ADP-Ribosylation: Metabolic Effects and Regulatory Functions

246 Pages·1994·12.176 MB·English

by  Takashi Sugimura, Masanao Miwa (auth.), Joel Moss, Peter Zahradka (eds.)

ADP-RIBOSYLATION: METABOLIC EFFECTS AND REGULATORY FUNCTIONS
Developments in Molecular and Cellular Biochemistry
Series Editor: Naranjan S. Dhalla, Ph.D., FACC
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Springer-Science+Business Media, B.Y.
ADP-Ribosylation:
Metabolie Effects and
Regulatory Functions
Edited by
JOEL MOSS
Laboratory of Cellular Metabolism,
National Heart, Lung and Blood Institute, NIH,
Building 10, Room 5N-307
Bethesda, MD 20892, USA
and
PETER ZAHRADKA
Division of Cardiovascular Sciences,
St Boniface General Hospital Research Center,
351 Tache Avenue,
Winnipeg, MB R2H 2A6, Canada
Reprinted from Molecular and Cellular Biochemistry, Volume 138 (1994)
Springer Science+Business Media, B.V.
Library of Congress Cataloging-in-Publication Data
ADP-ribosylation: metabolic effects and regulatory functions / edited
by Joel Moss and Peter Zahradka.
p. cm. — (Developments in molecular and cellular biochemistry: 12)
ISBN 978-1-4613-6120-6 ISBN 978-1-4615-2614-8 (eBook)
DOI 10.1007/978-1-4615-2614-8
1. ADP-ribosylation. I. Moss, Joel. II. Zahradka, Peter,.
III. Series.
QP625, A29A347 1994
574,87'6-dc20 94-21849
CIP
ISBN 978-1-4613-6120-6
Printed on acid-free paper
All Rights Reserved
© 1994 Springer Science+Business Media Dordrecht
Originally published by Kluwer Academic Publishers 1994
Softcover reprint of the hardcover 1st edition 1994
No part of the material protected by this copyright notice may be reproduced or
utilized in any form or by any means, electronic or mechanical,
including photocopying, recording or by any information storage and
retrieval system, without written permission from the copyright owner.
Molecular and Cellular Biochemistry:
An International Journal for Chemical Biology in Health and Disease
CONTENTS VOLUME 138, No. 1-2, 1994
ADP-RIBOSYLATION: METABOLIC EFFECTS AND REGULATORY FUNCTIONS
Joel Moss and Peter Zahradka, guest editors
Preface
Dedication
Part I: Historical perspective
T. Sugimura and M. Miwa: Poly(ADP-ribose): Historical perspective 5
Part II: Poly(ADP-ribosyl)ation
A. Structure and enzymology ofpoly(ADP-ribose) polymerase
G. de Murcia, V. Schreiber, M. Molinete, B. Saulier, O. Poch, M. Masson, C. Niedergang and J.M. de Murcia:
Structure and function of poly(ADP-ribose) polymerase 15
K. Uchida and M. Miwa: Poly(ADP-ribose) polymerase: Structural conservation among different classes of animals
and its implications 25
R. Alvarez-Gonzalez, G. Pacheco-Rodriguez and H. Mendoza-Alvarez: Enzymology of ADP-ribose polymer synthesis 33
S. Yoshida and C.M.G. Simbulan: Interaction of poly(ADP-ribose)polymerase with DNA polymerase a 39
B. Polymer regulation
1. Laguex, G.M. Shah, L. Menard, H. Thomassin, C. Duchaine, C. Hengartner and G.G. Poirier: Poly(ADP-ribose)
catabolism in mammalian cells 45
F.R. Althaus, L. HOfferer, H.E. Kleckzkowska, M. Malanga, H. Naegeli, P.L. Panzeter and c.A. Realini: Histone
shuttling by poly ADP-ribosylation 53
C. Cellular functions
S. Chatterjee and N.A. Berger: Growth-phase-dependent response to DNA damage in poly(ADP-ribose) polymerase
deficient cell lines: basis for a new hypothesis describing the role of poly(ADP-ribose) polymerase in DNA
replication and repair 61
S. Shall: The function of poly (ADP-ribosylation) in DNA breakage and rejoining 71
M.E. Smulson: Poly(ADP-ribose) polymerase gene on chromosome lq: Early role in differentiation linked replication;
gene on human chromosome 13q: Marker of carcinogenesis 77
A. Burkle, M. Muller, I. Wolf and J.-H. Kupper: Poly(ADP-ribose) polymerase activity in intact or permeabilized
leukocytes from mammalian species of different longevity 85
P. Zahradka and L. Yau: ADP-ribosylation and gene expression 91
D. Poly(ADP-ribose) polymerase gene regulation
S.L. Oei, H. Herzog, M. Hirsch-Kauffmann, R. Schneider, B. Auer and M. Schweiger: Transcriptional regulation and
autoregulation of the human gene for ADP-ribosyltransferase 99
Part III: Mono(ADP-ribosylation)
A. ADP-ribosylation cycle
A. Zolkiewska, U. Okazaki and J. Moss: Vertebrate mono-ADP-ribosyltransferases 107
M. Tsuchiya and M. Shimoyama: Target protein for eucaryotic arginine-specific ADP-ribosyltransferas, 113
T. Takada, U. Okazaki and J. Moss: ADP-ribosylarginine hydrolases 119
P.W. Ludden: Reversible ADP-ribosylation as a mechanism of enzyme regulation in procaryotes 123
B. Cellular mono-ADP-ribosylation
W.J. Iglewski: Cellular ADP-ribosylation of Elongation Factor 2 131
T. Maehama, N. Sekine, H. Nishina, K. Takahashi and T. Katada: Characterization of botulinum C3-catalyzed ADP-
ribosylation of rho proteins and identification of mammalian C3-like ADP-ribosyltransferase 135
B.E. Ledford and G.H. Leno: ADP-rybosylation of the molecular chaperone GRP78IBiP 144
Part IV: Toxin mono-ADP-ribosylation
J. vanderSpek, L. Cosenza, T. Woodworth, J.C. Nichols and J.R. Murphy: Diphtheria toxin-related cytokine fusion
proteins: Elongation factor 2 as a target for the threatment of neoplastic disease 151
C.F. Welsh, J. Moss and M. Vaughan: ADP-ribosylation factors: a family of -20-kOa guanine nucleotide-binding
proteins that activate cholera toxin 157
K. Aktories: Clostridial ADP-ribosylating toxins: effects on ATP and GTP-binding proteins 167
I.J. Okazaki and J. Moss: Common structure of the catalytic sites of mammalian and bacterial toxin ADP-
ribosyltransferases 177
Part V: Inhibitors and activators of ADP-ribosylation
M. Banasik and K. Ueda: Inhibitors and activators of ADP-ribosylation reactions 185
Part VI: Derivation of proteins with ADP-ribose, NAD and their analogues
L.J. McDonald and J. Moss: Nitric oxide and NAD-dependent protein modification 201
E.L. Jacobson, D. Cervantes-Laurean and M.K. Jacobson: Glycation of proteins by ADP-ribose 207
R. Alvarez-Gonzalez: DeoxyNAD and deoxyADP-ribosylation of proteins 213
LJ. McDonald and J. Moss: Enzymatic and nonenzymatic ADP-ribosylation of cysteine 221
Part VII: Cyclic ADP-ribose, NAD hydrologis and ADP-ribose synthesis
H.C. Lee: Cyclic ADP-ribose: A calcium mobilizing metabolite of NAD+ 229
H. Kim, E.L. Jacobson and M.K. Jacobson: NAD glycohydrolases: A possible function in calcium homeostasis 237
N.J. Oppenheimer: NAD hydrolysis: Chemical and enzymatic mechanisms 245
Index to Volume 138 253
Molecular and Cellular Biochemistry 138: 1-2, 1994.
© 1994 Kluwer Academic Publishers.
Preface
Over a quarter of a century has passed since Paul Mandel and his associates first established that ADP-ribose is synthesized b
eucaryotic cells. During these 25 years, much has been accomplished in defining the basic biochemical and molecull
characteristics of ADP-ribosylation reactions and in identifying the cellular functions of this modification system. It is no'
obvious that two classes of post-translational modification, mono(ADP-ribosyl)ation and poly(ADP-ribosyl)ation, are distil
guishable in eucaryotes. The different metabolic and functional parameters associated with each reaction has led to
dichotomy within the field, with poly(ADP-ribose) being the domain of those predominantly interested in nuclear process{
and investigators of mono(ADP-ribose) generally examining cytoplasmic events. The recent discoveries of ADP-ribosylatio
factors and cyclic ADP-ribose, however, have expanded the scope of this discipline in ways previously unforeseen an
demonstrated that ADP-ribose can influence cellular events at any point between the plasma membrane and the nucleu
Within this context, ADP-ribose can be viewed as a participant in the receptor-mediated activation of second messengt
systems, ion flux mechanisms, membrane transport processes, chromatin organization and nucleic acid metabolism.
Considering the current interest in cellular regulation and intracellular signalling systems, it is surprising that the contributio
of ADP-ribosylation reactions to the modulation of a variety of specific cell processes, in parallel with other post-translationl
modifications such as phosphorylation, has not been generally recognized. While it was not feasible to cover all aspects (
ADP-ribosylation, the thirty-one articles contained in this volume should provide a valuable overview of recent progress in th
field within the context of cell control mechanisms. For the convenience of the reader, the various topics have been groupe
into several sections: (a) poly(ADP-ribosyl)ation, (b) mono-ADP-ribosylation, (c) toxin mono-ADP-ribosylation, (d) inhibitor
and activators, (e) protein modification with ADP-ribose and its analogues, and (f) non-modification forms of ADP-ribose. Th
contents of the individual chapters reflect the ideas of the contributors, many of whom have spent their careers attempting t
resolve the biological functions of ADP-ribosylation. We hope that this publication will serve as a useful reference for thos
investigators that are new to the area as well as those who are actively studying ADP-ribosylation.
Dedication
This book is dedicated to Paul Mandel (1908-1992), a dedicated scientist and pioneer, whose laboratory was among the first t
identify ADP-ribosylation as an essential cell process and who continued to be a leader in the field.
2
Dr. Paul Mandel
(1908-1992)
who pioneered the studies of ADP-Ribolysation
PART I
HISTORICAL PERSPECTIVE
Molecular and Cellular Biochemistry 138: 5-12, 1994.
© 1994 Kluwer Academic Publishers.
Poly(ADP-ribose): Historical perspective
Takashi Sugimura 1 and Masanao Miwa2
I National Cancer Center, Tsukiji 5-chome, Chuo-ku, Tokyo J 04 Japan,2 Department of Biochemistry, Institute of Medical
Sciences, The University of Tsukuba, Tsukuba, Ibaraki 305, Japan
Abstract
The early historical background of the discovery ofpoly(ADP-ribose) and the following development of science on poly(ADP
ribose) are reviewed. Fundamental knowledge on the natures of poly(ADP-ribose), poly(ADP-ribose) polymerase and en
zymes degrading poly(ADP-ribose) are summarized with brief description on the methodology for their purification and
characterization. Future prospect of research on biological significance of poly(ADP-ribose) has also been discussed briefly.
(Mol Cell Biochem 138: 5-12, 1994)
Key words: discovery of poly(ADP-ribose), phosphoribosyl-AMP( <p-ADP-ribose), poly(ADP-ribose) polymerase,
phosphodiesterases, poly(ADP-ribose) glycohydrolase, branched structure of poly(ADP-ribose)
Initiation of studies on poly(ADP-ribose)
pected that the acid-insoluble product was poly(A). But Dr.
in the laboratory of Dr. Paul Mandel
Doly, who joined Dr. Mandel's group in the early phase of
the study, told me that they soon realized that the product
Studies on the ADP-ribosylation reaction have two differ might not be poly(A), and they reported data on the nature
ent origins. One was the finding by the late Dr. Paul Mandel of the product in 1966 [3].
in Strassbourg in 1963 that poly(ADP-ribose) is formed in Studies on poly(ADP-ribose) were also initiated in the
mammalian cell nuclei [I]. The other was the finding by National Cancer Center, Tokyo, by our group [4]. Using a
Dr. R.J. Collier and Dr. A.M. Pappenheimer in 1964 [1] nuclear preparation from rat liver, we confirmed the obser
that NAD was required for inhibiting protein synthesis in a vation by Dr. Mandel's group that NMN greatly enhanced
cell-free system by diphtheria toxin which led later to the the formation of acid-insoluble material from [I4C-ade ]ATP.
discoveries of mono(ADP-ribosyl)ation reactions of cyto Our studies were motivated by the idea that the biosynthesis
plasmic and membrane proteins of mammalian cells by bac of high-molecular weight compounds, such as RNA and
terial toxins. poly(A) could be regulated by allosteric effectors of low
In this chapter, the historical background of the discov molecular weight compounds, such as a nucleotide, NMN.
ery and development of the early stage of science on We suspected that abnormality of a control regulatory sys
poly(ADP-ribose) is described. The prospect for the future tem such as this might be related to autonomous growth of
of science on poly (ADP-ribose) will be briefly mentioned, cancer cells.
but avoidance of any overlapped descriptions with those in We confirmed that the product was hydrolysed by snake
other chapters will be intended. venom phosphodiesterase, as reported by Dr. Mandel's
The first report on poly(ADP-ribose) formation by Drs. group. However, we found that the product was resistant in
P. Chambon, 1. Weil and P. Mandel was published in 1963 alkaline conditions under which poly(A) should be
[I]. They found that the incorporation of C4C-adenine) hydrolyzed to adenosine 3'-monophosphate [4--6]. Further
labeled ATP into the acid-insoluble fraction by a nuclear more, on paper chromatography, the mobility of the prod
preparation from chicken liver was enhanced 1,000 times uct, with an [14C]adenine moiety, hydrolized, by the snake
5r
by nicotinamide mononucleotide (NMN). At first, they sus- venom phosphodiesterase was different from that of 4C-
Address for offprints: T. Sugimura, National Cancer Canter, Tsukiji 5 Chome, Chuo-ku, Tokyo 104, Japan