ADP-Ribosylation in Animal Tissues: Structure, Function, and Biology of Mono (ADP-ribosyl) Transferases and Related Enzymes PDF
Preview ADP-Ribosylation in Animal Tissues: Structure, Function, and Biology of Mono (ADP-ribosyl) Transferases and Related Enzymes
ADP-RIBOSYLATION IN ANIMAL TISSUES Structure, Function,and Biologyof Mono (ADP-ribosyl) Transferases and Related Enzymes ADVANCES IN EXPERIMENTAL MEDICINE AND BIOLOGY Editorial Board: NATHAN BACK,State UniversityofNew YorkatBuf/alo IRUN R. COHEN, The Weizmann InstituteofScience DAVID KRITCHEVSKY, WistarInstitute ABEL LAJTHA,N. S. Kline Institutefor PsychiatricResearch RODOLFO PAOLETTI,UniversityofMilan Recent Volumes in this Series Volume 411 OXYGENTRANSPORTTOTISSUE XVIII Edited by Edwin M. Nemotoand Joseph C. LaManna Volume 412 MECHANISMS IN THE PATHOGENESISOF ENTERIC DISEASES Edited by Prem S. Paul, David H. Francis,and David A. Benfield Volume 413 OPTICAL IMAGINGOF BRAIN FUNCTION AND METABOLISM 2: Physiological BasisandComparisonto Other Functional Neuroimaging Methods Edited by Arno Villringerand Ulrich Dirnagl Volume414 ENZYMOLOGY AND MOLECULAR BIOLOGY OFCARBONYL METABOLISM 6 Edited by Henry Weiner, Ronald Lindahl, David W. Crabb,andT. 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ADP-RIBOSYLATION IN ANIMAL TISSUES Structure, Function, and Biology of Mono (ADP-ribosyl) Transferases and Related Enzymes Edited by Friedrich Haag Friedrich Koch-Nolte University Hospital Hamburg-Eppendorf Hamburg. Germany SPRINGER SCIENCE+BUSINESS MEDIA, LLC llbrlry of Congresl Cataloging-In-Publication Data AOP-rl~osylatlon In anl.al tissues structure. function. and biology of lono (ADP-rlbOSyll transferases anD relateD enZYles I eDiteD by Friedrich Haag, FriedriCh Koch-Nalte. p. CI. -- (Advances In exporl •• ntal ledlelne and ~Iology ; v. 419) -Proceedings of an InternatiOnal Workshop on the BiologIcal Slgnlflcanc, of Mono ADP-Ribosylatlon In Anl •• l Tissues. helo May 19-23. 1996. In Huburg, Geruny'--Lp. v,rso. Includes ~Ibllograpl"llcal referencu ind Index. ISBN 978-1-4613-4652-4 ISBN 978-1-4419-8632-0 (eBook) DOI 10.1007/978-1-4419-8632-0 I. ADP-rlbosylatlon--Congresses. I. Haag. Friedrich. 11. Koch -Nolte, FrIedrich. Ill. International HorkshOp on tl'le DialogIcal Significance of Mono ADP-RI~osylatIOn In Anin i TIssues (1996 H• • burg. Ger.any. lu. Series. [DNLM: I. Adenosine Diphosphate Rlbos"--.eta~oll'I--congresses. 2. NAD+ ...oP-R I bosy I transferase--.etabo I I u--congresses. HI A0559 v.419 1997 f au 57 A240B 19971 0P625.A29A346 1997 572·.7921--oc21 DNLMIOLC for Library of Congress 97-7429 Proceedings of an [nternational workshop on the Biological Significance of mono ADP-rioosy[ation in Anima[ Tissues, held May [9- 23, [996, in Hamburg. Germany [SBN 978-1-46[3-4652-4 o 1997 Springer Seicnce+Business Media New York Origina[[y published by Plenum Press, New York in 1997 Sol\cover reprint of the hardcover 1st OOilion 1997 htlp:/lwww.plenum.com [098765432 [ All rights reserved No pan of this book may be reproduced, siored in a relrieva[ system, or transmitted in any form or by any means. electronic, mechanical. photocopying, microfilming, recording, or otherwise, without wrinen permission from the Publisher PREFACE Although ADP-ribosylation has been known as a post-translational modification of proteins for approximately thirty years, the study ofendogenous mono-ADP-ribosylation in animal tissues has remained somewhat of an orphan field during this time. Until re cently, interest in the field has concentrated on two types ofphenomena: (I) poly-ADP-ri bosylation of nuclear proteins in eukaryotes as a mechanism possibly involved in DNA excision repair and (2) mono-ADP-ribosylation by bacterial enzymes, either as a toxic mechanism in eukaryotic host cells or as a reversible regulatory mechanism for control of nitrogen fixation. The identification of diphtheria, cholera, and pertussis toxins as mono(ADP-ribosyl)transferases and their subsequent purification and crystallization have shaped ourcurrent knowledge ofthe biology ofmono-ADP-ribosylation reactions and the structure-function relationships of the enzymes involved. In contrast, endogenous trans ferases ofanimal tissues escaped molecular cloning, and for a long time their biological relevance was merely postulated by analogy to theirbacterial cousins. The molecular characterization of the first mammalian mono(ADP-ribosyl)trans ferase from rabbit skeletal muscle, as well as the consequent realization that a well-studied surface membrane protein of T cells, RT6, is a mono(ADP-ribosyl)transferase, have changed this situation. With their genes at hand, the question ofthe significance ofthese enzymes in animal tissues can now be addressed more directly. The international work shop "Biological Significance ofMono-ADP-Ribosylation in Animal Tissues," held May 19-23, 1996, in Hamburg, was the first ofits kind and was felt by many members ofthe community to be a necessary focal point whose time was now due. The conference was held in the beautiful setting ofthe Elsa-Brandstrom-Haus, over looking the shores ofthe Elbe river in Hamburg-Blankenese, and attended by 70 scientists from Europe, North America, and Japan. It is an interesting historical anecdote that the first scientific conference to be held at this site was one ofthe early international work shops on ADP-ribosylation, organized twenty years ago by Helmuth Hilz, Professor emeritus ofthe Department of Physiological Chemistry and a special guest at this meet ing. Thirty-nine papers were presented by invited speakers, 22 as posters and short oral communications. Almost all ofthese are united in this volume, essentially arranged in the orderthey were presented at the conference. The first section deals with the lessons to be learned from the studies ofprokaryotic mono(ADP-ribosyl)transferases. In these enzymes, structure-function relationships have already been well established by crystallography and site-directed mutagenesis. These studies facilitate the prediction ofcatalytic residues ofthe eukaryotic transferases, gener ating hypotheses that can be tested experimentally by site-directed mutagenesis. The regu lation of the dinitrogenase reductase system in photobacteria also provides an attractive v vi Preface model for reversible regulation ofmetabolic functions by ADP-ribosylation in animal tis sues. The second section focuses on the structural and biochemical characterization ofthe eukaryotic transferases. In the forefront are the reports on the elucidation ofthe primary structure oftransferases from diverse vertebrate tissues and species. Transferase activity has been demonstrated also in fungi, although the enzyme(s) involved has/have not yet been cloned. Some ofthe cloned vertebrate enzymes have already been expressed in a re combinant form, and mutagenesis experiments have been conducted to test some ofthe structural hypothesesgenerated in the first section. Thethirdandfourth sectionsaddress the biological function ofmono-ADP-ribosyla tion in the immune and othersystems. Several reports sumup what is known to date about the biological significance of the RT6 T-cell mono(ADP-ribosyl)transferases. RT6 has been well studied over the years as a T-cell differentiation marker, especially in light of the observation that RT6 expression defects coincide with increased disease susceptibility in different animal models for autoimmune diseases. Thus, although its enzymatic activity has only recently been recognized, RT6 is the transferase whose gene structure has been the most extensively studied and the system in which hypotheses regarding possible dis ease association ofdefective transferases are most advanced. ADP-ribosylation reactions have been implicated in the modulation ofactivation ofnot only T cells, but also other cells of the immune system, including monocytes/macrophages and granulocytes. In skeletal and cardiac muscle, target proteins for ADP-ribosylation are being identified, leading to testable hypotheses as to the biological significance ofthese reactions. Regula tory effects of ADP-ribosylation have also been demonstrated in central and peripheral nervous tissue. In the latter case, interestingly, an association between a metabolic disor der (diabetes mellitus) and endogenous ADP-ribosylation could be found. Finally, exten sive work has gone into the characterization ofADP-ribosylation reactions in the context ofregulation ofcellulartransportprocesses. The fifth section attempts to shed some light on a puzzle that still impedes a clear understanding ofhow ADP-ribosylation works in animal cells. Although NAD+ is a clas sic intracellular metabolite, all vertebrate mono(ADP-ribosyl)transferases (and also ADP ribosyl cyclases) cloned to date are predicted to be localized extracellularly, the majority as GPI-anchored cell surface enzymes. Therefore, the cellular compartmentalization, dy namics, and interaction with signal transduction processes of GPI-anchored molecules havebeenaddressed. The sixth section examines the mechanisms and biological significance of other ADP-ribose transfer reactions, especially the production ofcyclic ADPR and related cal cium-mobilizing secondmessengersbyADP-ribosyl cyclases. Aspecial session ofthe conference wasdedicated to Prof. Heinz-GunterThiele, one ofthe pioneers ofresearch on the T-cell mono(ADP-ribosyl)transferase RT6, at the occa sion ofhis retirement. This session was highlighted by an eloquent pleaby Prof. Jonathan Howard, anotherone ofthe "fathers"ofRT6, to considerthe implications ofthe extensive polymorphism within the RT6 system when assessing its function, as this may point to ward a role ofRT6 within the context ofa defense system that needs to adapt to achang ingenvironment. We wish to express our sincere thanks to the Deutsche Forschungsgemeinschaft (DFG) and the many other groups whose generous financial supportmade this conference possible, as well as to our students and laboratory staff who worked hard to make the meetingarewardingexperience for all participants. Preface vii We believe that the present volume represents a condensation ofpresent knowledge ofmono(ADP-ribosyl)transferases and related enzymes and hope that it will fulfill its in tended function to stimulate and facilitate further research into the significance ofthese intriguingenzymes. Friedrich Haag Friedrich Koch-Nolte Hamburg. Germany ACKNOWLEDGMENTS Financial support for the conference was provided by the following sponsors: THE DEUTSCHEFORSCHUNGSGEMEINSCHAFT THE UNIVERSITY HOSPITAL HAMBURG-EPPENDORF ELIAS BIOTEST BOEHRINGER MANNHElM DIANOVA DYNAL SANDOZ SORVALL WILKE & WITZEL BECKMANN BECTON DICKINSON BYK SANGTEC PHARMACIA SIGMA SCHLEICHER & SCHUELL THE BINDING SITE The organizers thank the department secretary, Ms. Eva-Maria Hobbje; their gradu ate students Rickmer Braren, Katrin Firner, Martina Matthes, Stefan Rothenburg, and Kar sten Wursthorn; and their technicians Sandra Bauschus, Roman Girisch, Maren KOhl, and Cornelia Ritterfor theirsupport. The organizers thank theirsignificantothers for their understanding. ix CONTENTS INTRODUCTION I. Mono(ADP-Ribosyl)Transferasesand Related Enzymesin AnimalTissues: EmergingGene Families . FriedrichKoch-Nolte andFriedrich Haag 2. ADP-Ribose: AHistoricalOverview 15 Helmuth Hilz 3. ADP-RibosylarginineHydrolasesand ADP-Ribosyltransferases: Partnersin ADP-RibosylationCycles. ...................................... 25 Joel Moss, AnnaZolkiewska,andIanOkazaki MONO-ADP-RIBOSYLATION IN PROCARYOTES PlenaryLectures 4. Crystal StructureofDiphtheriaToxinBoundtoNicotinamideAdenine Dinucleotide 35 Charles E. Bell and David Eisenberg 5. SelectionofDiphtheriaToxin Active-Site Mutants inYeast: Rediscoveryof Glutamic Acid-148 asaKey Residue. ............................. 45 HaianFu, Steven R. Blanke,LarryC. Mattheakis, and R. John Collier 6. Identificationofthe Catalytic SiteofClostridial ADP-Ribosyltransferases 53 KlausAktories 7. AProposed Role for Protein: ProteinComplexesin the Regulationofthe ReversibleADP-RibosylationofDinitrogenaseReductase ... .......... 61 SandraK. Grunwald, YaopingZhang,CaleHalbleib,GaryP. Roberts, and PaulW. Ludden 8. ADP-Ribosylationand EarlyTranscriptionRegulationbyBacteriophageT4 71 Kai Wilkens, BerndTiemann,FernandoBazan,andWolfgangRuger xi xii Contents PosterReports 9. PertussisToxin: EntryintoCellsandEnzymaticActivity. ................... 83 AlielBayii, RuthLinnemann, LarsvonOlleschik-Elbheim,and M. AlexanderSchmidt 10. MembraneAnchoredSynthetic PeptidesasaTool forStructure-Function AnalysisofPertussisToxinand ItsTargetProteins. ................... 87 Lars vonOlleschik-Elbheim,Aliel Bayii,andM. AlexanderSchmidt II. EnhancedDegradationofStimulatoryG-Protein(Gsa)byCholeraToxinIs MediatedbyADP-RibosylationofGsa ProteinbutNotbyIncreased CyclicAMPLevels ............................................. 93 BukhtiarH. Shah MOLECULARAPPROACHESTOEUCARYOTIC MONO(ADP-RIBOSYL)TRANSFERASES PlenaryLectures 12. SequenceandStructuralLinksbetweenDistantADP-Ribosyltransferase Families. ..................................................... 99 1. FernandoBazanandFriedrichKoch-Nolte 13. MolecularCloningandCharacterizationoftheT-Cell Mono(ADP-Ribosyl)TransferaseRT6: Relationshipsto OthermADPRTs andPossibleFunctions .......................... 109 Heinz-GunterThiele,FriedrichHaag,andFriedrichKoch-Nolte 14. MolecularCloningandCharacterizationofaMono(ADP-Ribosyl)Transferase from HumanTestis 121 IsabelleLevy,Andre Pawlak,MarieGenevieveMattei,andGeorgesGuellaen 15. MolecularCloningandCharacterizationofLymphocyteand Muscle ADP-Ribosyltransferases 129 Ian1.Okazaki,Hyun-Ju Kim, andJoel Moss 16. MolecularCloningandCharacterizationofArginine-Specific ADP-Ribosyltransferasesfrom Chicken Bone MarrowCells. ........... 137 MakotoShimoyama,MikakoTsuchiya,NobumasaHara,Kazuo Yamada,and HarumiOsago 17. Purification,Characterisation,andMolecularCloningofaChickenErythroblast Mono(ADP-Ribosyl)Transferase 145 TerenceDavis,Jamal S. M. Sabir,ManoochehrTavassoli,andSydneyShall 18. MolecularCharacterisationofaFungalMono(ADP-Ribosyl)Transferase ....... 155 MarthaDeveze-Alvarez,JesusGarcia-Soto,and Guadalupe Martinez-Cadena
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