DOCSLIB.ORG

(CP) Gene of Papaya Ri

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text

Load more

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 861 MG977150 This study IN-MH-KO MH-Kolhapur 858 MG977147 This study IN-MH-PL MH-Palghar 858 MG977149 This study IN-MH-SN MH-Sangli 861 MG977151 This study IN-MH-JL MH-Jalgaon 858 MG977146 This study IN-MH-AM MH-Amravati 858 MG977145 This study IN-MH-AK MH-Akola 855 MG977144 This study IN-MH-NS MH-Nashik 858 MG977148 This study IN-PU-S MH-Pune 855 AY238881 Jain et al., 2004a IN-PU-M MH-Pune 855 AF063220 Jain et al., 2004a IN-HP HP 852 AY458617 Jain et al., 2004a IN-BH BH 852 EF210196 IN-RJ RJ 855 KF989499 IN-MP MP 858 KC149501 IN-AS AS 852 KC149500 IN-SIK SIK 852 DQ354072 Jain et al., 2004a IN-MG MG 861 MF356497 Mishra and Patil, 2018 IN-CG1 CG 861 DQ354071 IN-CG2 CG 852 AY491011 Jain et al., 2004a IN-HY HR 852 DQ088670 IN-JK JH-Ranchi 852 AY458619 Jain et al., 2004a IN-UP1 UP 855 AY238882 Jain et al., 2004a IN-UP2 UP 852 AY458620 Jain et al.,2004a IN-DL DL 846 AY238883 Jain et al., 2004a IN-WB WB 852 JN979406 Srinivasulu and IN-AP1 AP 918 DQ666638 SaiGopal, 2012 Srinivasulu and IN-AP2 AP 918 AY839864 SaiGopal, 2012 IN-TN1 TN 918 DQ666641 Srinivasulu and Page | 37 Results and Discussion SaiGopal, 2012 IN-TN2 TN 858 EF104919 Srinivasulu and IN-KE KE 918 DQ666640 SaiGopal, 2012 Srinivasulu and IN-KA1 KA 918 DQ666639 SaiGopal, 2012 IN-KA2 KA 918 AY238884 Jain et al.,2004a BD Bangladesh 861 AY423557 Jain et al., 2004a CH1-HN China 867 KT895257 CH2-LM China 858 KT633943 Shen et al.,2014 ID-1 Indonesia 831 AF374864 JP-S Japan 858 D50591 MY-M185P Malaysia 861 AB044342 MN-P Myanmar 851 AB822931 Asia NP-Ne2 Nepal 852 AB823733 (other PH Philippines 834 AF374863 than SL Sri Lanka 837 U14741 Bateson et al.,1994 India) TW-YK Taiwan 861 X97251 Wang et al.,1997 Charoensilp et TH Thailand 858 AY162218 al.,2003 VN-P24 Viet Nam 834 AF506867 BR-PA1 Brazil 861 KC748221 Martinez et al.,2014 CO Colombia 861 KT275938 Ortiz-Rojas et al.,2017 CU-MT1 Cuba 861 KC748227 Martinez et al.,2014 America US-FL US (Florida) 855 AF196839 Davis et al.,1999 US-HA US (Hawaii) 861 S46722 Yeh et al.,1992 JM-FS Jamaica 834 DQ104817 Chin et al.,2007 MX-VrAl Mexico 855 AF319496 VE-T Venezuela 837 DQ339578 Chin et al.,2007 Australia AU-BD Australia 837 U14736 Bateson et al.,1994 Page | 38 Results and Discussion *Name of the isolates are abbreviated or modified in this study. References mentioned only to published sequences. Blank cells/ Columns indicates only NCBI submitted sequences which are not published. ¥Indian States Name Abbreviated as: AP: Andhra Pradesh, AS: Assam, BH:Bihar, CG: Chhattisgarh, DL: Delhi, GU: Gujarat, HP: Himachal Pradesh, HR: Haryana, JK/JH: Jharkhand, KA: Karnataka, KE: Kerala, MG: Meghalaya, MH: Maharashtra, MP: Madhya Pradesh, SIK: Sikkim,RJ: Rajasthan, TN: Tamil Nadu, UP: Uttar Pradesh, WB: West Bengal. Previously reported KE (lysine and glutamic acid) repeats in the N-terminus of the PRSV CP (Silva-Rosales et al., 2000) were observed in all isolates of PRSV-P sequence analyzed. The conserved regions commonly found in Potyviruses CP sequences such as WCIEN, PQQID, DAG and QMKAAA (Shukla et al., 1994) were present in all the PRSV-P isolates from Maharashtra and Gujarat. The 14 CP sequences obtained from this study along with 46 other reported sequences of PRSV-P were compared at amino acid and nucleotide levels (Table 4.2). A general summary of sequence diversity among 60 isolates of PRSV-P, including present isolates of Gujarat and Maharashtra, from different countries and continents have been presented (Table 4.3). The isolates from Maharashtra and Gujarat when compared with other Asian countries and other Indian isolates, showed significantly diverse heterogeneity with the sequence identity of 82-98 % at amino acid (aa) level and 81-100 % at nucleotide (nt) level amongst each other (Table 4.3). Similarly, isolates from neighboring countries showed presence of diverse PRSV population (at aa level) 87-91 % sequence identity with Bangladesh, 85-93 % with Nepal, 85-89 % with Myanmar, 87-90 % with Sri Lanka and 88-93 % with China. However, the PRSV-P isolates from Gujarat and Maharashtra were found more closely related with the PRSV-P isolate from Japan (92-94 %) and USA (91-95 %) at aa level (Table 4.2). All Indian isolates showed identity of aa to Asian isolates by 81–96 %, Australian isolates by 83-93 %, whereas showed 81- 97% with American isolates. Considerably heterogeneous population of PRSV-P was observed within Gujarat which showed the amino acid sequence identity of 91-100 %. A similar situation was also observed within Maharashtra where the shared aa sequence identities among the PRSV-P population were between 91-99 % (Table 4.3). Page | 39 Results and Discussion Table 4.2: PRSV coat protein (CP) gene (amino acid) percent identity between PRSV-P isolates from this study and other reported isolates from different countries. Gujarat State Maharashtra State JL PL SN NS PN PU JN AK SU DS KO VL AM - PRSV-P isolates RM - - - - - - - - - - - - - GU GU GU GU MH MH MH MH MH MH GU MH MH MH - - - - - - - - - - - - - - IN IN IN IN IN IN IN IN IN IN IN IN IN IN IN-HP 86 91 87 90 91 89 90 90 89 88 91 90 90 93 IN-MG 86 92 88 90 91 89 91 90 89 88 92 91 90 92 IN-BH 86 91 87 90 91 89 91 90 89 89 90 90 91 89 IN-RJ 94 94 98 96 94 92 92 94 91 93 94 94 94 90 IN-MP 90 94 90 92 94 96 95 94 95 92 92 92 93 92 IN-AS 85 90 86 89 90 88 89 89 88 87 91 91 89 92 IN-SIK 85 90 86 89 90 88 89 89 88 87 91 91 89 93 IN-CG2 87 91 87 91 91 90 92 91 90 89 91 91 91 90 IN-CG1 91 94 92 94 94 94 93 94 93 94 93 93 95 93 IN-HY 86 92 88 90 92 90 92 91 90 90 91 91 92 93 IN-JK 86 92 88 91 92 90 91 91 90 90 92 91 92 93 India IN-UP2 87 91 87 91 91 90 92 91 90 89 91 91 91 94 (other IN-UP1 90 95 92 93 95 93 93 97 92 94 93 94 95 84 states) IN-DL 87 92 89 91 92 91 92 91 90 90 92 92 92 82 IN-WB 86 92 87 91 92 91 91 90 90 90 91 91 91 85 IN-AP1 84 89 85 86 89 90 90 88 90 87 86 86 88 90 IN-AP2 82 86 83 85 86 87 87 86 87 84 83 83 86 84 IN-TN1 85 89 85 87 89 90 90 88 89 86 86 86 88 83 IN-TN2 90 94 90 92 94 95 96 94 95 92 92 92 94 90 IN-KE 83 89 85 86 89 89 89 87 89 85 85 85 87 90 IN-KA1 84 88 84 86 88 88 89 88 89 85 85 85 87 90 IN-KA2 91 95 91 93 95 97 97 95 98 93 92 92 95 92 IN-PU-S 91 96 93 94 95 94 94 98 93 95 94 95 96 90 IN-PU-M 91 96 93 94 95 94 94 98 93 95 94 95 96 90 VN-P24 87 92 90 90 92 90 90 90 89 90 90 90 91 90 Asia ID-1 87 91 89 89 91 91 90 91 91 90 90 89 90 88 ( other PH 84 89 87 87 89 87 87 88 87 87 87 87 87 85 than TW-YK 89 94 91 92 93 92 94 93 92 91 92 93 93 90 India) CH1-HN 90 92 91 91 92 92 92 92 91 91 90 91 92 88 CH2-LM 90 93 91 91 93 92 93 93 92 91 91 92 93 90 TH 89 93 92 91 93 92 92 92 91 91 91 92 92 89 Page | 40 Results and Discussion JP-S 90 94 92 93 94 93 93 94 92 93 92 93 94 90 MN-P 86 89 87 87 89 87 87 87 87 85 87 87 87 85 NP-Ne2 85 90 86 89 90 88 90 89 88 88 90 90 90 93 BD 87 91 89 90 91 91 90 91 91 89 90 90 91 89 SL 87 90 88 89 90 89 90 90 89 88 87 88 90 86 MY-M185P 89 93 91 91 93 92 92 93 91 91 91 92 92 89 Australia AU-BD 89 92 90 91 92 91 91 91 91 91 90 91 91 89 Cu-MT1 89 93 91 93 92 92 92 92 91 91 91 91 92 89 BR-PA1 89 93 91 92 93 92 92 93 92 91 92 92 93 90 US-HA 91 95 93 94 95 94 94 94 93 94 94 94 95 92 US-FL 91 95 93 93 95 93 93 94 93 93 93 93 94 91 America CO 88 92 90 91 92 91 91 92 91 90 91 91 92 89 MX-VrAl 89 93 91 92 92 92 92 93 91 92 91 91 93 90 VE-T 87 91 89 90 90 89 89 90 89 89 89 89 90 87 JM-FS 84 88 86 87 87 87 87 87 86 85 86 86 87 86 Table 4.3: Summary of coat protein (CP) gene identity (percent minimum – maximum) at amino acid (diagonally lower values in blue) and nucleotide (diagonally upper values in yellow) levels between PRSV-P isolates from India and other countries.
Recommended publications
  • 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

    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.
  • Etude Des Sources De Carbone Et D'énergie Pour La Synthèse Des Lipides De Stockage Chez La Microalgue Verte Modèle Chlamydo

    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.
  • Lecture Inhibition of Photosynthesis Inhibition at Photosystem I

    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

    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.
  • Can Ferredoxin and Ferredoxin NADP(H) Oxidoreductase Determine the Fate of Photosynthetic Electrons?

    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.
  • Itraq-Based Proteome Profiling Revealed the Role of Phytochrome A

    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

    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
  • Supplementary Material Title Comparative Proteomic Analysis Of

    Supplementary Material Title Comparative Proteomic Analysis Of

    Supplementary Material Title Comparative proteomic analysis of wild-type Physcomitrella patens and an OPDA-deficient Physcomitrella patens mutant with disrupted PpAOS1 and PpAOS2 genes after wounding Authors Weifeng Luoa, Setsuko Komatsub, Tatsuya Abea, Hideyuki Matsuuraa, and Kosaku Takahashia,c* Affiliations aResearch Faculty of Agriculture, Hokkaido University, Sapporo 606-8589, Japan bDepartment of Environmental and Food Sciences, Faculty of Environmental and Information Sciences, Fukui University of Technology, 3-6-1 Gakuen, Fukui 910-8505, Japan cDepartment of Nutritional Science, Faculty of Applied BioScience, Tokyo University of Agriculture, Tokyo 165-8502, Japan. *To whom correspondence should be addressed: Tel.: +81-3-5477-2679; E-mail: [email protected]. Supplementary Fig. S1. Fig. S1. Disruption of PpAOS1 and PpAOS2 genes in P. p a te ns . A, Genomic structures of PpAOS1 and PpAOS2 in the wild-type and targeted PpAOS1 and PpAOS2 knock-out mutants (A5, A19, and A22). The npt II and aph IV expression cassettes were inserted in A5, A19, and A22 strains. B, Genomic PCR data of wild-type, and A5, A19 and A22 strains. P. patens genomic DNA was isolated from protonemata by the CTAB method (Nishiyama et al., Ref. 32). PCR was performed in 50 µL of a reaction mixture containing 1 µL of genomic DNA solution, 1.5 µL of each primer (5 µM), 25 µL of KOD One PCR Master Mix (Toyobo, Japan), and 21 µL of Milli-Q water. PCR was conducted with the following conditions: 30 cycles of 98°C for 10 s, 58°C for 5 s, and 68°C for 15 s.
  • Glycolysis Citric Acid Cycle Oxidative Phosphorylation Calvin Cycle Light

    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
  • How to Build a Water-Splitting Machine: Structural Insights Into Photosystem II Assembly

    How to Build a Water-Splitting Machine: Structural Insights Into Photosystem II Assembly

    bioRxiv preprint doi: https://doi.org/10.1101/2020.09.14.294884; this version posted September 15, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. How to build a water-splitting machine: structural insights into photosystem II assembly Jure Zabret1#, Stefan Bohn2#, Sandra K. Schuller3,4, Oliver Arnolds5, Madeline Möller1, Jakob Meier-Credo6, Pasqual Liauw1, Aaron Chan7, Emad Tajkhorshid7, Julian D. Langer6,8, Raphael Stoll5, Anja Krieger-Liszkay9, Benjamin D. Engel2,10,11, Till Rudack12,13,*, Jan M. Schuller3,4,*, Marc M. Nowaczyk1,* Affiliations: 1Department of Plant Biochemistry, Faculty of Biology & Biotechnology, Ruhr University Bochum, 44780 Bochum, Germany. 2Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany. 3Department of Structural Cell Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany. 4 SYNMIKRO Research Center, Philipps-University Marburg, 35043 Marburg, Germany. 5Biomolecular Spectroscopy and RUBiospek|NMR, Faculty of Chemistry and Biochemistry, Ruhr-University Bochum, 44780 Bochum, Germany 6Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, 60438 Frankfurt/Main, Germany. 7NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, Department of Biochemistry, and Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 8Max Planck Institute for Brain Research, Max von Laue Strasse 4, 60438 Frankfurt/Main, Germany. 9Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198, Gif-sur-Yvette, France 10Helmholtz Pioneer Campus, Helmholtz Zentrum München, Ingolstädter Landstraße 1, 85764 Neuherberg, Germany. 11Department of Chemistry, Technical University of Munich, Lichtenbergstraße 4, 85748 Garching, Germany.
  • Structure of the Cytochrome B6 F Complex of Oxygenic Photosynthesis

    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.
  • The Structure of Photosystem II and the Mechanism of Water Oxidation in Photosynthesis

    The Structure of Photosystem II and the Mechanism of Water Oxidation in Photosynthesis

    PP66CH02-Shen ARI 23 March 2015 13:26 The Structure of Photosystem II and the Mechanism of Water Oxidation in Photosynthesis Jian-Ren Shen Photosynthesis Research Center, Graduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, Japan; email: [email protected] Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China Annu. Rev. Plant Biol. 2015. 66:23–48 Keywords First published online as a Review in Advance on crystal structure, membrane proteins, oxygen evolution, photosynthesis, February 26, 2015 photosystem II, S state, water splitting The Annual Review of Plant Biology is online at plant.annualreviews.org Abstract This article’s doi: Oxygenic photosynthesis forms the basis of aerobic life on earth by con- 10.1146/annurev-arplant-050312-120129 verting light energy into biologically useful chemical energy and by split- Access provided by CAPES on 04/20/18. For personal use only. Copyright c 2015 by Annual Reviews. ting water to generate molecular oxygen. The water-splitting and oxygen- All rights reserved evolving reaction is catalyzed by photosystem II (PSII), a huge, multisubunit Annu. Rev. Plant Biol. 2015.66:23-48. Downloaded from www.annualreviews.org membrane-protein complex located in the thylakoid membranes of organ- isms ranging from cyanobacteria to higher plants. The structure of PSII has been analyzed at 1.9-A˚ resolution by X-ray crystallography, revealing a clear picture of the Mn4CaO5 cluster, the catalytic center for water oxidation. This article provides an overview of the overall structure of PSII followed by detailed descriptions of the specific structure of the Mn4CaO5 cluster and its surrounding protein environment.