GTL PI Meeting 2003 PNNL Poster

Total Page:16

File Type:pdf, Size:1020Kb

GTL PI Meeting 2003 PNNL Poster PNNL Protein Complex Characterization Efforts Richard D. Smith, Joshua N. Adkins, Gordon A. Anderson, Deanna L. Auberry, Yuri A. Gorby, Eric A. Hill, Kim K. Hixson, Chiann-Tso Lin, Mary S. Lipton, Lye Meng Markillie, Uljana Mayer, Matthew E. Monroe, Ronald J. Moore, Sewite Negash, Ljiljana Paša-Tolić, Liang Shi, David L. Springer, Thomas C. Squier, Eric F. Strittmatter, Keqi Tang, and Nikola Tolić Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352 Himadri B. Pakrasi, Department of Biology, Washington University, St. Louis, MO 63130 Identifying protein complexes using Higher characterization throughput at lower cost AM T tags A component of the PNNL program is to develop an approach that provides both increased confidence, higher P rotein synthesis Nucleoba se synthesis 96% 97% Am ino acid biosynthesis throughput, and a quanti tati ve tool for characterizing protei n complexes. We have ini ti all y expl ored the utili ty of The database of Shew anell a accurate mass and time (AMT) 96% Othe r categories Transcription 94% 40% characterizing protein complexes at the peptide level using AMT tags with Q-TOF instrumentation as an alternative tags provi des the basi s for hi gh throughput characteri zati on of Cen tral intermediar y metabolism 94% to much less sensitive and lower throughput approaches based upon tandem MS (e.g., using ion trap mass protein complexes at either the peptide level or intact protein Ener gy metabolism 94% Prot ein fate spectrometers) or more expensive FTICR instrumentation that is needed for much more demanding “whole level. The intact protein level analysis is enabled by the Fa tty acid and phospholipid peptide level approach (by providing their initial me tabolism 94% proteome” analyses. T ransport and binding pr oteins 93% identifications) and also complements the information Cov erage This initial evaluation examined the highly active oxygen-evolving photosystem II (PSII) complex purified from the Hypothetical pro teins DNA metab olism 9 3% obtainable at the peptide-level with additional information on65% HT-3 strain of the cyanobacterium Synechocystis sp. PCC 6803. This initial study used high pressure capillary LC- protein modifications (e.g., chemical modifications, protein Regulator y functions 93% Q-TOF instrumentation and used AMT tags that were generated from capillary LC-MS/MS analyses. The table truncation). Regardless, the use of AMT tags can greatly Cell envelope 93% below shows a partial listing of >120 proteins that were identified, along with a measure of their relative abundances speed the analysis and potentially allows characterization S ignal transdu ction 92% based upon the integrated peak intensities for the corresponding peptides. The proteins highlighted in yellow were Cellular pro cesses times of <5 minutes per complex. Proteome coverage by 91% previously identified by Pakrasi and coworkers (Kashino et al., Biochemistry 2002, 41, 8004 – 8012). All proteins B iosynthesis of cofactors Unknown function 90 % AMT tags is indicated by the pie chart (right). 90 % that were assi gned based upon more than one peptide are done so wi th very hi gh confidence. Value-added protein complex characterization at the intact protein Mass Tag Average Approx. Reference Description Descr iption fr om fromFASTA FASTAGene GeneCount Ab un Count da nc e otherwise) AbundaSLR0906 ncephotosystem MW II core light harvesting protein psbB 26 23386 45 00 0 level – initial demonstration SL L1 13 0 unknown protein 7 2 31 13 10 00 0 SL L1 63 8 hypothetical protein psbQ 12 14362 11 00 0 T he se re su l ts sh o w: SLR0144 hypothetical protein 4 1 36 78 24 00 8 To evaluate our approach, we have initially studied the well characterized yeast large ribosomal SL L0 42 7 photosystem II manganese-stabiliz ing polype ptide ps bO 19 12461 31 00 0 • Q-TOF instrumentation augmented SL L0 25 8 c yt o ch r o me c5 50 p s bV 11 11983 16 00 0 SL L1 41 8 s imilar to p ho to syst em I I o xyg en - evo lvin g comp le x 2 3K pr ote in Psb P p sb P 2 78 78 16 82 8 subunit. The 43 proteins in this complex were previously identified at the peptide level using tandem SL L1 39 0 hypothetical protein 7721321 00 0 by the use of LC elution time SLR1181 photosystem II D1 protein psbA1 4 7098 32161 MS, providing an expected set of tentative molecular weights. The constrained level of complexity SL L1 09 9 e lo ng atio n fa cto r T u tu fA 22 67 91 35 47 2 information provides sufficient SL L1 19 4 photosystem II 12 kDa extrinsic protein psbU 12 67 41 10 00 0 associated with most protein complexes (ignoring obviously low-level contaminants) allows the SLR0172 hypothetical protein guaB 3667515 00 0 specificity for application of AMT tag SSR0692 hypothetical protein 3 6445 4746 detected masses to be assigned to the various proteins, as well as (in most cases) assignment of SL L0 85 1 photosystem II CP43 protein psbC 22 62 67 34 00 0 approaches. SLR1604 cell division protein FtsH ftsH 21 61 82 57 00 0 their modification states. SL L1 41 4 hypothetical protein 7617724 00 0 SL R0 01 2 r ib ulo se bis ph os ph at e c ar bo xyla se sm a ll s ub un it r bc S 4 61 58 10 73 8 • The AMT tag approach with SLR1051 enoyl acyl-carrier-protein 7 6001 22407 Partial 2-D display SSL0426 putative transposase ISY100_t 1 5806 8867 LC-Q-TOF analysis provides SLR0228 cell division protein FtsH ftsH 19 56 46 59 00 0 Capillary LC-FTICR of SML0007 photosystem II protein Y psbY 1549236 00 suffi cient speci fi city for protei n L6B SL L1 86 7 photosystem II D1 protein psbA3 6548327 00 0 yeast ribo somal comp lex L6A SLR1311 photosystem II D1 protein psbA2 6548327 00 0 L17AB Acetylated SL L1 39 8 photosystem II reaction center W protein (Psb28 b?) psbW, psb13, ycf79 5527710 00 0 complex characterization, along with L14B SLR1128 hypothetical protein 14 50 96 28 97 8 Acetylated SL L1 02 9 c ar bo n dio xid e con ce nt ra tin g m e ch an ism p r ote in Ccm K cc m K 5 49 95 98 16 high throughput, and preliminary Acetylated L14A SL L0 84 9 photosystem II reaction center D2 protein psbD 9475329 00 0 L11A/B L25 L28 SLR0927 photosystem II reaction center D2 protein psbD2 9 47 53 29 00 0 quantitation. L35AB L32 SLR1622 soluble inorganic pyrophosphatase ppa 6 4707 15482 SLR0151 unknown protein 13 46 93 28 32 0 SLL1694 pilin polypeptide PilA1 pilA1 2 4478 14254 • The use of quantitative information Methylated SL R0 00 9 r ib ulo se bis ph os ph at e c ar bo xyla se la rg e sub u nit r bc L 11 43 37 42 57 6 Mass L23 L31A/B SL L1 46 3 c ell divis ion p ro te in F t sH ft sH 21 42 20 55 31 7 and multiple analyses (e.g., using L38 SL L1 54 5 g lu tat hio ne S- tr an sfe ra se 8 4113 24143 L36A/B SSL2245 unknown protein 1 4087 7467 SLL1106 hypothetical protein 5 3985 14625 di fferent wash condi ti ons) wi ll be SLR0670 hypothetical protein 11 39 72 26 50 4 SLL1543 hypothetical protein 1 3921 13433 needed with this approach to better SLR1645 photosystem II 11 kD protein (Psb27 b?) psbZ 7378191 00 0 200 400 600 800 1000 1200 1400 SLR1165 sulfate adenylyltransferase 13 37 24 35 44 2 qualify which proteins are part of the SMR0007 photosystem II PsbL protein psbL 1368046 00 Spectrum Number SSL 25 98 photosystem II PsbH proteinpsbH 3360957 00 complex in contrast to being non- SLR1855 unknown protein 20 34 92 56 78 0 SSR 34 51 cytochrome b559 alpha subunit psbE 3332378 00 specifically associated. SLR0752 enolase 13 28 77 37 74 0 Large Riboso mal Su bu nit Coverage by In tact Prot ein An alysis Spectrum number SLR1218 hypothetical protein YCF39 ycf39 1 2874 14339 SL L1 02 8 c ar bo n dio xid e con ce nt ra tin g m e ch an ism p r ote in Ccm K cc m K 5 28 69 90 31 SLL1212 GDP-mannose 4,6-dehydratase 5 2866 33526 rpL1 rpL2 rpL3 rpL4 rpL5 rpL6 rp L7 rpL8 rpL9 rpL10 SLL1835 hypothetical protein 2 2852 23386 AB AB A/B A/B A/B A/B A/ B SL L0 08 0 N -a ce tyl- ga m m a- glu ta m yl-p ho sp ha te r ed uc tas e a rg C 6 28 42 30 99 2 Ac & 1 Me 1 Me Ac SLL0680 phosphate-binding periplasmic protein precursor (PBP) 10 2770 32463 Loss of Met Lo ss of Met Loss of Met Lo ss o f Me t Lo ss of M et L os s o f Me t Loss o f M et L os s of M et L os s of M et Advantages of intact protein proteomics: SSL1498 hypothetical protein 2 2728 5191 rpL11 rpL12 rpL13 rpL14 rpL15 rpL16 rp L1 7 rpL18 rpL19 rpL20 SLR0149 hypothetical protein 5 2717 14913 A/B AB A/B A/B AB A/B A/B AB AB A/B SLR1619 hypothetical protein 3 2716 22510 Ac 6 Me Ac Ac • Augments pepti de level anal yses SL L1 45 0 n itr at e/n itr ite tr an sp or t s yste m s ub str at e- bin din g pr ot ein n rt A 13 26 78 39 71 7 Loss of Met Lo ss of M et Lo ss o f M et L os s of M et Lo ss of Met Loss of Met Lo ss of Met Lo ss o f Me t Loss of Me t SLL1654 hypothetical protein 1 2430 11805 rpL21 rpL22 rpL23 rpL24 rpL25 rpL26 rp L2 7 rpL28 rpL29 rpL30 SL L1 04 3 p o lyrib on uc leo tid e nu cleo tid yltr an sf er as e 18 24 14 63 13 0 A/B A/B AB A/B A/B A/B • L e ss co m pl e xi ty SLR0476 unknown protein 1 2405 11675 Ac & 4 Me SL L1 85 2 nucleo side diphosphate kinase 3 22 97 13 53 9 Loss of Met Loss of Met Loss of Met Lo ss of M et L os s o f Me t Loss of Met Loss of Met Loss of M et L os s of M et rpL31 rpL32 rpL33 rpL34 rpL35 rpL36 rp L3 7 rpL38 rpL39 rpL40 SL R1 21 6 M g 2+ t ra ns po rt pr ot ein 5 2280 41448 A/B A/B A/B AB A/B A/B AB • Much more information on protein SL L1 55 5 t wo -co m po n en t h ybr id se ns or a nd re g ula tor 4 22 59 33 63 9 SLL1641 glutamate de ca rboxylase 4215143022 Lo ss of Met Loss o f Met L os s of Met Lo ss o f Met Loss of Me t L os s o fMe t Loss o f M et L os s of M et Lo ss of Met Fragment, 77- 1 28 modification states SLR0723 hypothetical protein 5 2128 33603 rpL41 rpL42 rpL43 SLR1618 unknown protein 3 2123 23523 AB AB AB • 42 of the 43 core l arge ribosomal subunit proteins (58 of SLL0290 polyphosphate kinase ppk 13 2115 67003 2 Me 1 Me the 64 possible core larg e subunit pro tein iso forms) are • Potenti all y more quanti tati ve, faster, and SL L0 01 8 f ru cto se -b isp ho sp ha te a ldo las e, cla ss II fb a A, f da 8 21 01 31 61 0 Lo ss of Met Lo ss of Met i den ti fied in a si ngl e an aly sis.
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 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.
    [Show full text]
  • 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.
    [Show full text]
  • (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
    [Show full text]
  • 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.
    [Show full text]
  • 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
    [Show full text]
  • 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.
    [Show full text]
  • 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
    [Show full text]
  • 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.
    [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]
  • 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.
    [Show full text]
  • Faculty Publications and Presentations 2011-12
    UNIVERSITY OF ARKANSAS FAYETTEVILLE, ARKANSAS PUBLICATIONS & PRESENTATIONS JULY 1, 2011 – JUNE 30, 2012 Revision A Table of Contents Bumpers College of Agricultural, Food and Life Sciences………………………………….. Page 3 Fay Jones School of Architecture…………………………………………..………………... Page 94 Fulbright College of Arts and Sciences………………………………………………………. Page 102 Sam M. Walton College of Business ……..………………………………………………….. Page 259 College of Education and Health Professions………………………………………………… Page 275 College of Engineering………………………………………………………………………... Page 303 School of Law…………………………………………………………………………………. Page 353 University Libraries………………………………………………….………………………… Page 360 DALE BUMPERS SCHOOL OF AGRICULTURE Peer-reviewed publications or juried event Agricultural Economics and Agricultural Business Ahrendsen, Bruce L., Dixon, B. L., Settlage, L. A., Koenig, S. R. and Dodson, C. B. 2011. “A triple hurdle model of us commercial bank use of guaranteed operating loans and interest assistance.” Agricultural Finance Review 71,3:310-328. Akaichi, F., Gil, J. and Nayga, Jr., R. M. 2011. “Bid Affiliation in repeated random nth price auction.” Spanish Journal of Agricultural Research. 9,1:22-27. Akaichi, F., Gil, J. and Nayga, Jr., R. M. 2012. “Assessing the market potential for local food product: evidence from a non-hypothetical economic experiment.” British Food Journal. Vol 114, Issue 1. http://www.emeraldinsight.com/journals.htm?issn=0007-070X&show=latest Campbell, B., Nayga, Jr., R. M., Park, J. and Silva, A. 2011. “Does the national school lunch program improve children’s dietary outcomes?” American Journal of Agricultural Economics, 93,4:1099-1130. Doi: 10,1093/ajae/aar031 Chang, H.-H. and Nayga, Jr., R. M. 2011. “Mother’s nutritional label use and children’s body weight.” Food Policy 36:171-178.
    [Show full text]
  • Adjustments of Photosystem Stoichiometry in Chloroplasts
    Proc. Natl. Acad. Sci. USA Vol. 87, pp. 7502-7506, October 1990 Botany Adjustments of photosystem stoichiometry in chloroplasts improve the quantum efficiency of photosynthesis (thylakoids/chloroplast acclimation/reaction center/quantum yield/light quality) WAH SOON CHOW*t, ANASTASIOS MELISt, AND JAN M. ANDERSON* *Commonwealth Scientific and Industrial Organisation, Division of Plant Industry, G.P.O. Box 1600, Canberra, Australian Capital Territory 2601, Australia; and *Department of Plant Biology, University of California, Berkeley, CA 94720 Communicated by Daniel L. Arnon, July 3, 1990 ABSTRACT The efficiency of photosynthetic electron apparatus, given the contrasting light environments in differ- transport depends on the coordinated interaction of photosys- ent plant ecosystems (6-8) and the fact that substantially tem II (PSH) and photosystem I (PSI) in the electron-transport different pigments absorb light for PSI and for PSII in the chain. Each photosystem contains distinct pigment-protein thylakoid membrane of oxygenic photosynthesis. complexes that harvest lightfrom different regions ofthe visible These findings suggested that higher plants and algae spectrum. The light energy is utilized in an endergonic electron- possess regulatory mechanisms that enable chloroplasts to transport reaction at each photosystem. Recent evidence has adjust and optimize the function of the light reactions under shown a large variability in the PSI/PSI stoichiometry in diverse conditions. Recently, evidence in the literature sug- plants grown under different environmental irradiance condi- gested long-term adjustments in photosystem stoichiometry tions. Results in this work are consistent with the notion of a as a plant response to different light-quality conditions during dynamic, rather than static, thylakoid membrane in which the stoichiometry of the two photosystems is adjusted and opti- growth (9, 10).
    [Show full text]