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NATO ASI Series
Advanced Science Institutes Series

A series presenting the results of activities sponsored by the NATO Science
Committee, which aims at the dissemination of advanced scientific and
technological knowledge, with a view to strengthening links between scientific
communities.

The Series is published by an international board of publishers in conjunction with
the NATO Scientific Affairs Division

A Life Sciences
B Physics

C Mathematical and
Physical Sciences

D Behavioural and
Social Sciences

E Applied Sciences

F Computer and
Systems Sciences

G Ecological Sciences
H Cell Biology
I Global Environmental

Change

NATo-peo DATABASE

Plenum Publishing Corporation
London and New York

Kluwer Academic Publishers
Dordrecht, Boston and London

Springer-Verlag
Berlin Heidelberg New York
London Paris Tokyo Hong Kong
Barcelona Budapest

The electronic index to the NATO ASI Series provides full bibliographical
references (with keywords and/or abstracts) to more than 30000 contributions
from international scientists published in all sections of the NATO ASI Series.
Access to the NATO-PCO DATABASE is possible in two ways:

- via online FILE 128 (NATO-PCO DATABASE) hosted by ESRIN,
Via Galileo Galilei, 1-00044 Frascati, Italy.

- via CD-ROM "NATO-PCO DATABASE" with user-friendly retrieval software
in English, French and German (© WTV GmbH and DATAWARE Technologies
Inc. 1989).

The CD-ROM can be ordered through any member of the Board of Publishers
or through NATO-PCO, Overijse, Belgium.

Series H: Cell Biology Vol. 51

Page 2

The ASI Series Books Published as a Result of
Activities of the Special Programme on
CELL TO CELL SIGNALS IN PLANTS AND ANIMALS

The books published as a result of the activities of the Special Programme are:

Vol. 1: Biology and Molecular Biology of Plant-Pathogen Interactions. Edited by J.A. Bailey. 1986.
Vol. 2: Glial-Neuronal Communication in Development and Regeneration.

Edited by H.H. Althaus and W. Seifert. 1987.
Vol. 3: Nicotinic Acetylcholine Receptor: Structure and Function. Edited by A. Maelicke. 1986.
Vol. 4: Recognition in Microbe-Plant Symbiotic and Pathogenic Interactions.

Edited by B. Lugtenberg. 1986.
Vol. 5: Mesenchymal-Epithelial Interactions in Neural Development.

Edited byJ.A. Wolff, J. Sievers, and M. Berry. 1987.
Vol. 6: Molecular Mechanisms of Desensitization to Signal Molecules.

Edited byT.M. Konjin, P.J.M. Van Haastert, H. Van der Starre, H. Van derWel,
and M.D. Houslay. 1987.

Vol. 7: Gangliosides and Modulation of Neuronal Functions. Edited by H. Rahmann. 1987.
Vol. 9: Modification of Cell to Cell Signals During Normal and Pathological Aging.

Edited By S. Govoni and F. Battaini. 1987.
Vol. 10: Plant Hormone Receptors. Edited by D. Kliimbt. 1987.
Vol. 11: Host-Parasite Cellular and Molecular Interactions in Protozoal Infections.

Edited by K.-P. Chang and D. Snary. 1987.
Vol. 12: The Cell Surface in Signal Transduction. Edited by E. Wagner, H. Greppin, and B. Millet. 1987.
Vol. 19: Modulation of Synaptic Transmission and Plasticity in Nervous Systems.

Edited byG. Hertting and H.-C. Spatz. 1988.
Vol. 20: AminoAcid Availability and Brain Function in Health and Disease. Edited by G. Huether. 1988.
Vol. 21: Cellular and Molecular Basis of Synaptic Transmission. Edited by H. Zimmermann. 1988.
Vol. 23: The Semiotics of Cellular Communication in the Immune System.

Edited by E.E. Sercarz, F. Celada, NA Mitchison, and T. Tada. 1988.
Vol. 24: Bacteria, Complement and the Phagocytic Cell. Edited by F.C. Cabello and C. Pruzzo. 1988.
Vol. 25: Nicotinic Acetylcholine Receptors in the Nervous System.

Edited byF. Celementi, C. Gotti, and E. Sher. 1988.
Vol. 26: Cell to Cell Signals in Mammalian Development.

Edited by SW. de Laat, J.G. Bluemink, and C.L. Mummery. 1989.
Vol. 27: Phytotoxins and Plant Pathogenesis. Edited by A. Graniti, A.D. Durbin, and A. Ballio. 1989.
Vol. 31: Neurobiology ofthe Inner Retina. Edited by R. Weiler and N.N. Osborne. 1989.
Vol. 32: Molecular Biology of Neuroreceptors and Ion Channels. Edited by A. Maelicke. 1989.
Vol. 33: Regulatory Mechanisms of Neuron to Vessel Communication in the Brain.

Edited by F. Battaini, S. Govoni, M.S. Magnoni, and M. Trabucchi. 1989.
Vol. 35: Cell Separation in Plants: Physiology, Biochemistry and Molecular Biology.

Edited by D.J. Osborne and M.B. Jackson. 1989.
Vol. 36: Signal Molecules in Plants and Plant-Microbe Interactions. Edited by B.J.J. Lugtenberg. 1989.
Vol. 39: Chemosensory Information Processing. Edited by D. Schild. 1990.
Vol. 41: Recognition and Response in Plant-Virus Interactions. Edited by R.S.S. Fraser. 1990.
Vol. 43: Cellular and Molecular Biology of Myelination.

Edited byG. Jeserich, H. H. Althaus, andT. V. Waehneldt. 1990.
Vol. 44: Activation and Desensitization ofTransducing Pathways.

Edited byT. M. Konijn, M. D. Houslay, and P.J. M. Van Haastert.1990.
Vol. 45: Mechanism of Fertilization: Plants to Humans. Edited by B. Dale. 1990.
Vol. 46: Parallels in Cell to Cell Junctions in Plants and Animals.

Edited by A. W. Robards, W. J. Lucas, J. D. Pitts, H. J. Jongsma, and D. C. Spray, 1990.
Vol. 50: Phytochrome Properties and Biological Action. Edited by B. Thpmas and C. B. Johnson, 1991.
Vol. 51: Cell to Cell Signals in Plants and Animals. Edited by V. Neuhoff and J. Friend, 1991.

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187

This process is called photomorphogenesis and requires the involvement of photorecep-
tor pigments. These absorb light and provide the initial biochemical signal to trigger the
plant's photo response.

In terms of cell signalling photomorphogenesis provides a context peculiar to plants
in which photoreceptors act as primary signals. Transduction of the photoreceptor sig-
nals along signalling pathways, on the other hand, almost certainly does not involve un-
ique mechanisms. The identification and characterization of photo receptors and elucida-
tion of their mechanism of action is a major goal of plant biochemists and an essential
part of the study of cell signalling in plants.

Phytochrome

A large number of photomorphogenetic responses are under the control of the
chromoprotein photoreceptor phytochrome. Phytochrome is found in all green plants in-
cluding algae, mosses and ferns. The protein exists as two photoisomers. One form (Pr)
has a characteristic absorbance spectrum with a major absorbance maximum ("-max) at
about 660nm and a secondary maximum at about 380nm. The other form (Pfr) has a "-max
at about 730nm and a secondary peak at about 400nm . When either form absorbs light
a series of photochemical and protein conformational changes is initiated leading within
milliseconds to the formation of the other photoisomer. For many responses red light at
about 660nm is the most effective part of the spectrum and the effect of red can be pre-
vented by a subsequent far-red irradiation at about 703nm. In such cases red, far-red
photoreversibility is frequently repeatable over several cycles of irradiation. This is under-
standable in terms of the photoreversible interconversions between Pr and Pfr as long as
it is assumed that Pfr is biologically active and Pr inactive. The following represents a
simple model for the phytochrome system.

Red light

Pr hv Pfr -----.~ Response
..
Far-red light

Under continuous illumination a dynamic photoequilibrium is established between Pr
and Pfr, but because Pr and Pfr have different absorbance characteristics the relative
proportions of the two forms varies depending on the spectral distribution of incident
light. Red light at 660nm establishes the maximum proportion of phytochrome as Pfr
(80-90%) whereas far-red light at 730nm will result in only about 3% as Pfr.

The net result of these photochemical properties is that phytochrome is uniquely
placed to serve as a molecular monitor of the light environment. To give two examples:
phytochrome is synthesised as Pr and in seedlings penetrating the soil the formation of
Pfr as light first impinges upon the plant acts as an early warning of microenvironmental
change. The plant responds by modifying its strategy from searching for light to maximis-
ing its absorbtion. Developmental emphasis shifts from shoot elongation to leaf expan-
sion coupled with switching on the synthesis of photosynthetic proteins and protective
pigments. This is achieved through the co-ordinated activation and deactivation of spe-
cific plant genes.

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188

Secondly, variation in the relative amounts of light energy in the red and far-red parts
of the spectrum is caused by vegetational shading. Consequential changes in the Pfr/P
total of shaded plants enable them to detect this shading. How the plant responds will
depend partly on the ecological strategy it uses for survival.

PHYTOCHROME CHARACTERISATION

Phytochrome genes

The cloning of Avena phytochrome cDNA clones by Peter Quail's group (7) represents
something of a watershed in phytochrome research. This enabled the sequence of the
protein to be deduced and resolved several outstanding controversies regarding its pro-
perties. It also made possible the regulation and autoregulation of its synthesis to be
characterised in detail.

Phytochrome cDNA clones were first isolated and characterised from Avena sativa
(3, 7). Restriction endonuclease site polymorphism between clones indicated that phyto-
chrome exists as a small gene family in this species. There are at least four members ex-
pressed. No clone was obtained with the complete coding region and analysis was
based on partial sequences. DNA sequence analysis of three of the classes showed a
98% squence similarity in the coding regions and 5' untranslated regions. Complete
sequences for two members of the gene family shows them to both have an open read-
ing frame of 3384bp. This equates to proteins 1128 amino acid residues long with molec-
ular masses of 124, 870 and 124, 949 Da. The attachment site for the tetrapyrrole chrom-
ophore was located at Cysteine-321.

Based on restriction endonuclease analysis, two classes of genomic clone were
isolated from Avena and one of these has been sequenced (8). This gene, designated
type 3, is approximately 5.9kbp long and contains six exons and 5 introns. The mRNA
coded for by this gene has a total length of 3781 nucleotides consisting of 142 nucleo-
tides of untranslated 5' sequence, 249 nucleotides of untranslated 3' sequence and 3390
nucleotides of amino acid coding sequence, including initiator and stop codons.

Subsequently cDNAs and genomic clones have been isolated from a number of
species. At the present time details have been published for phytochrome genes from
Cucurbita (9), Pisum (10) and Oryza (11). No overall pattern has yet emerged regarding
the organisation of phytochrome genes. It is claimed that only one copy of the phyto-
chrome gene is present in Pisum and Oryza, compared to four in Avena and at least two
in Cucurbita. Multiple transcripts have, however been detected in Avena, Cucurbita and
Pisum. In the latter case multiple transcripts are detectable by primer extension analysis
indicating that the differences lie in the length of the 5' untranslated sequence (10). Re-
solution of these apparent anomalies requires further work.

Comparison of phytochrome sequences from different species reveals about 65%
nucleotide and amino acid sequence similarity between monocot and dicot phyto-
chromes. Dicot phytochromes have a higher level of similarity at about 77% (12). Se-
quence conservation is not evenly distributed. Most of the amino-terminal two thirds of
the aligned polypeptide chains show localised regions with a high degree of similarity. A
very high degree of conservation is seen at the chromophore attachment site. A stretch
of 29 amino acids is shown to be entirely the same in Avena and Cucurbita at this part of
the molecule. This presumably reflects the highly constrained nature of the protein

Page 396

NATO ASI Series H

Vol. 21: Cellular and Molecular Basis of Synaptic Transmission.
Edited by H. Zimmermann. 547 pages. 1988.

Vol. 22: Neural Development and Regeneration. Cellular and Molecular Aspects.
Edited by A. Gorio, J. R. Perez-Polo, J. de Vellis, and B. Haber. 711 pages. 1988.

Vol. 23: The Semiotics of Cellular Communication in the Immune System.
Edited by E. E. Sercarz, F Celada, N. A. Mitchison, and T. Tada. 326 pages. 1988.

Vol. 24: Bacteria, Complement and the Phagocytic Cell.
Edited by F C. Cabello und C. Pruzzo. 372 pages. 1988.

Vol. 25: Nicotinic Acetylcholine Receptors in the Nervous System.
Edited by F Clementi, C. Gotti, and E. Sher. 424 pages. 1988.

Vol. 26: Cell to Cell Signals in Mammalian Development.
Edited by S. W. de Laat, J. G. Bluemink, and C. L. Mummery. 322 pages. 1989.

Vol. 27: Phytotoxins and Plant Pathogenesis.
Edited by A. Graniti, R. D. Durbin, and A. Ballio. 508 pages. 1989.

Vol. 28: Vascular Wilt Diseases of Plants. Basic Studies and Control.
Edited by E. C. Tjamos and C. H. Beckman. 590 pages. 1989.

Vol. 29: Receptors, Membrane Transport and Signal Transduction.
Edited by A. E. Evangelopoulos, J. P. Changeux, L. Packer, T. G. Sotiroudis,
and K. W. A. Wirtz. 387 pages. 1989.

Vol. 30: Effects of Mineral Dusts on Cells.
Edited by B. T. Mossman and R. O. Begin. 470 pages. 1989.

Vol. 31: Neurobiology of the Inner Retina.
Edited by R. Weiler and N. N. Osborne. 529 pages. 1989.

Vol. 32: Molecular Biology of Neuroreceptors and Ion Channels.
Edited by A. Maelicke. 675 pages. 1989.

Vol. 33: Regulatory Mechanisms of Neuron to Vessel Communication in Brain.
Edited by F. Battaini, S. Govoni, M.S. Magnoni, and M. Trabucchi. 416 pages. 1989.

Vol. 34: Vectors as Tools forthe Study of Normal and Abnormal Growth and Differentiation.
Edited by H. Lother, R. Dernick, and W. Ostertag. 477 pages. 1989.

Vol. 35: Cell Separation in Plants: Physiology, Biochemistry and Molecular Biology.
Edited by D. J. Osborne and M. B. Jackson. 449 pages. 1989.

Vol. 36: Signal Molecules in Plants and Plant-Microbe Interactions.
Edited by B. J. J. Lugtenberg. 425 pages. 1989.

Vol. 37: Tin-Based Antitumour Drugs. Edited by M. Gielen. 226 pages. 1990.

Vol. 38: The Molecular Biology of Autoimmune Disease.
Edited by A. G. Demaine, J-P. Banga, and A. M. McGregor. 404 pages. 1990.

Vol. 39: Chemosensory Information Processing. Edited by D. Schild. 403 pages. 1990.

Vol. 40: Dynamics and Biogenesis of Membranes.
Edited by J.A. F Op den Kamp. 367 pages. 1990.

Vol. 41: Recognition and Response in Plant-Virus Interactions.
Edited by R. S. S. Fraser. 467 pages. 1990.

Page 397

NATO ASI Series H

Vol. 42: Biomechanics of Active Movement and Deformation of Cells.
Edited by N. Akkafi). 524 pages. 1990.

Vol. 43: Cellular and Molecular Biology of Myelination.
Edited by G. Jeserich, H. H. Althaus, and T. V. Waehneldt. 565 pages. 1990.

Vol. 44: Activation and Desensitization ofTransducing Pathways.
Edited byT. M. Konijn, M. D. Houslay, and P. J. M. Van Haastert. 336 pages. 1990.

Vol. 45: Mechanism of Fertilization: Plants to Humans.
Edited by B. Dale. 710 pages. 1990.

Vol. 46: Parallels in Cell to Cell Junctions in Plants and Animals.
Edited by A. W. Robards, W. J. Lucas, J. D. Pitts, H. J. Jongsma, and D. C. Spray.
296 pages. 1990.

Vol. 47: Signal Perception and Transduction in Higher Plants.
Edited by R. Ranjeva and A. M. Boudet. 357 pages. 1990.

Vol. 48: Calcium Transport and Intracellular Calcium Homeostasis.
Edited by D. Pansu and F. Bronner. 456 pages. 1990.

Vol. 49: Post-Transcriptional Control of Gene Expression.
Edited by J. E. G. McCarthy and M. F. Tuite. 671 pages. 1990.

Vol. 50: Phytochrome Properties and Biological Action.
Edited by B. Thomas and C. B. Johnson, 1991.

Vol. 51: Cell to Cell Signals in Plants and Animals.
Edited by V. Neuhoff and J. Friend. 404 pages. 1991.

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