Transport Proteins Enabling Plant Photorespiratory Metabolism
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ADHERENCE and ALKALINIZATION by Elizabeth Hwang
TWO EARLY PROCESSES DURING INFECTION BY THE FUNGAL PATHOGEN CANDIDA GLABRATA: ADHERENCE AND ALKALINIZATION By Elizabeth Hwang-Wong A dissertation submitted to Johns Hopkins University in conformity with the requirements for the degree of Doctor of Philosophy Baltimore, Maryland November, 2016 Abstract Candida glabrata is a yeast pathogen of increasing diagnostic incidence. Its intrinsic resistance to antifungal agents used in standard clinical settings compels a need to further characterize and understand the pathogenesis of this species. The ability of C. glabrata to adhere to both abiotic surfaces and host cells is an essential early step in establishment of infection. It is also postulated that the capability of this pathogen to externally alkalinize an acidic environment, such as that found within an immune effector’s phagolysosome, could provide an evasive mechanism to resist initial onslaught of an innate immune response. Members of a major class of adhesins encoded by the C. glabrata genome were previously described as Epithelial Adhesins (Epas). Earlier studies have demonstrated the existence of more than 20 members of this class, many of which are encoded in subtelomeric regions of the pathogen’s genome. A major sequencing project has now defined a total complement of 25 members, a newly described one of which is shown to function as a major adhesin across multiple host cell types. In fact, functional adherence of all putative adhesins encoded in the subtelomeres of C. glabrata has been tested, and with minor exception, all are EPAs. The ligand specificities of these functional adhesins were further tested utilizing glycan arrays, and revealed clues identifying a specific EPA responsible for mediating adherence to macrophages. -
Bioinorganic Chemistry Content
Bioinorganic Chemistry Content 1. What is bioinorganic chemistry? 2. Evolution of elements 3. Elements and molecules of life 4. Phylogeny 5. Metals in biochemistry 6. Ligands in biochemistry 7. Principals of coordination chemistry 8. Properties of bio molecules 9. Biochemistry of main group elements 10. Biochemistry of transition metals 11. Biochemistry of lanthanides and actinides 12. Modell complexes 13. Analytical methods in bioinorganic 14. Applications areas of bioinorganic chemistry "Simplicity is the ultimate sophistication" Leonardo Da Vinci Bioinorganic Chemistry Slide 1 Prof. Dr. Thomas Jüstel Literature • C. Elschenbroich, A. Salzer, Organometallchemie, 2. Auflage, Teubner, 1988 • S.J. Lippard, J.N. Berg, Bioinorganic Chemistry, Spektrum Akademischer Verlag, 1995 • J.E. Huheey, E. Keiter, R. Keiter, Anorganische Chemie – Prinzipien von Struktur und Reaktivität, 3. Auflage, Walter de Gruyter, 2003 • W. Kaim, B. Schwederski: Bioinorganic Chemistry, 4. Auflage, Vieweg-Teubner, 2005 • H. Rauchfuß, Chemische Evolution und der Ursprung des Lebens, Springer, 2005 • A.F. Hollemann, N. Wiberg, Lehrbuch der Anorganischen Chemie, 102. Auflage, de Gruyter, 2007 • I. Bertini, H.B. Gray, E.I. Stiefel, J.S. Valentine, Biological Chemistry, University Science Books, 2007 • N. Metzler-Nolte, U. Schatzschneier, Bioinorganic Chemistry: A Practical Course, Walter de Gruyter, 2009 • W. Ternes, Biochemie der Elemente, Springer, 2013 • D. Rabinovich, Bioinorganic Chemistry, Walter de Gruyter, 2020 Bioinorganic Chemistry Slide 2 Prof. Dr. Thomas Jüstel 1. What is Bioinorganic Chemistry? A Highly Interdisciplinary Science at the Verge of Biology, Chemistry, Physics, and Medicine Biochemistry Inorganic Chemistry (Micro)- Physics & Biology Spectroscopy Bioinorganic Chemistry Pharmacy & Medicine & Toxicology Physiology Diagnostics Bioinorganic Chemistry Slide 3 Prof. Dr. Thomas Jüstel 2. Evolution of the Elements Most Abundant Elements in the Universe According to Atomic Fraction Are: 1. -
Interdependence Between Chloroplasts and Mitochondria in the Light and the Dark
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Biochimica et Biophysica Acta 1366 (1998) 235^255 Review Interdependence between chloroplasts and mitochondria in the light and the dark Marcel H.N. Hoefnagel a, Owen K. Atkin b, Joseph T. Wiskich a;* a Department of Botany, University of Adelaide, Adelaide, SA 5005, Australia b Research School for Biological Sciences, Australian National University, Canberra, ACT 0200, Australia Received 21 April 1998; revised 3 June 1998; accepted 10 June 1998 ß 1998 Elsevier Science B.V. All rights reserved. Keywords: Chloroplast; Chlororespiration; Excess reductant; Metabolite exchange; Mitochondrion; Photosynthesis; Respiration Contents 1. Introduction .......................................................... 236 2. Interactions between organelles depends on metabolite exchange . .................. 236 2.1. ATP exchange ..................................................... 236 2.2. Transport of reducing equivalents across membranes . ....................... 237 2.3. Exchange of carbon compounds ....................................... 238 3. Respiration in the light . ................................................. 239 3.1. Does respiration continue in the light? . .................................. 239 3.2. Substrates for the mitochondria in the light . ............................ 240 3.3. ATP supply in the light: chloroplasts versus mitochondria . .................. 240 3.4. Adenylate control of respiration in the light . -
Membrane Protein Production for Structural Analysis
Chapter 1 Membrane Protein Production for Structural Analysis Isabelle Mus-Veteau, Pascal Demange and Francesca Zito 1.1 Introduction Integral membrane proteins (IMPs) account for roughly 30 % of all open reading frames in fully sequenced genomes (Liu and Rost 2001). These proteins are of main importance to living cells. They are involved in fundamental biological processes like ion, water, or solute transport, sensing changes in the cellular environment, signal transduction, and control of cell–cell contacts required to maintain cellular homeostasis and to ensure coordinated cellular activity in all organisms. IMP dys- functions are responsible for numerous pathologies like cancer, cystic fibrosis, epi- lepsy, hyperinsulinism, heart failure, hypertension, and Alzheimer diseases. How- ever, studies on these and other disorders are hampered by a lack of information about the involved IMPs. Thus, knowing the structure of IMPs and understanding their molecular mechanism not only is of fundamental biological interest but also holds great potential for enhancing human health. This is of paramount importance in the pharmaceutical industry, which produces many drugs that bind to IMPs, and recognizes the potential of many recently identified G-protein-coupled receptors (GPCRs), ion channels, and transporters, as targets for future drugs. GPCR, which account for 50 % of all drug targets, is one of the largest and most diverse IMP families encoded by more than 800 genes in the human genome (Fredriksson et al. 2003; Lundstrom 2006). However, whereas high-resolution structures are avail- able for a myriad of soluble proteins (more than 42,000 in the Protein Data Bank, I. Mus-Veteau () Institute for Molecular and Cellular Pharmacology, UMR-CNRS 7275, University of Nice-Sophia Antipolis, Valbonne, France e-mail: [email protected] P. -
Additional File 10. Transporter Distribution in Hemiascomycete Species
Additional File 10. Transporter distribution in hemiascomycete species Transporters were identified through a two step process on the proteomes of S. cerevisiae, C. glabrata, K. lactis, D. hansenii, K. pastoris, Y. lipolytica and A. adeninivorans: 1) identification of protein products having at least three transmembrane domains using THMM (v2.0; http://www.cbs.dtu.dk/services/TMHMM-2.0), 2) identification of transporters by a Blastp search against the TCDB database16. Table S10A Transporter distribution in hemiascomycete species. Table S10B TCDB classification of transporters of A. adeninivorans. Table S10C Class of transporters amplified in A. adeninivorans compared to two other pre-CTG species. Figure S10D Phylogeny of sugar porters in A. adeninivorans and D. hansenii. 1 Table S10A Transporter distribution in hemiascomycete species Type Subfamily Species code TCDB ARAD YALI PIPA DEHA KLLA CAGL SACE Total TCDB Family 1.A.1.10 1 1 The Voltage-gated Ion Channel (VIC) Family 1.A.1.11 1 1 1 1 1 1 1 7 The Voltage-gated Ion Channel (VIC) Family 1.A.1.5 1 1 The Voltage-gated Ion Channel (VIC) Family 1.A.1.7 1 2 1 1 1 6 The Voltage-gated Ion Channel (VIC) Family 1.A.11.1 1 1 1 1 1 5 The Ammonia Transporter Channel (Amt) Family 1.A.11.2 2 2 4 The Ammonia Transporter Channel (Amt) Family 1.A.11.3 2 3 5 The Ammonia Transporter Channel (Amt) Family 1.A.15.1 1 1 1 1 1 5 The Non-selective Cation Channel-2 (NSCC2) Family 1.A.15.2 1 1 The Non-selective Cation Channel-2 (NSCC2) Family 1.A.16.1 1 1 1 1 1 5 The Yeast Stretch-Activated, Cation-Selective, -
Calvin Cycle E
Photosynthesis Photosynthesis is the process by which plants use sunlight (light energy) to produce glucose from carbon dioxide and water, with oxygen as a byproduct. This process occurs LIGHT STROMA in the chloroplasts in a plant cell and has DEPENDENT Cytochrome b f Reduced REACTIONS two stages – the light-dependent reactions 6 NADP NADP + 1. Light activation of and the light-independent reactions. H ATP synthase photocentres It all starts with the sunlight hitting e- PSII 2. Photolysis of water - + the fi rst photocentre (PSII). (P68 e PSI H e- (P 3. Electron transport e- ATP e- + 4. Pumping H into the + O H thylakoid space ADP + Pi H O + + H 5. Synthesis of ATP H 6. Reduction of NADP Photolysis THYLAKOID SPACE CO OXYGEN Thylakoid membrane GLUCOSE REDUCED NADP & ATP NADP REDUCED Glucose is used in respiration for energy. Glucose is converted to: 1. Cellulose for cell walls 2. Sucrose for transport 3. Starch for storage ADP + Pi & NADP + Pi ADP CHLOROPLAST CALVIN C LIGHT CO YCL E ( Six INDEPENDENT RuBisCO tu rn enzyme BON FIXAT s CAR ION to REACTIONS p ro d u c Calvin cycle e RuBP GP g l 1. Carbon fi xation u Ribulose bisphosphate Glycerate phosphate c o s e ) 2. Reduction P B 3. Regeneration of RuBP u R ATP F ADP + Pi O N ADP + Pi O R I ATP E T D A R Reduced NADP U E C N T E I O G NADP N E R GALP Glyceraldehyde phosphate Hexose Glucose LAMELLA THYLAKOIDS STROMA KEY TO SYMBOLS INNER CHLOROPLAST MEMBRANE Carbon atom: Electron transport: e- OUTER CHLOROPLAST MEMBRANE H+ movement: GLOSSARY ATP synthase: An enzyme that catalyses the Ferrodoxin: An electron carrier sitting just Light-dependent reactions: The fi rst stage Photosystem I (PSI): The second photosystem Plastoquinone: A molecule that is reduced Regeneration of RuBP: The third stage of Stroma: The aqueous solution that fi lls the synthesis of ATP from ADP and inorganic outside the thylakoid in the chloroplast of photosynthesis. -
Supplementary Tables and Figures
SUPPLEMENTARY TABLES AND FIGURES The Complete Genome Sequence of Moorella thermoacetica (f. Clostridium thermoaceticum) Elizabeth Pierce1, Gary Xie2,3, Ravi D. Barabote2,3, Elizabeth Saunders2,3, Cliff S. Han2,3, John C. Detter2,3, Paul Richardson2,4, Thomas S. Brettin2,3, Amaresh Das5, Lars G. Ljungdahl5, and Stephen W. Ragsdale1 1Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan; 2 Los Alamos National Laboratory, Bioscience Division, Los Alamos, New Mexico; 3Department of Energy Joint Genome Institute, Walnut Creek, CA; 4Lawrence Berkeley National Laboratory, Berkeley, CA; 5Department of Biochemistry and Molecular Biology, University of Georgia 1 Supplementary Table 1. Pseudogenes found in the M .thermoacetica genome. Locus Tag Product Name AA Seq Length Remnants Redundance Moth_0037 FAD/FMN-containing 462 early stop codon, 2 paralogs dehydrogenases frameshift Moth_0138 purine-cytosine permease and 417 early stop codon no paralog related proteins Moth_0164 dTDP-4-dehydrorhamnose 283 fragment, frameshift 2 paralogs reductase Moth_0166 glucose-1-phosphate 227 deletion in central region no paralog thymidylyltransferase Moth_0180 helicase 77 C-terminal fragment no paralog Moth_0276 putative resolvase 484 N-terminal fragment 1 paralog Moth_0410 response regulator receiver 45 N-terminal fragment 2 paralogs Moth_0411 GGDEF 181 C-terminal fragment 7 paralogs Moth_0413 phage integrase 97 fragment 1 paralog Moth_0472 ATPase, E1-E2 type 351 C terminal left 1 paralog Moth_0627 reverse transcriptase 97 C-terminal fragment -
Bisphosphate Carboxylase/Oxygenase Activation in Tomato (Lycopersicon Esculentum Mil!.)
Plant Physiol. (1995) 107: 585-591 The Effects of Chilling in the Light on Ribulose-1,5- Bisphosphate Carboxylase/Oxygenase Activation in Tomato (Lycopersicon esculentum Mil!.) George T. Byrd’, Donald R. Ort, and William 1. Ogren* Photosynthesis Research Unit, Agricultura1 Research Service, United States Department of Agriculture (G.T.B., D.R.O., W.L.O.), and Department of Plant Biology, University of lllinois at Urbana-Champaign (D.R.O., W.L.O.), Urbana, lllinois 61801 reduced leve1 of RuBP. The bisphosphatases are activated Photosynthesis rate, ribulose-l,5-bisphosphate carboxylase/oxy- by the Fd/thioredoxin system (Buchanan, 1980), which genase (Rubisco) activation state, and ribulose bisphosphate con- may be affected by the light-chilling regime. Thus, in to- centration were reduced after exposing tomato (Lycopersicon es- mato, chilling in the light appears to limit the capacity of culentum Mill.) plants to light at 4°C for 6 h. Analysis of lysed and leaves to regenerate RuBP, the substrate in photosynthetic reconstituted chloroplasts showed that activity of the thylakoid CO, fixation catalyzed by the enzyme Rubisco (EC membrane was inhibited and that Rubisco, Rubisco activase, and 4.1.1.39). other soluble factors were not affected. Leaf photosynthesis rates Rubisco activity also has been reported to be directly and the ability of chilled thylakoid membranes to promote Rubisco impaired during chilling in the light in short-term (Sas- activation recovered after 24 h at 25°C. Thylakoid membranes from control tomato plants were as effective as spinach thylakoids in senrath et al., 1990) and long-term (Briiggemann et al., activating spinach Rubisco in the presence of spinach Rubisco ac- 1992) experiments. -
ADP-Ribosyl)Hydrolases: Structure, Function, and Biology
Downloaded from genesdev.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press SPECIAL SECTION: REVIEW (ADP-ribosyl)hydrolases: structure, function, and biology Johannes Gregor Matthias Rack,1,3 Luca Palazzo,2,3 and Ivan Ahel1 1Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom; 2Institute for the Experimental Endocrinology and Oncology, National Research Council of Italy, 80145 Naples, Italy ADP-ribosylation is an intricate and versatile posttransla- Diversification of NAD+ signaling is particularly apparent tional modification involved in the regulation of a vast in vertebrata, being linked to evolutionary optimization of variety of cellular processes in all kingdoms of life. Its NAD+ biosynthesis and increased (ADP-ribosyl) signaling complexity derives from the varied range of different (Bockwoldt et al. 2019). ADP-ribosylation is used by or- chemical linkages, including to several amino acid side ganisms from all kingdoms of life and some viruses chains as well as nucleic acids termini and bases, it can (Perina et al. 2014; Aravind et al. 2015) and controls a adopt. In this review, we provide an overview of the differ- wide range of cellular processes such as DNA repair, tran- ent families of (ADP-ribosyl)hydrolases. We discuss their scription, cell division, protein degradation, and stress re- molecular functions, physiological roles, and influence sponse to name a few (Bock and Chang 2016; Gupte et al. on human health and disease. Together, the accumulated 2017; Palazzo et al. 2017; Rechkunova et al. 2019). In ad- data support the increasingly compelling view that (ADP- dition to proteins, several in vitro observations strongly ribosyl)hydrolases are a vital element within ADP-ribosyl suggest that nucleic acids, both DNA and RNA, can be signaling pathways and they hold the potential for novel targets of ADP-ribosylation (Nakano et al. -
© 2010 Jong Nam Kim
© 2010 Jong Nam Kim GENETIC AND BIOCHEMICAL ANALYSIS OF NITROGEN METABOLISM IN RUMINAL ANAEROBIC BACTERIA: A COMPARISON BETWEEN RUMINOCOCCUS ALBUS 8 AND PREVOTELLA RUMINICOLA 23 BY JONG NAM KIM DISSERTATION Submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Animal Sciences in the Graduate College of the University of Illinois at Urbana-Champaign, 2010 Urbana, Illinois Doctoral Committee: Professor Roderick I. Mackie, Chair Associate Professor Isaac K. O. Cann Associate Professor Bruce W. Fouke Assistant Professor Juan J. Loor ABSTRACT These studies were conducted to improve the understanding of the genetic regulation and biochemical pathways utilized by the rumen bacteria, Ruminococcus albus 8 and Prevotella ruminicola 23 during growth on, and metabolism of, different nitrogen sources. Both R. albus 8 and P. ruminicola 23 were grown using different nitrogen sources; ammonia, urea, or peptides for R. albus 8 and ammonia or peptides for P. ruminicola 23 as the sole nitrogen source. Gene expression levels and enzyme activities were analyzed by RT-qPCR, and enzyme assays, as well as microarray and proteomic analyses for P. ruminicola. The results varied according to nitrogen source and also by growth phase. For R. albus 8 growth on ammonia or urea led to the synthesis of glutamate from ammonia by the NADPH-dependent glutamate dehydrogenase (NADPH-GDH). This glutamate was then transformed to glutamine by glutamine synthetase (GS). The later transformation was especially evident during early log phase, while the further transformation from glutamate to α-ketoglutarate by the up-regulated NADH-dependent glutamate dehydrogenase (NADH-GDH) was more evident during late exponential phase. -
AP Biology Life’S Beginning on Earth According to Scientific Findings (Associated Learning Objectives: 1.9, 1.10, 1.11, 1.12, 1.27, 1.28, 1.29, 1.30, 1.31, and 1.32)
AP Auburn University AP Summer Institute BIOLOGYJuly 11-14, 2016 AP Biology Life’s beginning on Earth according to scientific findings (Associated Learning Objectives: 1.9, 1.10, 1.11, 1.12, 1.27, 1.28, 1.29, 1.30, 1.31, and 1.32) I. The four steps necessary for life to emerge on Earth. (This is according to accepted scientific evidence.) A. First: An abiotic (non-living) synthesis of Amino Acids and Nucleic Acids must occur. 1. The RNA molecule is believed to have evolved first. It is not as molecularly stable as DNA though. 2. The Nucleic Acids (DNA or RNA) are essential for storing, retrieving, or conveying by inheritance molecular information on constructing the components of living cells.. 3. The Amino Acids, the building blocks of proteins, are needed to construct the “work horse” molecules of a cell. a. The majority of a cell or organism, in biomass (dry weight of an organism), is mostly protein. B. Second: Monomers must be able to join together to form more complex polymers using energy that is obtained from the surrounding environment. 1. Seen in monosaccharides (simple sugars) making polysaccharides (For energy storage or cell walls of plants.) 2. Seen in the making of phospholipids for cell membranes. 3. Seen in the making of messenger RNA used in making proteins using Amino Acids. 4. Seen in making chromosomes out of strings of DNA molecules. (For information storage.) C. Third: The RNA/DNA molecules form and gain the ability to reproduce and stabilize by using chemical bonds and complimentary bonding. -
Revealing the Metabolic Capacity of Streblomastix Strix and Its Bacterial Symbionts Using Single- Cell Metagenomics
Revealing the metabolic capacity of Streblomastix strix and its bacterial symbionts using single- cell metagenomics Sebastian C. Treitlia, Martin Koliskob, Filip Husníkc, Patrick J. Keelingc, and Vladimír Hampla,1 aDepartment of Parasitology, Faculty of Science, Charles University, BIOCEV, 252 42 Vestec, Czech Republic; bInstitute of Parasitology, Biology Centre, Czech Academy of Sciences, 370 05 Cˇeské Budeˇ jovice, Czech Republic; and cDepartment of Botany, University of British Columbia, Vancouver, BC V6T 1Z4, Canada Edited by Nancy A. Moran, University of Texas at Austin, Austin, TX, and approved August 14, 2019 (received for review June 26, 2019) Lower termites harbor in their hindgut complex microbial commu- Besides partial ribosomal (r)RNA genes used for diversity studies, nities that are involved in the digestion of cellulose. Among these are there are almost no molecular or biochemical data available for protists, which are usually associated with specific bacterial symbi- any of these protists. Early studies showed that Trichomitopsis onts found on their surface or inside their cells. While these form the termopsidis and several Trichonympha species, from the hindgut of foundations of a classic system in symbiosis research, we still know Zootermopsis (13–16), have the capacity to degrade cellulose (17, little about the functional basis for most of these relationships. Here, 18), but for other flagellates, including all oxymonads, the in- we describe the complex functional relationship between one pro- volvement in cellulose digestion remains unclear. Recent results tist, the oxymonad Streblomastix strix, and its ectosymbiotic bacte- have shown that the bacterial symbionts of oxymonads have the rial community using single-cell genomics.