Structure of the Cytochrome B6 F Complex of Oxygenic Photosynthesis
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Light-Induced Psba Translation in Plants Is Triggered by Photosystem II Damage Via an Assembly-Linked Autoregulatory Circuit
Light-induced psbA translation in plants is triggered by photosystem II damage via an assembly-linked autoregulatory circuit Prakitchai Chotewutmontria and Alice Barkana,1 aInstitute of Molecular Biology, University of Oregon, Eugene, OR 97403 Edited by Krishna K. Niyogi, University of California, Berkeley, CA, and approved July 22, 2020 (received for review April 26, 2020) The D1 reaction center protein of photosystem II (PSII) is subject to mRNA to provide D1 for PSII repair remain obscure (13, 14). light-induced damage. Degradation of damaged D1 and its re- The consensus view in recent years has been that psbA transla- placement by nascent D1 are at the heart of a PSII repair cycle, tion for PSII repair is regulated at the elongation step (7, 15–17), without which photosynthesis is inhibited. In mature plant chloro- a view that arises primarily from experiments with the green alga plasts, light stimulates the recruitment of ribosomes specifically to Chlamydomonas reinhardtii (Chlamydomonas) (18). However, we psbA mRNA to provide nascent D1 for PSII repair and also triggers showed recently that regulated translation initiation makes a a global increase in translation elongation rate. The light-induced large contribution in plants (19). These experiments used ribo- signals that initiate these responses are unclear. We present action some profiling (ribo-seq) to monitor ribosome occupancy on spectrum and genetic data indicating that the light-induced re- cruitment of ribosomes to psbA mRNA is triggered by D1 photo- chloroplast open reading frames (ORFs) in maize and Arabi- damage, whereas the global stimulation of translation elongation dopsis upon shifting seedlings harboring mature chloroplasts is triggered by photosynthetic electron transport. -
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 The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity.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. -
Etude Des Sources De Carbone Et D'énergie Pour La Synthèse Des Lipides De Stockage Chez La Microalgue Verte Modèle Chlamydo
Aix Marseille Université L'Ecole Doctorale 62 « Sciences de la Vie et de la Santé » Etude des sources de carbone et d’énergie pour la synthèse des lipides de stockage chez la microalgue verte modèle Chlamydomonas reinhardtii Yuanxue LIANG Soutenue publiquement le 17 janvier 2019 pour obtenir le grade de « Docteur en biologie » Jury Professor Claire REMACLE, Université de Liège (Rapporteuse) Dr. David DAUVILLEE, CNRS Lille (Rapporteur) Professor Stefano CAFFARRI, Aix Marseille Université (Examinateur) Dr. Gilles PELTIER, CEA Cadarache (Invité) Dr. Yonghua LI-BEISSON, CEA Cadarache (Directeur de thèse) 1 ACKNOWLEDGEMENTS First and foremost, I would like to express my sincere gratitude to my advisor Dr. Yonghua Li-Beisson for the continuous support during my PhD study and also gave me much help in daily life, for her patience, motivation and immense knowledge. I could not have imagined having a better mentor. I’m also thankful for the opportunity she gave me to conduct my PhD research in an excellent laboratory and in the HelioBiotec platform. I would also like to thank another three important scientists: Dr. Gilles Peltier (co- supervisor), Dr. Fred Beisson and Dr. Pierre Richaud who helped me in various aspects of the project. I’m not only thankful for their insightful comments, suggestion, help and encouragement, but also for the hard question which incented me to widen my research from various perspectives. I would also like to thank collaboration from Fantao, Emmannuelle, Yariv, Saleh, and Alisdair. Fantao taught me how to cultivate and work with Chlamydomonas. Emmannuelle performed bioinformatic analyses. Yariv, Saleh and Alisdair from Potsdam for amino acid analysis. -
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. -
Lecture Inhibition of Photosynthesis Inhibition at Photosystem I
1 Lecture Inhibition of Photosynthesis Inhibition at Photosystem I 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 I are considered to be contact herbicides and are often referred to as membrane disruptors. The end result is that cell membranes are rapidly destroyed resulting in leakage of cell contents into the intercellular spaces. These herbicides act as “electron interceptors” or “electron thieves” within Photosystem I of the light reaction of photosynthesis. They divert electrons from the normal electron transport sequence necessary in Photosystem I. This in turn inhibits photosynthesis. The membrane disruption occurs as a result of secondary responses. Herbicides that inhibit Photosystem I are represented by only one family, the bipyridyliums. See chemical structure shown under herbicide families. These molecules are cationic (positively charged) and are therefore highly water soluble. Their cationic properties also make them highly adsorbed to soil colloids resulting in no soil activity. 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). -
Photosystem I-Based Applications for the Photo-Catalyzed Production of Hydrogen and Electricity
University of Tennessee, Knoxville TRACE: Tennessee Research and Creative Exchange Doctoral Dissertations Graduate School 12-2014 Photosystem I-Based Applications for the Photo-catalyzed Production of Hydrogen and Electricity Rosemary Khuu Le University of Tennessee - Knoxville, [email protected] Follow this and additional works at: https://trace.tennessee.edu/utk_graddiss Part of the Biochemical and Biomolecular Engineering Commons Recommended Citation Le, Rosemary Khuu, "Photosystem I-Based Applications for the Photo-catalyzed Production of Hydrogen and Electricity. " PhD diss., University of Tennessee, 2014. https://trace.tennessee.edu/utk_graddiss/3146 This Dissertation is brought to you for free and open access by the Graduate School at TRACE: Tennessee Research and Creative Exchange. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of TRACE: Tennessee Research and Creative Exchange. For more information, please contact [email protected]. To the Graduate Council: I am submitting herewith a dissertation written by Rosemary Khuu Le entitled "Photosystem I- Based Applications for the Photo-catalyzed Production of Hydrogen and Electricity." I have examined the final electronic copy of this dissertation for form and content and recommend that it be accepted in partial fulfillment of the equirr ements for the degree of Doctor of Philosophy, with a major in Chemical Engineering. Paul D. Frymier, Major Professor We have read this dissertation and recommend its acceptance: Eric T. Boder, Barry D. Bruce, Hugh M. O'Neill Accepted for the Council: Carolyn R. Hodges Vice Provost and Dean of the Graduate School (Original signatures are on file with official studentecor r ds.) Photosystem I-Based Applications for the Photo-catalyzed Production of Hydrogen and Electricity A Dissertation Presented for the Doctor of Philosophy Degree The University of Tennessee, Knoxville Rosemary Khuu Le December 2014 Copyright © 2014 by Rosemary Khuu Le All rights reserved. -
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. -
Can Ferredoxin and Ferredoxin NADP(H) Oxidoreductase Determine the Fate of Photosynthetic Electrons?
Send Orders for Reprints to [email protected] Current Protein and Peptide Science, 2014, 15, 385-393 385 The End of the Line: Can Ferredoxin and Ferredoxin NADP(H) Oxidoreductase Determine the Fate of Photosynthetic Electrons? Tatjana Goss and Guy Hanke* Department of Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück,11 Barbara Strasse, Osnabrueck, DE-49076, Germany Abstract: At the end of the linear photosynthetic electron transfer (PET) chain, the small soluble protein ferredoxin (Fd) transfers electrons to Fd:NADP(H) oxidoreductase (FNR), which can then reduce NADP+ to support C assimilation. In addition to this linear electron flow (LEF), Fd is also thought to mediate electron flow back to the membrane complexes by different cyclic electron flow (CEF) pathways: either antimycin A sensitive, NAD(P)H complex dependent, or through FNR located at the cytochrome b6f complex. Both Fd and FNR are present in higher plant genomes as multiple gene cop- ies, and it is now known that specific Fd iso-proteins can promote CEF. In addition, FNR iso-proteins vary in their ability to dynamically interact with thylakoid membrane complexes, and it has been suggested that this may also play a role in CEF. We will highlight work on the different Fd-isoproteins and FNR-membrane association found in the bundle sheath (BSC) and mesophyll (MC) cell chloroplasts of the C4 plant maize. These two cell types perform predominantly CEF and LEF, and the properties and activities of Fd and FNR in the BSC and MC are therefore specialized for CEF and LEF re- spectively. -
(CP) Gene of Papaya Ri
Results and Discussion 4. RESULTS AND DISCUSSION 4.1 Genetic diversity analysis of coat protein (CP) gene of Papaya ringspot virus-P (PRSV-P) isolates from multiple locations of Western India Results – 4.1.1 Sequence analysis In this study, fourteen CP gene sequences of PRSV-P originating from multiple locations of Western Indian States, Gujarat and Maharashtra (Fig. 3.1), have been analyzed and compared with 46 other CP sequences from different geographic locations of America (8), Australia (1), Asia (13) and India (24) (Table 4.1; Fig. 4.1). The CP length of the present isolates varies from 855 to 861 nucleotides encoding 285 to 287 amino acids. Fig. 4.1: Amplification of PRSV-P coat protein (CP) gene from 14 isolates of Western India. From left to right lanes:1: Ladder (1Kb), 2: IN-GU-JN, 3: IN-GU-SU, 4: IN-GU-DS, 5: IN-GU-RM, 6: IN-GU-VL, 7: IN-MH-PN, 8: IN-MH-KO, 9: IN-MH-PL, 10: IN-MH-SN, 11: IN-MH-JL, 12: IN-MH-AM, 13: IN-MH-AM, 14: IN-MH-AK, 15: IN-MH-NS,16: Negative control. Red arrow indicates amplicon of Coat protein (CP) gene. Table 4.1: Sources of coat protein (CP) gene sequences of PRSV-P isolates from India and other countries used in this study. Country Name of Length GenBank Origin¥ Reference isolates* (nts) Acc No IN-GU-JN GU-Jamnagar 861 MG977140 This study IN-GU-SU GU-Surat 855 MG977142 This study IN-GU-DS GU-Desalpur 855 MG977139 This study India IN-GU-RM GU-Ratlam 858 MG977141 This study IN-GU-VL GU-Valsad 855 MG977143 This study IN-MH-PU MH-Pune 861 MH311882 This study Page | 36 Results and Discussion IN-MH-PN MH-Pune -
Itraq-Based Proteome Profiling Revealed the Role of Phytochrome A
www.nature.com/scientificreports OPEN iTRAQ‑based proteome profling revealed the role of Phytochrome A in regulating primary metabolism in tomato seedling Sherinmol Thomas1, Rakesh Kumar2,3, Kapil Sharma2, Abhilash Barpanda1, Yellamaraju Sreelakshmi2, Rameshwar Sharma2 & Sanjeeva Srivastava1* In plants, during growth and development, photoreceptors monitor fuctuations in their environment and adjust their metabolism as a strategy of surveillance. Phytochromes (Phys) play an essential role in plant growth and development, from germination to fruit development. FR‑light (FR) insensitive mutant (fri) carries a recessive mutation in Phytochrome A and is characterized by the failure to de‑etiolate in continuous FR. Here we used iTRAQ‑based quantitative proteomics along with metabolomics to unravel the role of Phytochrome A in regulating central metabolism in tomato seedlings grown under FR. Our results indicate that Phytochrome A has a predominant role in FR‑mediated establishment of the mature seedling proteome. Further, we observed temporal regulation in the expression of several of the late response proteins associated with central metabolism. The proteomics investigations identifed a decreased abundance of enzymes involved in photosynthesis and carbon fxation in the mutant. Profound accumulation of storage proteins in the mutant ascertained the possible conversion of sugars into storage material instead of being used or the retention of an earlier profle associated with the mature embryo. The enhanced accumulation of organic sugars in the seedlings indicates the absence of photomorphogenesis in the mutant. Plant development is intimately bound to the external light environment. Light drives photosynthetic carbon fxa- tion and activates a set of signal-transducing photoreceptors that regulate plant growth and development. -
CV – Professor Toshiki ENOMOTO
CV – Professor Toshiki ENOMOTO Name: Toshiki ENOMOTO, Ph.D. Date of Birth: May 14th 1958 Nationality: Japanese Present Position: Professor of Department of Food Science (Food Chemistry Laboratory), Faculty of Bioresources and Environmental Sciences, Ishikawa Prefectural University Office Address 1-308 Suematsu, Nonoichi, Ishikawa 921-8836, Japan Tel and Fax: +81-76-227-7452 E-mail: [email protected] Educational Background: 1983 Received BS. From Dept of Animal Science, Obihiro University of Agriculture and Veterinary Medicine 1985 Received MS. From Graduate School of Agricultural Science, Osaka Prefecture University 1988 Received PhD. From Graduate School of Agricultural Science, Osaka Prefecture University Research Field: Food Chemistry and Food Function Research Themes in 2019 1. Identification of oligosaccharides in honey 2. The volatile compounds of Kaga boucya (roasted stem tea) 3. Chemical composition and microflora of Asian fermented fish products 4. Anti-influenza virus activity of agricultural, forestry and fishery products 5. Chemical composition and microflora of kefir 6. Elucidation of detoxification mechanism of tetrodotoxin from puffer fish ovaries picked in rice bran Professional Carrier: 1988 Assistant Professor, Division of Life and Health Sciences, 1 Joetsu University of Education 1993 Associate Professor, Department of Food Science, Ishikawa Agricultural College 1994-1995 Visiting Scientist Supported by Ministry of Education, Culture, Sports, Science and Technology-Japan, School of Biological Sciences, University -
Glycolysis Citric Acid Cycle Oxidative Phosphorylation Calvin Cycle Light
Stage 3: RuBP regeneration Glycolysis Ribulose 5- Light-Dependent Reaction (Cytosol) phosphate 3 ATP + C6H12O6 + 2 NAD + 2 ADP + 2 Pi 3 ADP + 3 Pi + + 1 GA3P 6 NADP + H Pi NADPH + ADP + Pi ATP 2 C3H4O3 + 2 NADH + 2 H + 2 ATP + 2 H2O 3 CO2 Stage 1: ATP investment ½ glucose + + Glucose 2 H2O 4H + O2 2H Ferredoxin ATP Glyceraldehyde 3- Ribulose 1,5- Light Light Fx iron-sulfur Sakai-Kawada, F Hexokinase phosphate bisphosphate - 4e + center 2016 ADP Calvin Cycle 2H Stroma Mn-Ca cluster + 6 NADP + Light-Independent Reaction Phylloquinone Glucose 6-phosphate + 6 H + 6 Pi Thylakoid Tyr (Stroma) z Fe-S Cyt f Stage 1: carbon membrane Phosphoglucose 6 NADPH P680 P680* PQH fixation 2 Plastocyanin P700 P700* D-(+)-Glucose isomerase Cyt b6 1,3- Pheophytin PQA PQB Fructose 6-phosphate Bisphosphoglycerate ATP Lumen Phosphofructokinase-1 3-Phosphoglycerate ADP Photosystem II P680 2H+ Photosystem I P700 Stage 2: 3-PGA Photosynthesis Fructose 1,6-bisphosphate reduction 2H+ 6 ADP 6 ATP 6 CO2 + 6 H2O C6H12O6 + 6 O2 H+ + 6 Pi Cytochrome b6f Aldolase Plastoquinol-plastocyanin ATP synthase NADH reductase Triose phosphate + + + CO2 + H NAD + CoA-SH isomerase α-Ketoglutarate + Stage 2: 6-carbonTwo 3- NAD+ NADH + H + CO2 Glyceraldehyde 3-phosphate Dihydroxyacetone phosphate carbons Isocitrate α-Ketoglutarate dehydogenase dehydrogenase Glyceraldehyde + Pi + NAD Isocitrate complex 3-phosphate Succinyl CoA Oxidative Phosphorylation dehydrogenase NADH + H+ Electron Transport Chain GDP + Pi 1,3-Bisphosphoglycerate H+ Succinyl CoA GTP + CoA-SH Aconitase synthetase