Single-Letter Codes for Amino Acids
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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. -
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. -
Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases
International Journal of Molecular Sciences Review Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases Peter Goettig Structural Biology Group, Faculty of Molecular Biology, University of Salzburg, Billrothstrasse 11, 5020 Salzburg, Austria; [email protected]; Tel.: +43-662-8044-7283; Fax: +43-662-8044-7209 Academic Editor: Cheorl-Ho Kim Received: 30 July 2016; Accepted: 10 November 2016; Published: 25 November 2016 Abstract: Posttranslational modifications are an important feature of most proteases in higher organisms, such as the conversion of inactive zymogens into active proteases. To date, little information is available on the role of glycosylation and functional implications for secreted proteases. Besides a stabilizing effect and protection against proteolysis, several proteases show a significant influence of glycosylation on the catalytic activity. Glycans can alter the substrate recognition, the specificity and binding affinity, as well as the turnover rates. However, there is currently no known general pattern, since glycosylation can have both stimulating and inhibiting effects on activity. Thus, a comparative analysis of individual cases with sufficient enzyme kinetic and structural data is a first approach to describe mechanistic principles that govern the effects of glycosylation on the function of proteases. The understanding of glycan functions becomes highly significant in proteomic and glycomic studies, which demonstrated that cancer-associated proteases, such as kallikrein-related peptidase 3, exhibit strongly altered glycosylation patterns in pathological cases. Such findings can contribute to a variety of future biomedical applications. Keywords: secreted protease; sequon; N-glycosylation; O-glycosylation; core glycan; enzyme kinetics; substrate recognition; flexible loops; Michaelis constant; turnover number 1. -
Serine Proteases with Altered Sensitivity to Activity-Modulating
(19) & (11) EP 2 045 321 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 08.04.2009 Bulletin 2009/15 C12N 9/00 (2006.01) C12N 15/00 (2006.01) C12Q 1/37 (2006.01) (21) Application number: 09150549.5 (22) Date of filing: 26.05.2006 (84) Designated Contracting States: • Haupts, Ulrich AT BE BG CH CY CZ DE DK EE ES FI FR GB GR 51519 Odenthal (DE) HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI • Coco, Wayne SK TR 50737 Köln (DE) •Tebbe, Jan (30) Priority: 27.05.2005 EP 05104543 50733 Köln (DE) • Votsmeier, Christian (62) Document number(s) of the earlier application(s) in 50259 Pulheim (DE) accordance with Art. 76 EPC: • Scheidig, Andreas 06763303.2 / 1 883 696 50823 Köln (DE) (71) Applicant: Direvo Biotech AG (74) Representative: von Kreisler Selting Werner 50829 Köln (DE) Patentanwälte P.O. Box 10 22 41 (72) Inventors: 50462 Köln (DE) • Koltermann, André 82057 Icking (DE) Remarks: • Kettling, Ulrich This application was filed on 14-01-2009 as a 81477 München (DE) divisional application to the application mentioned under INID code 62. (54) Serine proteases with altered sensitivity to activity-modulating substances (57) The present invention provides variants of ser- screening of the library in the presence of one or several ine proteases of the S1 class with altered sensitivity to activity-modulating substances, selection of variants with one or more activity-modulating substances. A method altered sensitivity to one or several activity-modulating for the generation of such proteases is disclosed, com- substances and isolation of those polynucleotide se- prising the provision of a protease library encoding poly- quences that encode for the selected variants. -
(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 -
And SPP-Like Proteases☆
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Biochimica et Biophysica Acta 1828 (2013) 2828–2839 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbamem Review Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases☆ Matthias Voss a, Bernd Schröder c, Regina Fluhrer a,b,⁎ a Adolf Butenandt Institute for Biochemistry, Ludwig-Maximilians University Munich, Schillerstr. 44, 80336 Munich, Germany b DZNE — German Center for Neurodegenerative Diseases, Munich, Schillerstr. 44, 80336 Munich, Germany c Biochemical Institute, Christian-Albrechts-University Kiel, Olshausenstrasse 40, 24118 Kiel, Germany article info abstract Article history: Signal peptide peptidase (SPP) and the homologous SPP-like (SPPL) proteases SPPL2a, SPPL2b, SPPL2c and Received 27 December 2012 SPPL3 belong to the family of GxGD intramembrane proteases. SPP/SPPLs selectively cleave transmembrane Received in revised form 25 March 2013 domains in type II orientation and do not require additional co-factors for proteolytic activity. Orthologues of Accepted 29 March 2013 SPP and SPPLs have been identified in other vertebrates, plants, and eukaryotes. In line with their diverse subcellular localisations ranging from the ER (SPP, SPPL2c), the Golgi (SPPL3), the plasma membrane Keywords: (SPPL2b) to lysosomes/late endosomes (SPPL2a), the different members of the SPP/SPPL family seem to Regulated intramembrane proteolysis fi Intramembrane-cleaving proteases exhibit distinct functions. Here, we review the substrates of these proteases identi ed to date as well as GxGD proteases the current state of knowledge about the physiological implications of these proteolytic events as deduced Signal peptide peptidase from in vivo studies. -
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. -
Supplementary Data
Supplementary Fig. 1 A B Responder_Xenograft_ Responder_Xenograft_ NON- NON- Lu7336, Vehicle vs Lu7466, Vehicle vs Responder_Xenograft_ Responder_Xenograft_ Sagopilone, Welch- Sagopilone, Welch- Lu7187, Vehicle vs Lu7406, Vehicle vs Test: 638 Test: 600 Sagopilone, Welch- Sagopilone, Welch- Test: 468 Test: 482 Responder_Xenograft_ NON- Lu7860, Vehicle vs Responder_Xenograft_ Sagopilone, Welch - Lu7558, Vehicle vs Test: 605 Sagopilone, Welch- Test: 333 Supplementary Fig. 2 Supplementary Fig. 3 Supplementary Figure S1. Venn diagrams comparing probe sets regulated by Sagopilone treatment (10mg/kg for 24h) between individual models (Welsh Test ellipse p-value<0.001 or 5-fold change). A Sagopilone responder models, B Sagopilone non-responder models. Supplementary Figure S2. Pathway analysis of genes regulated by Sagopilone treatment in responder xenograft models 24h after Sagopilone treatment by GeneGo Metacore; the most significant pathway map representing cell cycle/spindle assembly and chromosome separation is shown, genes upregulated by Sagopilone treatment are marked with red thermometers. Supplementary Figure S3. GeneGo Metacore pathway analysis of genes differentially expressed between Sagopilone Responder and Non-Responder models displaying –log(p-Values) of most significant pathway maps. Supplementary Tables Supplementary Table 1. Response and activity in 22 non-small-cell lung cancer (NSCLC) xenograft models after treatment with Sagopilone and other cytotoxic agents commonly used in the management of NSCLC Tumor Model Response type -
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 -
Plant Signaling Peptides, Novel Insights Into Their Processing and Role in Root Development
Plant signaling peptides, novel insights into their processing and role in root development Sarieh Ghorbani 2014 Cover: GLV10 expression pattern during lateral root primordia development To my wonderful parents, Samarrokh and Bohloul ی ن هم ه ثم بهل تقد م هب مهربای اه و را ی اهی پدر و مارد زعزیم، ررخ و ول يک چند هب کودکی هب استاد شدیم يک چند هب استادی خود شاد شدیم سخ اپيان ن شنو هک ما را هچ رسيد از خاک رب آدمیم و رب باد شدیم حکیم عمر خیام Myself, when young did eagerly frequent Doctor and Saint, and heard great Argument About it and about: but evermore Came out by the same Door where in I went. Omar Khayyam (Persian poet, mathematician, astronomer, 1048 –1131) (translated by Edward FitzGerald) Ghent University Faculty of Sciences Department of Plant Biotechnology and Bioinformatics Plant signaling peptides, novel insights into their processing and role in root development Sarieh Ghorbani Promoters: Prof. Dr. Tom Beeckman and Dr. Pierre Hilson April 2014 VIB – Plant Systems Biology Thesis submitted in partial fulfillment of the requirements for the degree of Doctor of Science: Biochemistry and Biotechnology Promoters: Prof. Dr. Tom Beeckman Department of Plant Systems Biology, VIB and Department of Plant Biotechnology and Bioinformatics, Ghent University [email protected] Dr. Pierre Hilson Institut Jean-Pierre Bourgin, UMR1318 INRA-AgroParisTech, Versailles Cedex, France [email protected] Examination commission: Prof. Dr. Ann Depicker (Chair) Department of Plant Systems Biology, VIB and Department of Plant Biotechnology and Bioinformatics, Ghent University [email protected] Prof. Dr.