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Calcium-Induced Conformational Changes in the Regulatory Domain of the Human Mitochondrial ATP-Mg/Pi Carrier
Biochimica et Biophysica Acta 1847 (2015) 1245–1253 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbabio Calcium-induced conformational changes in the regulatory domain of the human mitochondrial ATP-Mg/Pi carrier Steven P.D. Harborne, Jonathan J. Ruprecht, Edmund R.S. Kunji ⁎ The Medical Research Council, Mitochondrial Biology Unit, Cambridge Biomedical Campus, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK article info abstract Article history: The mitochondrial ATP-Mg/Pi carrier imports adenine nucleotides from the cytosol into the mitochondrial matrix Received 24 April 2015 and exports phosphate. The carrier is regulated by the concentration of cytosolic calcium, altering the size of the Received in revised form 15 June 2015 adenine nucleotide pool in the mitochondrial matrix in response to energetic demands. The protein consists of Accepted 6 July 2015 three domains; (i) the N-terminal regulatory domain, which is formed of two pairs of fused calcium-binding EF- Available online 9 July 2015 hands, (ii) the C-terminal mitochondrial carrier domain, which is involved in transport, and (iii) a linker region α Keywords: with an amphipathic -helix of unknown function. The mechanism by which calcium binding to the regulatory do- Calcium regulation mechanism main modulates substrate transport in the carrier domain has not been resolved. Here, we present two new crystal EF-hand conformational change structures of the regulatory domain of the human isoform 1. Careful analysis by SEC confirmed that although the SCaMC regulatory domain crystallised as dimers, full-length ATP-Mg/Pi carrier is monomeric. Therefore, the ATP-Mg/Pi Adenine nucleotide translocase carrier must have a different mechanism of calcium regulation than the architecturally related aspartate/glutamate Regulation of adenine nucleotides carrier, which is dimeric. -
(12) United States Patent (10) Patent No.: US 6,395,889 B1 Robison (45) Date of Patent: May 28, 2002
USOO6395889B1 (12) United States Patent (10) Patent No.: US 6,395,889 B1 Robison (45) Date of Patent: May 28, 2002 (54) NUCLEIC ACID MOLECULES ENCODING WO WO-98/56804 A1 * 12/1998 ........... CO7H/21/02 HUMAN PROTEASE HOMOLOGS WO WO-99/0785.0 A1 * 2/1999 ... C12N/15/12 WO WO-99/37660 A1 * 7/1999 ........... CO7H/21/04 (75) Inventor: fish E. Robison, Wilmington, MA OTHER PUBLICATIONS Vazquez, F., et al., 1999, “METH-1, a human ortholog of (73) Assignee: Millennium Pharmaceuticals, Inc., ADAMTS-1, and METH-2 are members of a new family of Cambridge, MA (US) proteins with angio-inhibitory activity', The Journal of c: - 0 Biological Chemistry, vol. 274, No. 33, pp. 23349–23357.* (*) Notice: Subject to any disclaimer, the term of this Descriptors of Protease Classes in Prosite and Pfam Data patent is extended or adjusted under 35 bases. U.S.C. 154(b) by 0 days. * cited by examiner (21) Appl. No.: 09/392, 184 Primary Examiner Ponnathapu Achutamurthy (22) Filed: Sep. 9, 1999 ASSistant Examiner William W. Moore (51) Int. Cl." C12N 15/57; C12N 15/12; (74) Attorney, Agent, or Firm-Alston & Bird LLP C12N 9/64; C12N 15/79 (57) ABSTRACT (52) U.S. Cl. .................... 536/23.2; 536/23.5; 435/69.1; 435/252.3; 435/320.1 The invention relates to polynucleotides encoding newly (58) Field of Search ............................... 536,232,235. identified protease homologs. The invention also relates to 435/6, 226, 69.1, 252.3 the proteases. The invention further relates to methods using s s s/ - - -us the protease polypeptides and polynucleotides as a target for (56) References Cited diagnosis and treatment in protease-mediated disorders. -
32-3824: FDX1 Recombinant Protein Description Product Info
ABGENEX Pvt. Ltd., E-5, Infocity, KIIT Post Office, Tel : +91-674-2720712, +91-9437550560 Email : [email protected] Bhubaneswar, Odisha - 751024, INDIA 32-3824: FDX1 Recombinant Protein Alternative Name : Adrenodoxin mitochondrial,Adrenal ferredoxin,Ferredoxin-1,Hepatoredoxin,FDX1,ADX. Description Source : Escherichia Coli. FDX1 Human Recombinant fused with a 15 amino acid T7 tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 139 amino acids (61-184 a.a.) and having a molecular mass of 15.0kDa.The FDX1 is purified by proprietary chromatographic techniques. Ferredoxin-1 is a small iron-sulfur protein who transfers electrons from NADPH through ferredoxin reductase to a terminal cytochrome P450. This specific oxidation/reduction system is located in steroidogenic tissues, and is involved with the synthesis of bile acid and vitamin D. FDX1 takes part in the synthesis of thyroid hormones and transfers electrons from adrenodoxin reductase to the cholesterol side chain cleavage cytochrome P450. FDX1 supports reactions catalyzed by human microsomal P450s- full length CYP17, truncated CYP17, and truncated CYP21. In addition to the FDX1 at the 11q22chromosomal locus, there are pseudogenes located on chromosomes 20 and 21. Product Info Amount : 25 µg Purification : Greater than 90.0% as determined by SDS-PAGE. Content : The FDX1 solution contains 20mM Tris-HCl buffer (pH8.0) and 10% Glycerol. Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of Storage condition : time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. -
Anti-FDX1 / Ferredoxin Antibody (ARG58670)
Product datasheet [email protected] ARG58670 Package: 100 μl anti-FDX1 / Ferredoxin antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes FDX1 / Ferredoxin Tested Reactivity Hu, Ms, Rat Tested Application IHC-P, WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name FDX1 / Ferredoxin Antigen Species Human Immunogen Recombinant fusion protein corresponding to aa. 1-184 of Human FDX1 (NP_004100.1). Conjugation Un-conjugated Alternate Names LOH11CR1D; Hepatoredoxin; ADX; Adrenal ferredoxin; FDX; Ferredoxin-1; Adrenodoxin, mitochondrial Application Instructions Application table Application Dilution IHC-P 1:50 - 1:200 WB 1:200 - 1:500 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control K562 Calculated Mw 19 kDa Observed Size 14 kDa Properties Form Liquid Purification Affinity purified. Buffer PBS (pH 7.3), 0.02% Sodium azide and 50% Glycerol. Preservative 0.02% Sodium azide Stabilizer 50% Glycerol Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. www.arigobio.com 1/2 Note For laboratory research only, not for drug, diagnostic or other use. Bioinformation Gene Symbol FDX1 Gene Full Name ferredoxin 1 Background This gene encodes a small iron-sulfur protein that transfers electrons from NADPH through ferredoxin reductase to mitochondrial cytochrome P450, involved in steroid, vitamin D, and bile acid metabolism. -
An Update on Jacalin-Like Lectins and Their Role in Plant Defense
International Journal of Molecular Sciences Review An Update on Jacalin-Like Lectins and Their Role in Plant Defense Lara Esch and Ulrich Schaffrath * ID Department of Plant Physiology, RWTH Aachen University, 52056 Aachen, Germany; [email protected] * Correspondence: [email protected]; Tel.: +49-241-8020100 Received: 30 June 2017; Accepted: 20 July 2017; Published: 22 July 2017 Abstract: Plant lectins are proteins that reversibly bind carbohydrates and are assumed to play an important role in plant development and resistance. Through the binding of carbohydrate ligands, lectins are involved in the perception of environmental signals and their translation into phenotypical responses. These processes require down-stream signaling cascades, often mediated by interacting proteins. Fusing the respective genes of two interacting proteins can be a way to increase the efficiency of this process. Most recently, proteins containing jacalin-related lectin (JRL) domains became a subject of plant resistance responses research. A meta-data analysis of fusion proteins containing JRL domains across different kingdoms revealed diverse partner domains ranging from kinases to toxins. Among them, proteins containing a JRL domain and a dirigent domain occur exclusively within monocotyledonous plants and show an unexpected high range of family member expansion compared to other JRL-fusion proteins. Rice, wheat, and barley plants overexpressing OsJAC1, a member of this family, are resistant against important fungal pathogens. We discuss the possibility that JRL domains also function as a decoy in fusion proteins and help to alert plants of the presence of attacking pathogens. Keywords: fusion protein; JRL domain; plant resistance; dirigent protein; decoy; chimeric protein 1. -
Cei'itre for Newfoundi.Ano Studies
CEI'ITRE FOR NEWFOUNDI.ANO STUDIES TOTAL OF 10 PACES ONLY MAY BE XEROXED (W1thout Author·• Pt-rminton) PURIFICATION AND CHARACTERIZATION OF MAJOR GELATIN CLEAVAGE ACTIVITIES IN THE APICALLY LOCATED EXTRACELLULAR MATRIX OF THE SEA URCHIN EMBRYO by Lavanya Ranganathan A Thesis Submitted to the School of Graduate Studies in Partial Fulfillment of the Requirements for the Degree of Master of Science Department of Biochemistry Memorial University of Newfoundland and Labrador May, 2004 St.John's Newfoundland and Labrador Canada Library and Bibliotheque et 1+1 Archives Canada Archives Canada Published Heritage Direction du Branch Patrimoine de !'edition 395 Wellington Street 395, rue Wellington Ottawa ON K1A ON4 Ottawa ON K1A ON4 Canada Canada Your file Votre reference ISBN: 0-612-99107-5 Our file Notre reference ISBN: 0-612-99107-5 NOTICE: AVIS: The author has granted a non L'auteur a accorde une licence non exclusive exclusive license allowing Library permettant a Ia Bibliotheque et Archives and Archives Canada to reproduce, Canada de reproduire, publier, archiver, publish, archive, preserve, conserve, sauvegarder, conserver, transmettre au public communicate to the public by par telecommunication ou par I' Internet, preter, telecommunication or on the Internet, distribuer et vendre des theses partout dans loan, distribute and sell theses le monde, a des fins commerciales ou autres, worldwide, for commercial or non sur support microforme, papier, electronique commercial purposes, in microform, et/ou autres formats. paper, electronic and/or any other formats. The author retains copyright L'auteur conserve Ia propriete du droit d'auteur ownership and moral rights in et des droits moraux qui protege cette these. -
Endocrinology
Endocrinology INTRODUCTION Endocrinology 1. Endocrinology is the study of the endocrine system secretions and their role at target cells within the body and nervous system are the major contributors to the flow of information between different cells and tissues. 2. Two systems maintain Homeostasis a. b 3. Maintain a complicated relationship 4. Hormones 1. The endocrine system uses hormones (chemical messengers/neurotransmitters) to convey information between different tissues. 2. Transport via the bloodstream to target cells within the body. It is here they bind to receptors on the cell surface. 3. Non-nutritive Endocrine System- Consists of a variety of glands working together. 1. Paracrine Effect (CHEMICAL) Endocrinology Spring 2013 Page 1 a. Autocrine Effect i. Hormones released by cells that act on the membrane receptor ii. When a hormone is released by a cell and acts on the receptors located WITHIN the same cell. Endocrine Secretions: 1. Secretions secreted Exocrine Secretion: 1. Secretion which come from a gland 2. The secretion will be released into a specific location Nervous System vs tHe Endocrine System 1. Nervous System a. Neurons b. Homeostatic control of the body achieved in conjunction with the endocrine system c. Maintain d. This system will have direct contact with the cells to be affected e. Composed of both the somatic and autonomic systems (sympathetic and parasympathetic) Endocrinology Spring 2013 Page 2 2. Endocrine System a. b. c. 3. Neuroendocrine: a. These are specialized neurons that release chemicals that travel through the vascular system and interact with target tissue. b. Hypothalamus à posterior pituitary gland History of tHe Endocrine System Bertold (1849)-FATHER OF ENDOCRINOLOGY 1. -
Figure S1. Quality Control Validation of MS Data. (A‑C) Mass Error Distribution of All Peptides Identified in the Acetylome
Figure S1. Quality control validation of MS data. (A‑C) Mass error distribution of all peptides identified in the acetylome, succi- nylome and quantitative proteome, respectively. (D‑F) Length distribution of peptides identified in the acetylome, succinylome and quantitative proteome, respectively. Figure S2. Comparison of modification level between breast cancer tissue and normal tissue. Comparison of acetylation level (A) and succinylation level (B) between breast cancer tissue and normal tissue. Data are medians and were analyzed using Wilcoxon Signed Rank Test. **P<0.01. Table SI. Protein sites whose acetylation and succinylation levels were both significantly upregulated in breast cancer tissues (fold change ≥1.5 compared with normal tissues). Protein ID Protein name Modification site P54868 HMCS2 310K Q15063 POSTN 549K Q99715 COCA1 1601K P51572 BAP31 72K P07237 PDLA1 328K Q06830 PRDX1 192K P48735 IDHP 180K P30101 PDIA3 417K P0DMV9 HS71B 526K Q01995 TAGL 21K P06748 NPM1 27K Q00325 MPCP 209K P00488 F13A 69K P02545 LMNA 260K P08133 ANXA6 478K P02452 CO1A1 751K Table SII. Protein sites whose acetylation and succinylation levels were both significantly downregulated in breast cancer tissues (fold change ≥1.5 compared with normal tissues). Protein ID Protein name Modification site RET4 P02753 30K PSG2 P07585 142K HBA P69905 12K IGKC P01834 80K HBA P69905 8K Table SIII. All proteins whose expression level were significantly upregulated in breast cancer tissues (fold change ≥1.5 compared with normal tissues). Protein ID Protein description -
Genes in Eyecare Geneseyedoc 3 W.M
Genes in Eyecare geneseyedoc 3 W.M. Lyle and T.D. Williams 15 Mar 04 This information has been gathered from several sources; however, the principal source is V. A. McKusick’s Mendelian Inheritance in Man on CD-ROM. Baltimore, Johns Hopkins University Press, 1998. Other sources include McKusick’s, Mendelian Inheritance in Man. Catalogs of Human Genes and Genetic Disorders. Baltimore. Johns Hopkins University Press 1998 (12th edition). http://www.ncbi.nlm.nih.gov/Omim See also S.P.Daiger, L.S. Sullivan, and B.J.F. Rossiter Ret Net http://www.sph.uth.tmc.edu/Retnet disease.htm/. Also E.I. Traboulsi’s, Genetic Diseases of the Eye, New York, Oxford University Press, 1998. And Genetics in Primary Eyecare and Clinical Medicine by M.R. Seashore and R.S.Wappner, Appleton and Lange 1996. M. Ridley’s book Genome published in 2000 by Perennial provides additional information. Ridley estimates that we have 60,000 to 80,000 genes. See also R.M. Henig’s book The Monk in the Garden: The Lost and Found Genius of Gregor Mendel, published by Houghton Mifflin in 2001 which tells about the Father of Genetics. The 3rd edition of F. H. Roy’s book Ocular Syndromes and Systemic Diseases published by Lippincott Williams & Wilkins in 2002 facilitates differential diagnosis. Additional information is provided in D. Pavan-Langston’s Manual of Ocular Diagnosis and Therapy (5th edition) published by Lippincott Williams & Wilkins in 2002. M.A. Foote wrote Basic Human Genetics for Medical Writers in the AMWA Journal 2002;17:7-17. A compilation such as this might suggest that one gene = one disease. -
![A Label-Free Cellular Proteomics Approach to Decipher the Antifungal Action of Dimiq, a Potent Indolo[2,3- B]Quinoline Agent, Against Candida Albicans Biofilms](https://docslib.b-cdn.net/cover/9827/a-label-free-cellular-proteomics-approach-to-decipher-the-antifungal-action-of-dimiq-a-potent-indolo-2-3-b-quinoline-agent-against-candida-albicans-biofilms-409827.webp)
A Label-Free Cellular Proteomics Approach to Decipher the Antifungal Action of Dimiq, a Potent Indolo[2,3- B]Quinoline Agent, Against Candida Albicans Biofilms
A Label-Free Cellular Proteomics Approach to Decipher the Antifungal Action of DiMIQ, a Potent Indolo[2,3- b]Quinoline Agent, against Candida albicans Biofilms Robert Zarnowski 1,2*, Anna Jaromin 3*, Agnieszka Zagórska 4, Eddie G. Dominguez 1,2, Katarzyna Sidoryk 5, Jerzy Gubernator 3 and David R. Andes 1,2 1 Department of Medicine, School of Medicine & Public Health, University of Wisconsin-Madison, Madison, WI 53706, USA; [email protected] (E.G.D.); [email protected] (D.R.A.) 2 Department of Medical Microbiology, School of Medicine & Public Health, University of Wisconsin-Madison, Madison, WI 53706, USA 3 Department of Lipids and Liposomes, Faculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland; [email protected] 4 Department of Medicinal Chemistry, Jagiellonian University Medical College, 30-688 Cracow, Poland; [email protected] 5 Department of Pharmacy, Cosmetic Chemicals and Biotechnology, Team of Chemistry, Łukasiewicz Research Network-Industrial Chemistry Institute, 01-793 Warsaw, Poland; [email protected] * Correspondence: [email protected] (R.Z.); [email protected] (A.J.); Tel.: +1-608-265-8578 (R.Z.); +48-71-3756203 (A.J.) Label-Free Cellular Proteomics of Candida albicans biofilms treated with DiMIQ Identified Proteins Accession # Alternate ID Gene names (ORF ) WT DIMIQ Z SCORE Proteins induced by DiMIQ Arginase (EC 3.5.3.1) A0A1D8PP00 CAR1 CAALFM_C504490CA 0.000 6.648 drug induced Glucan 1,3-beta-glucosidase BGL2 (EC 3.2.1.58) (Exo-1Q5AMT2 BGL2 CAALFM_C402250CA -
Segregating Expression Domains of Two Goosecoid Genes During the Transition from Gastrulation to Neurulation in Chick Embryos
Development 124, 1443-1452 (1997) 1443 Printed in Great Britain © The Company of Biologists Limited 1997 DEV2146 Segregating expression domains of two goosecoid genes during the transition from gastrulation to neurulation in chick embryos Lydia Lemaire1, Tobias Roeser1, Juan Carlos Izpisúa-Belmonte2 and Michael Kessel1,* 1Max-Planck-Institut für biophysikalische Chemie, Am Fassberg, D-37077 Göttingen, Germany 2The Salk Institute, 10010 N. Torrey Pines Road, La Jolla, California 92037, USA *Author for correspondence (e-mail: [email protected]) SUMMARY We report the isolation and characterization of a chicken plate around the anterior streak and overlying the pre- gene, GSX, containing a homeobox similar to that of the chordal plate. We demonstrate that the GSX-positive part goosecoid gene. The structure of the GSX gene and the of the primitive streak induces gastrulation, while the GSC- deduced GSX protein are highly related to the previously expressing part induces neurulation. After full extension of described goosecoid gene. The two homeodomains are 74% the streak, the fate of cells now characterized by GSX is to identical. In the first few hours of chick embryogenesis, the undergo neurulation, while those expressing GSC undergo expression pattern of GSX is similar to GSC, in the gastrulation. We discuss the effect of a duplicated basic posterior margin of the embryo and the young primitive goosecoid identity for the generation of a chordate nervous streak. Later during gastrulation, expression of the two system in ontogeny and phylogeny. genes segregate. GSC is expressed in the anterior part of the primitive streak, then in the node, and finally in the pre- chordal plate. -
Aldolase C (C-Terminus Specific) Data Sheet
Aldolase C (C-terminus Specific) Data Sheet Catalog Number: MO22157 Host: Mouse Product Type: Monoclonal IgG1 Species Human, horse, cow, pig, Affinity Purified Antibody Reactivity: chicken, rat, mouse Immunogen Sequence: C-terminal sequence Format: Liquid, 100 ul aliquot KYEGSGEDGGAAAQSLYIANHAY Concentration: 1 mg/ml HGNC name for this protein is ALDOC Applications: Immunofluorescence/Immunocytochemistry: 1:500-1:1,000 Immunohistochemistry: 1: 500-1:1,000 Western Blot: 1:1,000 Dilutions listed as a recommendation. Optimal dilution should be determined by investigator. Storage: Antibody can also be aliquoted and stored frozen at -20° C to -70° C in a manual defrost freezer for six months without detectable loss of activity. The antibody can be stored at 2° - 8° C for 1 month without detectable loss of activity. Avoid repeated freeze-thaw cycles. Application Notes Description/Data: Aldolase A is generally considered to be a muscle enzyme. Northern analysis of cultured cells suggests that it is present in both neurons and glia. Aldolase C shares 81% amino acid identity with aldolase A and 70% identity with aldolase B. Earlier studies using isozyme-specific antibodies report its location in gray matter astrocytes and cells of the pia mater. In situ hybridization of mouse central nervous system using isozyme-specific probes revealed that aldolase A and C are expressed in complementary cell types: aldolase A mRNA is found in neurons; aldolase C message is detected in astrocytes, some cells of the pia mater, and Purkinje cells. Aldolase C can in some situations be used as an astrocyte marker. However Purkinje cells of the cerebellum contain high levels of the enzyme, so the enzyme is not totally astrocyte specific.