A) Analysis of the Ncrnas of Arabidopsis Inflorescences and Pollen Bioreplicates (Two Bioreplicates for Each Tissue
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Promiscuity and Specificity of Eukaryotic Glycosyltransferases
Biochemical Society Transactions (2020) 48 891–900 https://doi.org/10.1042/BST20190651 Review Article Promiscuity and specificity of eukaryotic glycosyltransferases Ansuman Biswas and Mukund Thattai Simons Centre for the Study of Living Machines, National Centre for Biological Sciences, TIFR, Bangalore, India Correspondence: Mukund Thattai ([email protected]) Glycosyltransferases are a large family of enzymes responsible for covalently linking sugar monosaccharides to a variety of organic substrates. These enzymes drive the synthesis of complex oligosaccharides known as glycans, which play key roles in inter-cellular interac- tions across all the kingdoms of life; they also catalyze sugar attachment during the syn- thesis of small-molecule metabolites such as plant flavonoids. A given glycosyltransferase enzyme is typically responsible for attaching a specific donor monosaccharide, via a spe- cific glycosidic linkage, to a specific moiety on the acceptor substrate. However these enzymes are often promiscuous, able catalyze linkages between a variety of donors and acceptors. In this review we discuss distinct classes of glycosyltransferase promiscuity, each illustrated by enzymatic examples from small-molecule or glycan synthesis. We high- light the physical causes of promiscuity, and its biochemical consequences. Structural studies of glycosyltransferases involved in glycan synthesis show that they make specific contacts with ‘recognition motifs’ that are much smaller than the full oligosaccharide sub- strate. There is a wide range in the sizes of glycosyltransferase recognition motifs: highly promiscuous enzymes recognize monosaccharide or disaccharide motifs across multiple oligosaccharides, while highly specific enzymes recognize large, complex motifs found on few oligosaccharides. In eukaryotes, the localization of glycosyltransferases within compartments of the Golgi apparatus may play a role in mitigating the glycan variability caused by enzyme promiscuity. -
Fucosyltransferase Genes on Porcine Chromosome 6Q11 Are Closely Linked to the Blood Group Inhibitor (S) and Escherichia Coli F18 Receptor (ECF18R) Loci
Mammalian Genome 8, 736–741 (1997). © Springer-Verlag New York Inc. 1997 Two a(1,2) fucosyltransferase genes on porcine Chromosome 6q11 are closely linked to the blood group inhibitor (S) and Escherichia coli F18 receptor (ECF18R) loci E. Meijerink,1 R. Fries,1,*P.Vo¨geli,1 J. Masabanda,1 G. Wigger,1 C. Stricker,1 S. Neuenschwander,1 H.U. Bertschinger,2 G. Stranzinger1 1Institute of Animal Science, Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092 Zurich, Switzerland 2Institute of Veterinary Bacteriology, University of Zurich, CH 8057 Zurich, Switzerland Received: 17 February 1997 / Accepted: 30 May 1997 Abstract. The Escherichia coli F18 receptor locus (ECF18R) has fimbriae F107, has been shown to be genetically controlled by the been genetically mapped to the halothane linkage group on porcine host and is inherited as a dominant trait (Bertschinger et al. 1993) Chromosome (Chr) 6. In an attempt to obtain candidate genes for with B being the susceptibility allele and b the resistance allele. this locus, we isolated 5 cosmids containing the a(1,2)fucosyl- The genetic locus for this E. coli F18 receptor (ECF18R) has been transferase genes FUT1, FUT2, and the pseudogene FUT2P from mapped to porcine Chr 6 (SSC6), based on its close linkage to the a porcine genomic library. Mapping by fluorescence in situ hy- S locus and other loci of the halothane (HAL) linkage group (Vo¨- bridization placed all these clones in band q11 of porcine Chr 6 geli et al. 1996). The epistatic S locus suppresses the phenotypic (SSC6q11). Sequence analysis of the cosmids resulted in the char- expression of the A-0 blood group system when being SsSs (Vo¨geli acterization of an open reading frame (ORF), 1098 bp in length, et al. -
(12) Patent Application Publication (10) Pub. No.: US 2003/0082511 A1 Brown Et Al
US 20030082511A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2003/0082511 A1 Brown et al. (43) Pub. Date: May 1, 2003 (54) IDENTIFICATION OF MODULATORY Publication Classification MOLECULES USING INDUCIBLE PROMOTERS (51) Int. Cl." ............................... C12O 1/00; C12O 1/68 (52) U.S. Cl. ..................................................... 435/4; 435/6 (76) Inventors: Steven J. Brown, San Diego, CA (US); Damien J. Dunnington, San Diego, CA (US); Imran Clark, San Diego, CA (57) ABSTRACT (US) Correspondence Address: Methods for identifying an ion channel modulator, a target David B. Waller & Associates membrane receptor modulator molecule, and other modula 5677 Oberlin Drive tory molecules are disclosed, as well as cells and vectors for Suit 214 use in those methods. A polynucleotide encoding target is San Diego, CA 92121 (US) provided in a cell under control of an inducible promoter, and candidate modulatory molecules are contacted with the (21) Appl. No.: 09/965,201 cell after induction of the promoter to ascertain whether a change in a measurable physiological parameter occurs as a (22) Filed: Sep. 25, 2001 result of the candidate modulatory molecule. Patent Application Publication May 1, 2003 Sheet 1 of 8 US 2003/0082511 A1 KCNC1 cDNA F.G. 1 Patent Application Publication May 1, 2003 Sheet 2 of 8 US 2003/0082511 A1 49 - -9 G C EH H EH N t R M h so as se W M M MP N FIG.2 Patent Application Publication May 1, 2003 Sheet 3 of 8 US 2003/0082511 A1 FG. 3 Patent Application Publication May 1, 2003 Sheet 4 of 8 US 2003/0082511 A1 KCNC1 ITREXCHO KC 150 mM KC 2000000 so 100 mM induced Uninduced Steady state O 100 200 300 400 500 600 700 Time (seconds) FIG. -
Expression and Localization of Grass Carp Pkc-Θ (Protein Kinase C Theta) Gene After Its Activation T
Fish and Shellfish Immunology 87 (2019) 788–795 Contents lists available at ScienceDirect Fish and Shellfish Immunology journal homepage: www.elsevier.com/locate/fsi Full length article Expression and localization of grass carp pkc-θ (protein kinase C theta) gene after its activation T ∗∗ Rumana Mehjabina,b,1, Liangming Chena,b,1, Rong Huanga, , Denghui Zhua,b, Cheng Yanga,b, ∗ Yongming Lia, Lanjie Liaoa, Libo Hea, Zuoyan Zhua, Yaping Wanga, a State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan, 430072, China b University of Chinese Academy of Sciences, Beijing, 100049, China ARTICLE INFO ABSTRACT Keywords: Haemorrhagic disease caused by grass carp reovirus (GCRV) can result in large-scale death of young grass carp, Grass carp leading to irreparable economic losses that seriously affect large-scale breeding. Protein kinase C (PKC, also Grass carp reovirus (GCRV) known as PRKC) represents a family of serine/threonine protein kinases that includes multiple isozymes in many Protein kinase C (PKC) species. Among these, PKC-θ (PKC theta, also written as PRKCQ) is a novel isoform, mainly expressed in T cells, Host immune defences that is known to be involved in immune system function in mammals. To date, no research on immunological functions of fish Pkc-θ has been reported. To address this issue, we cloned the grass carp pkc-θ gene. Phylogenetic and syntenic analysis showed that this gene is the most evolutionarily conserved relative to zeb- rafish. Real-time quantitative PCR (RT-qPCR) indicated that pkc-θ was expressed at high levels in the gills and spleen of healthy grass carp. -
Mitochondrial ABC Transporters Vxpx Cargo-Targeting to Cilium Alpha
PA2GF PA2G5PA2GD PA21BPA2GEPA2GXPA2G3 Acyl chainAcyl chainremodelling remodelling of PI of PG Acyl chain remodelling of PS PA24C AcylAcyl chain chain remodelling remodelling of PCof PE GABA A receptor activation Neurotransmitter receptors and postsynaptic signal transmission GBRA2 GBRB3GBRA6GBRA5 PA2GA GBRA1GBRG2GBRB2GBRB1 GBRT GBRG3GBRA4GBRA3 PA24B Ligand-gated ion channel transport Acyl-CoA:dihydroxyacetonephosphateacyltransferase PPBI Hydrolysis of LPC Hydrolysis ofSynthesis LPE of PA LA Post-translational modification: synthesis of GPI-anchored proteins Catecholamine biosynthesis Plasmalogen biosynthesis GABAGBRR3 AGBRR2 (rho) receptor activation RNA Polymerase III Transcription Termination GBRR1 Creatine metabolism RNA Polymerase III AbortivePNMT AndDDC Retractive Initiation ReuptakeS6A11 of GABA PPBT DigestionPPBN S6A12SC6A7 Interaction between L1 and Ankyrins GLRA1 SC6A1 S6A13 SerotoninSodium/myo-inositol andInositol melatonin transporters cotransporter biosynthesis 2 GLRA2 KCRM FOLR2 KCNQ2 5HT3E5HT3D SC6A3 Astrocytic Glutamate-Glutamine Uptake And Metabolism 5HT3B EAA1 5HT3A5HT3C Na+/Cl- dependent neurotransmitter transportersDopamine clearance from the synaptic cleft SCN8AEAA2 Methylation of TransportINMTMeSeH forof inorganicexcretionSCNAASCN3ASCN2A cations/anions and amino acids/oligopeptidesGlycosyltransferase-likeO-linked glycosylation protein LARGE1 SC6A5SC6A9S6A15 SCN9ASCN4ASCN1ASCNBA SC6A6 SCN7ASCN5A Insulin effects increased synthesis of Xylulose-5-Phosphate SC6A2 TPH1 Potassium transport channels MOT2 Glutamine synthetaseCAC1I -
A-Transferase, 338 ABO Blood Group System, 330 and Cloning, 338
Index A-transferase, 338 ALG9,165 ABO blood group system, 330 ALGlO,168 and cloning, 338 genetic basis of, 22 B-transferase, 338 activated oligosaccharides bacterial S-Iayers in glycopeptide synthesis, 466, 470 glycosylation in, 439 2-aminoethylphosphonate bacterial toxins in invertebrate glycoproteins, 420 and glycosylation, 413 anomer, 5 biological macromolecules formal defmition of, 6 the four groups of, 2 Hudson definition of, 6 bird's nest soup, 16 anomeric carbon blood group antigens, 22 in synthesis, 459 and cancer, 23 anomeric effect, 8 prognostic value of, 23 anomeric oxygen exchange reactions, blood typing, 22 460,461 ABO system of, 22 anomeric oxygen-retaining reactions, 460, Lewis system of, 22 464 Bombay blood group, 331, 336, 348 antennae Bombay phenotype, 22 definition of, 10 branch specificity, 93 J3-arabinofuranose in plants, 418 caeruloplasmin, 23 asialoglycoprotein receptor, 494 calnexin, 54, 182 asparagine-linked glycosylation genes calreticulin, 54, 182, 188 ALGI, 158 capillary electrophoresis, 457 ALG2,161 carbohydrate metabolism, 1, 17 ALG3,165 Carbohydrate-Deficient Glycoprotein ALG5,167 Syndrome (COGS) Type 1, 152 ALG6,168 Carbohydrate-Deficient Glycoprotein ALG7,155 Syndrome (COGS) Type II, 226 ALGB,168 500 Index Carbohydrates; See a/so oligosaccharides deoxymannoj irimycin, 191 as molecules with key biological deoxynojirimycin, 184 functions, 3 dietary sugars, 1 biology of, 2 disaccharides covalent attachment to protein, 17 structural determination of, 17 definition of, 4 DNA,1 in bacterial and viral infection, -
Development and Validation of a Protein-Based Risk Score for Cardiovascular Outcomes Among Patients with Stable Coronary Heart Disease
Supplementary Online Content Ganz P, Heidecker B, Hveem K, et al. Development and validation of a protein-based risk score for cardiovascular outcomes among patients with stable coronary heart disease. JAMA. doi: 10.1001/jama.2016.5951 eTable 1. List of 1130 Proteins Measured by Somalogic’s Modified Aptamer-Based Proteomic Assay eTable 2. Coefficients for Weibull Recalibration Model Applied to 9-Protein Model eFigure 1. Median Protein Levels in Derivation and Validation Cohort eTable 3. Coefficients for the Recalibration Model Applied to Refit Framingham eFigure 2. Calibration Plots for the Refit Framingham Model eTable 4. List of 200 Proteins Associated With the Risk of MI, Stroke, Heart Failure, and Death eFigure 3. Hazard Ratios of Lasso Selected Proteins for Primary End Point of MI, Stroke, Heart Failure, and Death eFigure 4. 9-Protein Prognostic Model Hazard Ratios Adjusted for Framingham Variables eFigure 5. 9-Protein Risk Scores by Event Type This supplementary material has been provided by the authors to give readers additional information about their work. Downloaded From: https://jamanetwork.com/ on 10/02/2021 Supplemental Material Table of Contents 1 Study Design and Data Processing ......................................................................................................... 3 2 Table of 1130 Proteins Measured .......................................................................................................... 4 3 Variable Selection and Statistical Modeling ........................................................................................ -
CDG and Immune Response: from Bedside to Bench and Back Authors
CDG and immune response: From bedside to bench and back 1,2,3 1,2,3,* 2,3 1,2 Authors: Carlota Pascoal , Rita Francisco , Tiago Ferro , Vanessa dos Reis Ferreira , Jaak Jaeken2,4, Paula A. Videira1,2,3 *The authors equally contributed to this work. 1 Portuguese Association for CDG, Lisboa, Portugal 2 CDG & Allies – Professionals and Patient Associations International Network (CDG & Allies – PPAIN), Caparica, Portugal 3 UCIBIO, Departamento Ciências da Vida, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, 2829-516 Caparica, Portugal 4 Center for Metabolic Diseases, UZ and KU Leuven, Leuven, Belgium Word count: 7478 Number of figures: 2 Number of tables: 3 This article has been accepted for publication and undergone full peer review but has not been through the copyediting, typesetting, pagination and proofreading process which may lead to differences between this version and the Version of Record. Please cite this article as doi: 10.1002/jimd.12126 This article is protected by copyright. All rights reserved. Abstract Glycosylation is an essential biological process that adds structural and functional diversity to cells and molecules, participating in physiological processes such as immunity. The immune response is driven and modulated by protein-attached glycans that mediate cell-cell interactions, pathogen recognition and cell activation. Therefore, abnormal glycosylation can be associated with deranged immune responses. Within human diseases presenting immunological defects are Congenital Disorders of Glycosylation (CDG), a family of around 130 rare and complex genetic diseases. In this review, we have identified 23 CDG with immunological involvement, characterised by an increased propensity to – often life-threatening – infection. -
PKC-Theta-Mediated Signal Delivery from Thetcr/CD28 Surface Receptors
REVIEW ARTICLE published: 22 August 2012 doi: 10.3389/fimmu.2012.00273 PKC-theta-mediated signal delivery from theTCR/CD28 surface receptors Noah Isakov1* and Amnon Altman2 1 The Shraga Segal Department of Microbiology and Immunology, Faculty of Health Sciences and the Cancer Research Center, Ben-Gurion University of the Negev, Beer Sheva, Israel 2 Division of Cell Biology, La Jolla Institute for Allergy and Immunology, La Jolla, CA, USA Edited by: Protein kinase C-theta (PKCθ) is a key enzyme inT lymphocytes, where it plays an important Nick Gascoigne, Scripps Research role in signal transduction downstream of the activated T cell antigen receptor (TCR) and Institute, USA the CD28 costimulatory receptor. Interest in PKCθ as a potential drug target has increased Reviewed by: following recent findings that PKCθ is essential for harmful inflammatory responses medi- Balbino Alarcon, Consejo Superior de Investigaciones Cientificas, Spain ated byTh2 (allergies) andTh17 (autoimmunity) cells as well as for graft-versus-host disease Salvatore Valitutti, INSERM, France (GvHD) and allograft rejection, but is dispensable for beneficial responses such as antiviral *Correspondence: immunity and graft-versus-leukemia (GvL) response. TCR/CD28 engagement triggers the Noah Isakov, The Shraga Segal translocation of the cytosolic PKCθ to the plasma membrane (PM), where it localizes at Department of Microbiology and the center of the immunological synapse (IS), which forms at the contact site between an Immunology, Faculty of Health Sciences and the Cancer Research antigen-specificT cell and antigen-presenting cells (APC). However, the molecular basis for Center, Ben-Gurion University this unique localization, and whether it is required for its proper function have remained of the Negev, P.O. -
Thesematthieuvillegente2013annexes
Supplemental table 1: list of the proteins identifed from the total protein fraction of Amborella trichopoda isolated embryo by shot gun Proteins have been analyzed by mono-dimensional electrophoresis and identified by mass spectrometry LC/MS-MS. The protein spots were analysed by LC-MS/MS on the PAPPSO plateform (Benoit Valot, Thierry Balliau, Michel Zivy, INRA Moulon, France; http://pappso.inra.fr). Based on the spectrum generated, proteins were identified using the X-Tandem software. "NCBI accession number" is the accession number in NCBI database. "Protein name" . "Organism" relates to the organism from which the identied protein comes from for functional analysis - efforts were focus on Arabidopsis thaliana as a plant model. " "AGI" . "Function category" and "Function description" relate to the functional categories defined according to the ontological classification of Bevan et al . [Bevan et al . (1998) Nature 391:485-488]. "log(Evalue) identification" reflects the statistical power of the identification by BLAST (performed on TAIR or BLAST). "Identity" indicates in % the recovery of the Amborella protein sequence against the identified protein. "Compartement" indicates if the identification is found in the embryo (emb.), the endosperm (end.) or both (emb./end.). "Description" was taken from the Amborella EVM 27 Predicted Proteins (http://www.amborella.org). The "log (E value)" is a statistical parameter that represents the number of peptides present at random in the database. It was calculated by the product of the Evalue of unique peptides identified in the protein spot (Valot et al., 2011). "Coverage" refers to the recovery rate of the protein by the identified peptides, expressed in %. -
Novel Roles of SH2 and SH3 Domains in Lipid Binding
cells Review Novel Roles of SH2 and SH3 Domains in Lipid Binding Szabolcs Sipeki 1,†, Kitti Koprivanacz 2,†, Tamás Takács 2, Anita Kurilla 2, Loretta László 2, Virag Vas 2 and László Buday 1,2,* 1 Department of Molecular Biology, Institute of Biochemistry and Molecular Biology, Semmelweis University Medical School, 1094 Budapest, Hungary; [email protected] 2 Institute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary; [email protected] (K.K.); [email protected] (T.T.); [email protected] (A.K.); [email protected] (L.L.); [email protected] (V.V.) * Correspondence: [email protected] † Both authors contributed equally to this work. Abstract: Signal transduction, the ability of cells to perceive information from the surroundings and alter behavior in response, is an essential property of life. Studies on tyrosine kinase action fundamentally changed our concept of cellular regulation. The induced assembly of subcellular hubs via the recognition of local protein or lipid modifications by modular protein interactions is now a central paradigm in signaling. Such molecular interactions are mediated by specific protein interaction domains. The first such domain identified was the SH2 domain, which was postulated to be a reader capable of finding and binding protein partners displaying phosphorylated tyrosine side chains. The SH3 domain was found to be involved in the formation of stable protein sub-complexes by constitutively attaching to proline-rich surfaces on its binding partners. The SH2 and SH3 domains have thus served as the prototypes for a diverse collection of interaction domains that recognize not only proteins but also lipids, nucleic acids, and small molecules. -
Role of the Ras-Association Domain Family 1 Tumor Suppressor Gene in Human Cancers
Review Role of the Ras-Association Domain Family 1 Tumor Suppressor Gene in Human Cancers Angelo Agathanggelou, Wendy N. Cooper, and Farida Latif Section of Medical and Molecular Genetics, Division of Reproductive and Child Health, The Institute of Biomedical Research, University of Birmingham, Edgbaston, Birmingham, United Kingdom Abstract renal cell carcinomas was identified from region 3p25 confirming In recent years, the list of tumor suppressor genes (or this hypothesis (3). This prompted the search for TSGs within the candidate TSG) that are inactivated frequently by epigenetic other regions of 3p. An important TSG was suspected to reside in events rather than classic mutation/deletion events has been 3p21.3 because instability of this region is the earliest and most growing. Unlike mutational inactivation, methylation is frequently detected deficiency in lung cancer. Overlapping homo- reversible and demethylating agents and inhibitors of histone zygous deletions in lung and breast tumor cell lines reduced the deacetylases are being used in clinical trails. Highly sensitive critical region in 3p21.3 to 120 kb and this region was found to be and quantitative assays have been developed to assess exceptionally gene rich. From this critical region, eight genes were methylation in tumor samples, early lesions, and bodily fluids. identified, including CACNA2D2, PL6/placental protein 6, CYB561D2/101F6, TUSC4/NPRL2/G21, ZMYND10/BLU, RASSF1/ Hence, gene silencing by promoter hypermethylation has potential clinical benefits in early cancer diagnosis, prognosis, 123F2, TUSC2/FUS1, and HYAL2/LUCA2. However, despite extensive treatment, and prevention. The hunt for a TSG located at genetic analysis in lung and breast tumors, none of these candidate 3p21.3 resulted in the identification of the RAS-association genes were frequently mutated.