,4)- (9,10). The Arabidopsis APX2 gene that encodes cytosolic dichlorophenyl-1,1-dimethylurea, an inhibitor of the reduction ascorbate peroxidase has been most frequently used to study the of plastoquinone, whereas 2,5-dibromo-3-methyl-6-isopropyl- molecular mechanism of high-light activation of nuclear gene p-benzoquinone, an inhibitor of the oxidation of plastoquinone, expression. The high-light activation of APX2 is mediated by gave the contrasting effect, which may suggest that the redox hydrogen peroxide, which accumulates through excess light- state of the plastoquinone plays an important role in triggering dependent generation of oxygen radicals (11). Furthermore, it has the hydrogen peroxide–independent light stress signaling. been shown that the high-light signal for activation of APX2 is mediated from cell to cell (11). In addition, reduction of the plastoquinone pool has been suggested to be necessary for INTRODUCTION activation of APX2. However, many things need to be revealed For plants, sunlight is the one and only source of energy for to understand the whole signaling pathway from high-light photosynthesis and thus is indispensable for the growth of plants. perception to gene expression, including the relationship between reduction of the plastoquinone pool and generation of hydrogen peroxide, its perception and the downstream events after hydrogen {Posted on the website on 7 April 2003. peroxide accumulation. Furthermore, it is not known if all the high- *To whom correspondence should be addressed at: Plant Functions light–regulated genes are controlled by the same mechanism as Laboratory, RIKEN, Hirosawa 2-1, Wako, Saitama 351-0198, Japan. Fax: 8148-462-4674; e-mail: [email protected] APX2. Abbreviations: APX2::LUC, APX2 promoter–luciferase fusion; CCD, The ELIP was first identified from the pea as a transcript that charge-coupled device; DBMIB, 2,5-dibromo-3-methyl-6-isopropyl-p- was rapidly induced by light during greening (12). Subsequent benzoquinone; DCMU, 3-(3,4)-dichlorophenyl-1,1-dimethylurea; ELIP, analyses revealed that ELIP belongs to the CAB superfamily and early-light–inducible protein; ELIP2::LUC, ELIP2 promoter–luciferase fusion; ETS, electron transport system; mRNA, messenger RNA; RNase, associates with Photosystem II at the thylakoid membrane (4,13). ribonuclease; RT-PCR, reverse transcriptase–polymerse chain reaction. Because its expression is induced by light stress in many species, it Ó 2003 American Society for Photobiology 0031-8655/03 $5.00þ0.00 has been speculated that ELIP is an antistress component for the 668 Photochemistry and Photobiology, 2003, 77(6) 669 MATERIALS AND METHODS Plant material and light treatment. Preparation of transgenic Arabi- dopsis containing ELIP2::LUC (17), APX2 promoter–luciferase fusion (APX2::LUC) (11), 35S::LUC and plastocyanin promoter–luciferase fusion (PC::LUC) (18) is described elsewhere. Seeds of wild-type and transgenic Arabidopsis were surface sterilized, sown on GM medium supplemented with 0.8% Bactoagar (Difco, Detroit, MI) and 1% sucrose, cold treated for 2–4 days and grown under low-light conditions (6 W mÿ2, equivalent to ca 30 lmol mÿ2 sÿ1)at228C (17). Eight day-old seedlings were subjected to high-light treatment with a fluence rate of 150 W mÿ2 (equivalent to ca 800 lmol mÿ2 sÿ1) for 3 h, as described previously (17). For the experiments shown in Fig. 5, leaves grown in a greenhouse were detached, kept on GM medium for 1 day under low light (6 W mÿ2)at228C and locally irradiated with high light (150 W mÿ2) for 3 h at 228C with the aid of stainless sheets cut to remove either a straight slit or a Y-shaped slit. For 3-(3,4)- dichlorophenyl-1,1-dimethylurea (DCMU) and 2,5-dibromo-3-methyl-6- isopropyl-p-benzoquinone (DBMIB) treatments, 2 mL of the inhibitor solutions containing 1.8% (vol/vol) ethanol were sprayed per circular culture dish (10 cm diameter) 3 h before high-light treatments and sprayed again just before high-light treatment only for the DBMIB treatment (19). For controls, the corresponding amount of the ethanol solution without DCMU or DBMIB was sprayed. Luciferase assay. In vitro luciferase assays and in vivo assays using a high-performance charge-coupled device (CCD) camera were performed as described previously (17). For in vivo temporal analysis as shown in Fig. 3, seeds were sown in 96-cell black plates containing GM medium supplemented with 0.8% Bactoagar, 1% sucrose and 1 mM luciferin. They were cold treated for 2–4 days. The plates were sealed with clear adhesive sheets that had a tiny hole for each well and put into an automated scintillation counter (Topcount, Packard Japan, Tokyo, Japan). The plates were kept in the dark assay chamber for 5 min before starting the counting to allow the delayed chlorophyll fluorescence to fade. An assay was done Figure 1. Observation of ELIP2::LUC activation by high light. A and B: ÿ2 Induction of luciferase activity by high light in ELIP2::LUC transgenic for a week at 228C under dark or light (6 W m ) conditions. The data from plants observed with a high-performance CCD camera. A: Photograph of 8 an assay were logged into a text file and subsequently analyzed using Excel day old transgenic seedlings. B: Pseudocolor image of bioluminescence by software (Microsoft Japan, Tokyo, Japan). Typically, an assay for a week luciferase activity. Left, seedlings treated without high light (ÿHL). Right, was composed of about 400 data points. seedlings treated with high light (þHL, 150 W mÿ2 for 3 h). The color scale RNA analysis. Eight day-old seedlings were treated with or without high on the right shows the luminescence intensity from dark blue (lowest) to light for 3 h, and the aerial part of the seedlings was harvested for RNA white (highest). C: Photograph of a 2 week old seedling grown under low extraction (20). The ELIP2 messenger RNA (mRNA) was detected by light (6 W mÿ2). D: The corresponding bioluminescence image representing quantitative reverse transcriptase–polymerase chain reaction (RT-PCR) luciferase activity. The picture in (D) is a synthetic image created by according to a previous report (17). As a negative control, a RNA prep was overwriting the bioluminescence image (color) onto the black-and-white treated with ribonuclease (RNase) A for 6 h at 378C and used as a template image of the seedling. Both images in (D) were captured by the same CCD for RT-PCR. camera. Color bar indicates the scale of the color. protection of Photosystem II, although the biochemical function of RESULTS ELIP remains to be elucidated (4). Expression of ELIP2::LUC under nonstressful conditions Arabidopsis has two ELIP genes,
Load more

Recommended publications
  • Evolution of Photochemical Reaction Centres
    bioRxiv preprint doi: https://doi.org/10.1101/502450; this version posted December 20, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. 1 Evolution of photochemical reaction 2 centres: more twists? 3 4 Tanai Cardona, A. William Rutherford 5 Department of Life Sciences, Imperial College London, London, UK 6 Correspondence to: [email protected] 7 8 Abstract 9 The earliest event recorded in the molecular evolution of photosynthesis is the structural and 10 functional specialisation of Type I (ferredoxin-reducing) and Type II (quinone-reducing) reaction 11 centres. Here we point out that the homodimeric Type I reaction centre of Heliobacteria has a Ca2+- 12 binding site with a number of striking parallels to the Mn4CaO5 cluster of cyanobacterial 13 Photosystem II. This structural parallels indicate that water oxidation chemistry originated at the 14 divergence of Type I and Type II reaction centres. We suggests that this divergence was triggered by 15 a structural rearrangement of a core transmembrane helix resulting in a shift of the redox potential 16 of the electron donor side and electron acceptor side at the same time and in the same redox direction. 17 18 Keywords 19 Photosynthesis, Photosystem, Water oxidation, Oxygenic, Anoxygenic, Reaction centre 20 21 Evolution of Photosystem II 22 There is no consensus on when and how oxygenic photosynthesis originated. Both the timing and the 23 evolutionary mechanism are disputed.
    [Show full text]
  • Chapter 3 the Title and Subtitle of This Chapter Convey a Dual Meaning
    3.1. Introduction Chapter 3 The title and subtitle of this chapter convey a dual meaning. At first reading, the subtitle Photosynthetic Reaction might seem to indicate that the topic of the structure, function and organization of Centers: photosynthetic reaction centers is So little time, so much to do exceedingly complex and that there is simply insufficient time or space in this brief article to cover the details. While this is John H. Golbeck certainly the case, the subtitle is Department of Biochemistry additionally meant to convey the idea that there is precious little time after the and absorption of a photon to accomplish the Molecular Biology task of preserving the energy in the form of The Pennsylvania State University stable charge separation. University Park, PA 16802 USA The difficulty is there exists a fundamental physical limitation in the amount of time available so that a photochemically induced excited state can be utilized before the energy is invariably wasted. Indeed, the entire design philosophy of biological reaction centers is centered on overcoming this physical, rather than chemical or biological, limitation. In this chapter, I will outline the problem of conserving the free energy of light-induced charge separation by focusing on the following topics: 3.2. Definition of the problem: the need to stabilize a charge-separated state. 3.3. The bacterial reaction center: how the cofactors and proteins cope with this problem in a model system. 3.4. Review of Marcus theory: what governs the rate of electron transfer in proteins? 3.5. Photosystem II: a variation on a theme of the bacterial reaction center.
    [Show full text]
  • Nourishing and Health Benefits of Coenzyme Q10 – a Review
    Czech J. Food Sci. Vol. 26, No. 4: 229–241 Nourishing and Health Benefits of Coenzyme Q10 – a Review Martina BOREKOVÁ1, Jarmila HOJEROVÁ1, Vasiľ KOPRDA1 and Katarína BAUEROVÁ2 1Institute of Biotechnology and Food Science, Faculty of Chemical and Food Technology, Slovak University of Technology, Bratislava, Slovak Republic; 2Institute of Experimental Pharmacology, Slovak Academy of Sciences, Bratislava, Slovak Republic Abstract Boreková M., Hojerová J., Koprda V., Bauerová K. (2008): Nourishing and health benefits of coen- zyme Q10 – a review. Czech J. Food Sci., 26: 229–241. Coenzyme Q10 is an important mitochondrial redox component and endogenously produced lipid-soluble antioxidant of the human organism. It plays a crucial role in the generation of cellular energy, enhances the immune system, and acts as a free radical scavenger. Ageing, poor eating habits, stress, and infection – they all affect the organism’s ability to provide adequate amounts of CoQ10. After the age of about 35, the organism begins to lose the ability to synthesise CoQ10 from food and its deficiency develops. Many researches suggest that using CoQ10 supplements alone or in com- bination with other nutritional supplements may help maintain health of elderly people or treat some of the health problems or diseases. Due to these functions, CoQ10 finds its application in different commercial branches such as food, cosmetic, or pharmaceutical industries. This review article gives a survey of the history, chemical and physical properties, biochemistry and antioxidant activity of CoQ10 in the human organism. It discusses levels of CoQ10 in the organisms of healthy people, stressed people, and patients with various diseases. This paper shows the distribution and contents of two ubiquinones in foods, especially in several kinds of grapes, the benefits of CoQ10 as nutritional and topical supplements and its therapeutic applications in various diseases.
    [Show full text]
  • Structure of the Cytochrome B6 F Complex of Oxygenic Photosynthesis
    Structure of the Cytochrome b6 f Complex of Oxygenic Photosynthesis The photosynthetic unit of oxygenic photosynthesis data of 3.0 Å from the complex crystal with another is organized as two large multimolecular membrane analogue inhibitor, TDS, was collected at the SBC complexes, photosystem II (PSII) that extracts low- beamline 19ID, APS. The initial model was developed energy electrons from water and photosystem I (PSI) into a 3.4 Å map of the native complex. Final that raises the energy level of such electrons using refinement was carried out with a dataset from a co- light energy to produce a strong reductant, NADPH. crystal with TDS (Figs. 2, 3). The two photosystems operate in a series linked by a Viewed along the membrane normal, the b6f × third multiprotein complex called the cytochrome b6f complex is 90 Å 55 Å within the membrane side, × complex (Fig.1). The cytochrome b6f complex is a and 120 Å 75 Å on the lumen (p)side (Fig. 2). A membrane-spanning protein complex embedded in prominent feature of this structure is an extended the thylakoid membrane of photosynthetic organisms. quinone exchange cavity between the monomers, The molecular weight of the complex is 220,000 as a which exchanges lipophilic plastoquinone in the dimer with 26 transmembrane helices. The b6f complex bilayer center, and also mediates the electron and controls the electron transfer between the plastoquinol proton transfer across the complex. The heme-binding reduced by PSII and the electron carrier protein 4 transmembrane helices core of the b6f complex plastocyanin that associate with PSI.
    [Show full text]
  • Plastoquinol As a Singlet Oxygen Scavenger in Photosystem II ⁎ Jerzy Kruk A, , Achim Trebst B
    Available online at www.sciencedirect.com Biochimica et Biophysica Acta 1777 (2008) 154–162 www.elsevier.com/locate/bbabio Plastoquinol as a singlet oxygen scavenger in photosystem II ⁎ Jerzy Kruk a, , Achim Trebst b a Department of Plant Physiology and Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland b Plant Biochemistry, Ruhr-University Bochum, D-44780 Bochum, Germany Received 4 July 2007; received in revised form 16 October 2007; accepted 17 October 2007 Available online 25 October 2007 Abstract It has been found that in Chlamydomonas reinhardtii cells, under high-light stress, the level of reduced plastoquinone considerably increases while in the presence of pyrazolate, an inhibitor of plastoquinone and tocopherol biosynthesis, the content of reduced plastoquinone quickly decreases, similarly to α-tocopherol. In relation to chlorophyll, after 18 h of growth under low light with the inhibitor, the content of α-tocopherol was 22.2 mol/1000 mol chlorophyll and that of total plastoquinone (oxidized and reduced) was 19 mol/1000 mol chlorophyll, while after 2 h of high-light stress the corresponding amounts dropped to 6.4 and 6.2 mol/1000 mol chlorophyll for α-tocopherol and total plastoquinone, respectively. The degradation of both prenyllipids was partially reversed by diphenylamine, a singlet oxygen scavenger. It was concluded that plastoquinol, as well as α-tocopherol is decomposed under high-light stress as a result of a scavenging reaction of singlet oxygen generated in photosystem II. The levels of both α-tocopherol and of the reduced plastoquinone are not affected significantly in the absence of the inhibitor due to a high turnover rate of both prenyllipids, i.e., their degradation is compensated by fast biosynthesis.
    [Show full text]
  • Regulation of Photosynthetic Electron Transport☆
    Biochimica et Biophysica Acta 1807 (2011) 375–383 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbabio Review Regulation of photosynthetic electron transport☆ Jean-David Rochaix ⁎ Department of Molecular Biology, University of Geneva, Geneva, Switzerland Department of Plant Biology, University of Geneva, Geneva, Switzerland article info abstract Article history: The photosynthetic electron transport chain consists of photosystem II, the cytochrome b6 f complex, Received 14 September 2010 photosystem I, and the free electron carriers plastoquinone and plastocyanin. Light-driven charge separation Received in revised form 11 November 2010 events occur at the level of photosystem II and photosystem I, which are associated at one end of the chain Accepted 13 November 2010 with the oxidation of water followed by electron flow along the electron transport chain and concomitant Available online 29 November 2010 pumping of protons into the thylakoid lumen, which is used by the ATP synthase to generate ATP. At the other end of the chain reducing power is generated, which together with ATP is used for CO assimilation. A Keywords: 2 Electron transport remarkable feature of the photosynthetic apparatus is its ability to adapt to changes in environmental Linear electron flow conditions by sensing light quality and quantity, CO2 levels, temperature, and nutrient availability. These Cyclic electron flow acclimation responses involve a complex signaling network in the chloroplasts comprising the thylakoid Photosystem II protein kinases Stt7/STN7 and Stl1/STN7 and the phosphatase PPH1/TAP38, which play important roles in Photosystem I state transitions and in the regulation of electron flow as well as in thylakoid membrane folding.
    [Show full text]
  • Light-Harvesting Chlorophyll Pigments Enable Mammalian Mitochondria To
    ß 2014. Published by The Company of Biologists Ltd | Journal of Cell Science (2014) 127, 388–399 doi:10.1242/jcs.134262 RESEARCH ARTICLE Light-harvesting chlorophyll pigments enable mammalian mitochondria to capture photonic energy and produce ATP Chen Xu, Junhua Zhang, Doina M. Mihai and Ilyas Washington* ABSTRACT concentrations, and extends the median life span of Caenorhabditis elegans, upon light exposure; supporting the Sunlight is the most abundant energy source on this planet. However, hypothesis that photonic energy capture through dietary-derived the ability to convert sunlight into biological energy in the form of metabolites may be an important means of energy regulation in adenosine-59-triphosphate (ATP) is thought to be limited to animals. The presented data are consistent with the hypothesis chlorophyll-containing chloroplasts in photosynthetic organisms. that metabolites of dietary chlorophyll modulate mitochondrial Here we show that mammalian mitochondria can also capture light ATP stores by catalyzing the reduction of coenzyme Q. These and synthesize ATP when mixed with a light-capturing metabolite of findings have implications for our understanding of aging, normal chlorophyll. The same metabolite fed to the worm Caenorhabditis cell function and life on earth. elegans leads to increase in ATP synthesis upon light exposure, along with an increase in life span. We further demonstrate the same RESULTS potential to convert light into energy exists in mammals, as Light-driven ATP synthesis in isolated mammalian mitochondria chlorophyll metabolites accumulate in mice, rats and swine when To demonstrate that dietary chlorophyll metabolites can modulate fed a chlorophyll-rich diet. Results suggest chlorophyll type ATP levels, we examined the effects of the chlorophyll molecules modulate mitochondrial ATP by catalyzing the reduction metabolite pyropheophorbide-a (P-a) on ATP synthesis in of coenzyme Q, a slow step in mitochondrial ATP synthesis.
    [Show full text]
  • Ph DEPENDENCE of the EFFECTS of DIURON, ATRAZINE and DINOSEB on the LUMINESCENT PROPERTIES of THYLAKOID MEMBRANES
    BULG. J. PLANT PHYSIOL., 2001, 27(1–2), 85–100 85 pH DEPENDENCE OF THE EFFECTS OF DIURON, ATRAZINE AND DINOSEB ON THE LUMINESCENT PROPERTIES OF THYLAKOID MEMBRANES Petar Lambrev, Vassilij Goltsev* Department of Biophysics and Radiobiology, Biological Faculty, University of Sofia “St. Kliment Ohridski” Received May 17, 2001 Summary. The effect of the external pH in the range of 5.5 to 8.0 on the activity of three PSII herbicides (diuron, atrazine and dinoseb) was studied in isolated thylakoid membranes by means of prompt and delayed fluores- cence induction kinetics. Well-expressed pH dependence was established for prompt fluorescence parameters (Fv/Fm, Fi/Fm) as well as for delayed fluores- cence parameters (I1, I2). Two types of pH dependence of the herbicide effect were observed. The apparent resistance to herbicides of the urea/triazine type (diuron and atrazine) was found to be maximal at pH 6–6.5, although the amplitude of the herbicide effect was different between diuron and atrazine. The pH dependences for thylakoids treated with the phenolic herbicide, dino- seb, showed a minimum in the herbicide effect at pH 7.5. The mechanism by which pH influences the herbicide sensitivity of thylakoid membranes is supposed to involve pH-induced conformational changes of the QB-binding site on the D1 protein of PSII, resulting in alteration of the affinity to the herbicide molecule. The conformation of the QB-site at a cer- tain pH is characterized by maximal herbicide resistance. The optimal value of pH depends on the type of herbicide, specifically the location of the H- bond between the herbicide molecule and D1.
    [Show full text]
  • Synthesis of Plastoquinoneanalogs and Inhibition of Photosynthetic And
    Proc. Nat. Acad. Sci. USA Vol. 69, No. 12, pp. 3713-3717, December 1972 Synthesis of Plastoquinone Analogs and Inhibition of Photosynthetic and Mammalian Enzyme Systems* (chloroplasts/beef heart/coenzyme Q/electron transport) JAN BQLERt, RONALD PARDINIt, HANNA T. M\IUSTAFAt, KARL FOLKERSt, RICHARD A. DILLEYT, AND FREDERICK L. CRANE: t Stanford Research Institute, Menlo Park, California and Institute for Biomedical Research, The University of Texas at Austin, Texas 78712; and $ Purdue University, Lafayette, Indiana 47907 Contributed by Karl Folkers, September 25, 1972 ABSTRACT New 5-hydroxy- and 5-chloro-6-alkyl-1,4- energy (ATP) and the utilization of the hydrogen of water as benzoquinones with one or two methyl groups on the a source of reducing power (NADPH2). Data from nucleus were synthesized as potential antimetabolites of several plastoquinones for biological research on photosynthetic experimental approaches indicate that plastoquinone does and mammalian enzyme systems; the primary emphasis function in the electron transport system of chloroplasts. was on photosynthesis. The data stem from extraction-restoration studies, spectro- 2,3-Dimethyl-5 - hydroxy - 6 - phytyl - 1,4 - benzoquinone photometric and chemical determination of redox changes, completely inhibited in chloroplasts the water-de- pendent electron transport, but photosystem I was in- correlation with metabolic function, and changes in electron sensitive to this analog. The data are consistent with the transport in mutants, as well as its universal distribution in all interpretation that this analog inhibits electron transport oxygen-producing photosynthetic organisms (3). in the chain prior to the site of electron donation from the To study relationships between structure and activity in ascorbate-dichlorophenolindophenol couple.
    [Show full text]
  • Lecture Inhibition of Photosynthesis Inhibition at Photosystem II
    1 Lecture Inhibition of Photosynthesis Inhibition at Photosystem II 1. General Information The popular misconception is that susceptible plants treated with these herbicides “starve to death” because they can no longer photosynthesize. In actuality, the plants die long before the food reserves are depleted. The photosynthetic inhibitors can be divided into two distinct groups, the inhibitors of Photosystem I and inhibitors of Photosystem II. Both of these groups work in the energy production step of photosynthesis, or the light reactions. Light is required as well as photosynthesis for these herbicides to kill susceptible plants. Herbicides that inhibit Photosystem II do not act as “electron interceptors” or “electron thieves” but rather they bind to the QB protein in the normal electron transport sequence, thereby blocking electron transport to the PQ pool. Herbicides that inhibit Photosystem II are represented by several herbicide families including the symmetrical triazines, triazinones (asymmetrical triazines), substituted ureas, uracils, pyridazinones, phenyl carbamates, nitriles, benzothiadiazoles, phenyl pyridazines, and acid amides. These herbicides have preemergence and/or postemergence activity. ) Note: The pyridazinones, nitrile, and acid amide families of herbicides also have specific herbicides that do not have this mode of action (will be discussed later). 2. Mode of Action See Figure 7.1 (The electron transport chain in photosynthesis and the sites of action of herbicides that interfere with electron transfer in this chain (Q = electron acceptor; PQ = plastoquinone; page 2). Review Photosystem I and II. The specific mode of action is as follows: If foliar applied, herbicide moves through the cuticle into the cell and chloroplast. It binds to the QB protein preventing it from accepting and transferring electrons to the plastoquinone (PQ) pool in Photosystem II.
    [Show full text]
  • Physiological Roles of Plastid Terminal Oxidase in Plant Stress Responses
    Review Physiological roles of plastid terminal oxidase in plant stress responses XIN SUN* and TAO WEN Agronomy College, Chengdu Campus, Sichuan Agricultural University, Chengdu 611130, China *Corresponding author (Email, [email protected]) The plastid terminal oxidase (PTOX) is a plastoquinol oxidase localized in the plastids of plants. It is able to transfer electrons from plastoquinone (PQ) to molecular oxygen with the formation of water. Recent studies have suggested that PTOX is beneficial for plants under environmental stresses, since it is involved in the synthesis of photoprotective carotenoids and chlororespiration, which could potentially protect the chloroplast electron transport chain (ETC) from over-reduction. The absence of PTOX in plants usually results in photo-bleached variegated leaves and impaired adaptation to environment alteration. Although PTOX level and activity has been found to increase under a wide range of stress conditions, the functions of plant PTOX in stress responses are still disputed now. In this paper, the possible physiological roles of PTOX in plant stress responses are discussed based on the recent progress. [Sun X and Wen T 2011 Physiological roles of plastid terminal oxidase in plant stress responses. J. Biosci. 36 951–956] DOI 10.1007/s12038-011- 9161-7 1. Introduction important role in chloroplast biogenesis (Carol and Kuntz 2001;Aluruet al. 2006). There was also evidence that PTOX Plastid terminal oxidase (PTOX), a plastid-localized plasto- is the terminal oxidase of chlororespiration and regulates the quinol (PQ)/O2 oxidoreductase, exists widely in photosyn- redox state of the PQ pool (Aluru and Rodermel 2004;Peltier thetic species including algae and higher plants (Carol and and Cournac 2002).
    [Show full text]
  • Time-Independent Structure of the Cytochrome B6f Complex† William A
    Evolution of Photosynthesis: Time-Independent Structure of the Cytochrome b6f Complex† William A. Cramer,* Huamin Zhang, Jiusheng Yan, Genji Kurisu,‡ and Janet L. Smith Department of Biological Sciences, Lilly Hall of Life Sciences, 915 West State Street, Purdue UniVersity, West Lafayette, Indiana 47907-2054 ReceiVed March 22, 2004; ReVised Manuscript ReceiVed April 7, 2004 ABSTRACT: Structures of the cytochrome b6f complex obtained from the thermophilic cyanobacterium Mastigocladus laminosus and the green alga Chlamydomonas reinhardtii, whose appearance in evolution is separated by 109 years, are almost identical. Two monomers with a molecular weight of 110 000, containing eight subunits and seven natural prosthetic groups, are separated by a large lipid-containing “quinone exchange cavity”. A unique heme, heme x, that is five-coordinated and high-spin, with no strong field ligand, occupies a position close to intramembrane heme bn. This position is filled by the n-side bound quinone, Qn, in the cytochrome bc1 complex of the mitochondrial respiratory chain. The structure and position of heme x suggest that it could function in ferredoxin-dependent cyclic electron transport as well as being an intermediate in a quinone cycle mechanism for electron and proton transfer. The significant differences between the cyanobacterial and algal structures are as follows. (i) On the n-side, a plastoquinone molecule is present in the quinone exchange cavity in the cyanobacterial complex, and a sulfolipid is bound in the algal complex at a position corresponding to a synthetic DOPC lipid molecule in the cyanobacterial complex. (ii) On the p-side, in both complexes a quinone analogue inhibitor, TDS, passes through a portal that separates the large cavity from a niche containing the Fe2S2 cluster.
    [Show full text]