Plant Physiol. Biochem.

38 (2000) 647−655
© 2000 Éditions scientifiques et médicales Elsevier SAS. All rights reserved
S0981942800011785/REV

Review
Plant programmed cell death: A common way to die
Antoine Danon, Valérie Delorme, Nathalie Mailhac, Patrick Gallois*

Laboratoire génome et développement des plantes, université de Perpignan (CNRS, UMR 5096), 52, avenue de Villeneuve,
66860 Perpignan cedex, France

Received 2 February 2000; accepted 7 June 2000

Abstract – In the last few years programmed cell death in plants inspired many studies in development and environmental
stresses. Some of these studies showed that hallmarks of animal programmed cell death were found at cellular or molecular level
in plant cells in different experimental systems. Additionally the effect of over-expression in plants of animal genes implicated
in programmed cell death has been tested, and some plant homologues of these genes have been found. This suggests that,
despite some differences, plants and animals could share at least some common components of a core mechanism used to carry
out programmed cell death in eukaryotes. In this review, we will concentrate on the last findings that suggest similarity between
plant programmed cell death and its better known counterpart in animals. © 2000 Éditions scientifiques et médicales Elsevier
SAS

apoptosis / caspases / DNA ladder / necrosis / plants / programmed cell death / TUNEL

bp, base pair / HR, hypersensitive reaction / PCD, programmed cell death / PARP, poly (ADP-ribose) polymerase /
TUNEL, terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling

1. INTRODUCTION of the processes of development and defence mecha-

In animal development, a genetically controlled cell
death, termed programmed cell death (PCD), occurs at
different stages of growth, for example to eliminate
cells between developing digits or degeneration of
neurones that fail to form proper cellular connections.
Some cells also die during the organism’s life cycle to
regulate the size of distinct cell population in tissues.
Additionally when cells are confronted with environ-
mental stresses, they can either be destroyed acciden-
tally (murder), or can self-destruct using an active
mechanism (suicide). This depends on the stress type
or intensity. Inappropriate programmed cell death is
implicated in several human diseases such as Alzhe-
imer’s, Parkinson’s, AIDS or cancers (reviewed in
[49]).
In plants, it has been known for some time that a
genetically controlled cell death plays a role in some
* Correspondence and reprints: fax +33 4 6866 8499;
e-mail gallois@univ-perp.fr
nisms. For example lesion-mimic mutants, where a
localised cell death is triggered due to a genetic defect,
are a good illustration of the concept. Several studies
of plant cell death have been carried out to elucidate
the underlying molecular mechanism. Either of two
strategies has been used. First, molecular data can be
obtained using mutant studies or classical screening
approaches. Second, it is tempting to draw a parallel
between plant and animal cell death, so researchers
looked for the hallmarks currently used in animal
studies to discriminate between programmed and acci-
dental cell death, and for plant homologues of animal
genes implicated in programmed cell death.
The involvement of cell death in different aspects of
the plant life cycle has already been reviewed [38],
including the death response to plant pathogen attack
and its specific signalling (e.g. salicylic acid, reactive
oxygen species, etc.) [30, 39]. Identifying ancestral
components in plant PCD is crucial to fully understand
this process. Therefore in this paper, we will concen-
trate on reporting the latest findings concerning the
similarities between plant cell death and animal PCD.
This will show that in plants the research in the field of
PCD is at a turning point.
648 A. Danon et al. / Plant. Physiol. Biochem. 38 (2000) 647–655
2. APOPTOSIS AND PROGRAMMED CELL
DEATH IN ANIMALS
Apoptosis was originally defined in 1972, on the
basis of specific morphological changes occurring
during a genetically controlled cell death initiated by a
variety of environmental stimuli [24]. These cytologi-
cal criteria were first described to discriminate a form
of cell suicide from an accidental cell death termed
necrosis. In short, apoptosis begins with cell shrinkage
and chromatin condensation. Then, fragmentation of
the nucleus and ultimately of the entire cell occurs,
giving apoptotic bodies (nucleus fragments surrounded
by cell material and included in plasma membrane
fragments), which are then phagocytosed. This mor-
phological pattern in death constitutes a set of hall-
marks used to recognise apoptotic cells from others at
a cytological level.
It is only years later that some knowledge at the
molecular level was acquired. Each newly discovered
step was successively incorporated in a cell suicide
pathway under the name of programmed cell death
(PCD). This term implies the activation of a genome-
encoded biochemical pathway, leading in most cases
to the apoptotic morphological changes. The first
major molecular event described was a specific pattern
of genomic DNA cleavage, resulting in a DNA ladder
detected using electrophoresis in agarose gel. Typi-
cally the ladder ‘rungs’ are multiples of 180 bp, due to
internucleosomal excision of chromatin fragments by
an endonuclease [56]. The detection of this DNA
ladder is still currently used to distinguish at the
molecular level apoptosis from necrosis. In the latter,
genomic DNA degradation occurs randomly and results
in a smear detected when the DNA is separated on
agarose gel [23]. Alternatively, digested DNA in nuclei
can be detected using an in situ method called terminal
deoxynucleotidyl transferase-mediated dUTP nick end
labelling reaction (TUNEL), which detects free 3’-OH
DNA breaks [16].
The first apoptotic gene (BCL-2) was discovered at
the beginning of the nineties and was shown to be a
suppressor of apoptosis [19]. Other genes of the BCL-2
family were subsequently found on the basis of sequence
similarities and physical interactions. This gene family
is now composed of members suppressing apoptosis
(BCL-2, BCL-xL, MCL-1) or activating members (BAX,
BAK, BAD, BCL-xS) [40]. The best-described involve-
ment of the bcl-2 protein family is at the mitochondrial
membrane level. There, positive and negative regula-
tors determine whether an irreversible molecular cas-
cade ending in apoptosis is initiated [18]. This phase
begins with the release of different factors from
mitochondria (cytochrome c, APAF-1, AIF), which
activate a family of proteases. All the members of this
protease family possess a cysteine in their catalytic site
and cleave specifically after an aspartic acid residue,
hence the classification of these proteases under the
common name of caspases (cysteine dependent aspar-
tate specific proteases) [46]. Some of these caspases
are executioners of apoptosis and cleave several pro-
teins important for cell integrity (e.g. poly (ADP-
ribose) polymerase (PARP), lamins, gelsolin, etc.).
Destruction of these key substrates leads to the mor-
phological changes described earlier and to cell death.
In particular, the protein inhibitor (ICAD) of the
caspase-activated DNAse (CAD) is cleaved, and CAD
activation specifically causes the internucleosomal
cleavage of genomic DNA typically found in apoptosis
[12].
3. ANIMAL HALLMARKS OF APOPTOSIS
AND PCD DETECTED IN PLANT CELL
DEATH
In animal biology, the terms apoptosis and PCD
have variable meanings depending on the researchers
[48, 49]. We have chosen in this paper to use strict
definitions as proposed in Vaux and Korsmeyer [48,
49]. We restrict apoptosis to the morphological phe-
notype observed in some forms of animal PCD.
Although we know that for some researchers PCD
means developmental cell death, we restrict PCD to
cell death for which a genome-encoded biochemical
pathway has been shown to lead to cell demise and this
independently of the morphology of the dying cell. It
should be noted that the term physiological cell death
has also been proposed to rationalise the study of cell
death [48, 49]. It applies when a particular cell death is
not (yet) attributed to either apoptosis or PCD. Physi-
ological cell death can be cell-autonomous or non-cell-
autonomous [48, 49] (figure 1). As an example, the
elimination of suspensor cells has often been described
as a PCD event, part of embryo development. But to
date, there is no description of genome-encoded bio-
chemical pathway or of specific PCD or apoptosis
hallmarks. It could therefore be referred to as a case of
physiological cell death.
One current question in the study of PCD in plants
is to what extent hallmarks of apoptosis and of animal
PCD can be found.
 A. Danon et al. / Plant. Physiol. Biochem. 38 (2000) 647–655
Figure 1. Schematic representation of the different possible pathways
and hallmarks associated with cell death, as defined in animals.
(——), Active process; (- - -), passive process.
3.1. Cell and nucleus morphology during plant
PCD: an apoptotic-like phenomenon
In the last few years and due to the new interest in
a possible apoptotic-like phenomenon existing in plants,
morphological changes have been investigated during
plant PCD. Only some are similar to those reported in
animal apoptosis. Condensation and shrinkage of the
cytoplasm and nucleus have been described in carrot
cell culture, after cell death induced by heat shock
[28]. Fragmentation of the nucleus coupled with posi-
tive TUNEL labelling has been reported in cell death
induced by a pathogen toxin or UV-C radiation [7, 51].
In the latter case, the pattern of nucleus fragmentation
has been proposed to be divided into three classes.
DNA fragmentation happens in morphologically nor-
mal nuclei (round shaped), in crescent shaped and in
fragmented nuclei. In parallel, a gradient of chlorophyl
content was observed, going from high in cells with
intact nuclei to non-detectable in cells with fragmented
nuclei [7]. Whether this reflects a time course has not
been proven. Crescent shaped nuclei have also been
described during cell death induced by TMV, using
electronic microscopy [31]. Further studies will pos-
sibly validate the presence of crescent shaped nuclei as
a cytological marker of PCD in plants.
At the very end of animal apoptosis, apoptotic
bodies are formed and phagocytosed. Morphologically
similar apoptotic bodies have not been shown to form
during plant cell death. These bodies may be absent in
plant PCD because they are functionally irrelevant due
to the absence of possible phagocytosis by adjacent
cells in the presence of a cell wall. Instead the plant
649
pathway might involve autolysis. So, if using a strict
morphological definition, the term of apoptotic-like
phenomenon in plants should be used instead of
apoptosis since some of the terminal hallmarks of
animal apoptosis are absent.
3.2. Animal hallmarks of PCD in plants
Here we specifically summarise findings that sug-
gest the existence of animal PCD hallmarks in plants.
In addition to the often described DNA ladder, there is
other molecular evidence, definitive or not, that points
to a conservation of at least some steps of the animal
core mechanism of PCD.
3.2.1. The DNA ladder
The easiest animal PCD hallmark that can be
investigated in a plant system is the DNA ladder. In
animals, it is a very specific hallmark of PCD, whereas
in necrosis, DNA degradation is random and results in
a smear. It should be noted that the absence of a DNA
ladder does not rule out PCD since in some instances
of PCD, cleavage of the genomic DNA in 50-kb
fragments has been reported [31]. Detection of a smear
of DNA fragments however rules out PCD and implies
a passive death. In plants, DNA ladders have been
reported in different situations during development:
death of monocot aleurone layer [53] and endosperm
[62], senescence of petal, carpel tissue and leaves [36,
37, 61] or during anther development [52]. It has also
been reported after induction of death using different
stresses such as: cold [25], nutrient deprivation [5],
salt or D-mannose stresses [21, 43], UV radiation [7]
and during death induced by pathogens or a pathogen
toxin [33, 41, 51]. A recent paper brings a word of
caution, pointing out that improper DNA extraction
conditions may lead to artefactual DNA laddering
[13].
DNA fragmentation corresponding to the DNA
ladder can be detected in situ using the TUNEL
reaction, which labels the free 3’-OH DNA extremi-
ties. The TUNEL reaction is considered as a good
specific criterion of death by PCD in animals. It should
be noted that in plant studies, high temperature treat-
ments of suspension cells have been reported to induce
necrosis and that the necrotic cells are TUNEL posi-
tive [28]. This could be explained by the fact that
random DNA digestion occurs at the end of the
necrotic process. Moreover authors using plant tissue
have reported that sample preparation including fixa-
tion, embedding and sectioning, can cause sufficient
nicking of nuclear DNA to produce false TUNEL
650 A. Danon et al. / Plant. Physiol. Biochem. 38 (2000) 647–655
positive nuclei [51, 55]. Nevertheless the TUNEL
reaction protocols have now been adapted to plant
cells to eliminate artefacts thus allowing the detection
of nuclei with fragmented DNA that occurred in vivo
[51]. Additionally the fixation protocol is simpler
when using a protoplast or cell culture population and
has not been reported to induce false TUNEL positive
labelling. So on the whole the TUNEL reaction is more
specific to PCD when associated with time course
data, than other death markers such as fluorescein
diacetate (FDA) or Evan’s Blue. The latter two label
any dying cell without specificity with regards to
apoptosis or necrosis and results should be interpreted
carefully. In conclusion, to use TUNEL labelling or a
cell death marker as a marker of PCD in a particular
plant system, it is prudent to back up the results, at
least initially, with the detection of a genomic DNA
ladder or of other typical biochemical markers (see
below).
3.2.2. Early PCD hallmarks
In animals, one of the earliest events that occurs
after PCD induction is the loss of cell membrane
asymmetry. This is made visible by the translocation
of phosphatidylserine on the cell outer membrane. It
can be measured using Annexin V, which binds pref-
erentially to negatively charged phospholipids. When
death was induced by camptothecin using either tobacco
or human cells in a similar experiment, Annexin V
binding to the outer membrane could be detected [35].
This detection of Annexin V before DNA break
detection using the TUNEL reaction suggests a com-
mon phenomenon in animal and plant cell death.
Another early specific feature of animal PCD is
chromatin condensation [54]. This has also been
detected by flow cytometry during camptothecin-
induced death in tobacco before DNA fragmentation,
in a manner closely related to that which occurs in
mammalian cells [34].
3.2.3. Clues which implicate cytochrome c
In animal cells, inactive caspases are present in the
absence of cell death induction. In a well-characterised
example, it is only after an apoptotic stimulus that a
first caspase (caspase 9) is activated by factors released
from mitochondria (cytochrome c, APAF-1, AIF). This
activated caspase is the starting point of an activation
cascade of other caspase family members [18]. Thus,
release of cytochrome c from intact mitochondria is
another feature of PCD in animals. A specific release
of cytochrome c from intact mitochondria has been
described in cucumber cotyledon undergoing pro-
grammed cell death [4]. A release of cytochrome c in
the cytosol after a D-mannose or a menadione lethal
treatment has also been shown [43, 45]. Using an in
vitro system containing tobacco cytosol extract and
mouse nuclei, fragmentation of DNA could not be
induced by adding menadione in the absence of
mitochondria but adding exogenous cytochrome c did
induce it [45]. This strongly suggests a conservation of
the role of cytochrome c in plant PCD. However, a
definite proof would be an induction of PCD following
a cytochrome c injection in a plant cell.
3.2.4. Caspase-like activities in plants
Up till now, the caspase family in animals is
composed of twelve different proteases classified in
three phylogenetic groups: ICE, ICH1 and CPP32. All
these caspases have in common a highly conserved
catalytic site, a stringent substrate specificity to cleave
after an aspartic acid residue and a requirement for at
least four amino acids N terminal to the cleavage site
[15]. It is possible to classify these caspases on the
basis of their affinity for different substrates including
two tetrapeptides in particular: DEVD (ICH1 and
CPP32) and YVAD (ICE caspase). The different affini-
ties can be measured using fluorogenic or colorimetric
peptide substrates. Corresponding caspase activity can
be blocked with the same peptide substrates coupled
with an aldehyde (CHO: reversible inhibitor) or a
methylketone radical (CMK, FMK: irreversible inhibi-
tor). Recently in plants, caspase-like activities have
been measured during hypersensitive reaction (HR)
cell death [9]. The results show induction of a
YVADase activity, whereas no DEVDase activity was
detected. Surprisingly both inhibitor peptides (DEVD
and YVAD) were efficient in blocking the HR and the
YVADase activity. Encouragingly, none of the classi-
cal protease inhibitors could suppress the HR or the
YVADase activity. Different results were found during
the plant response to UV-C radiation, where both
caspase inhibitors can prevent DNA digestion detected
by TUNEL reaction, and where a UV-C inducible
DEVDase activity, but no YVADase activity, was
found (Danon and Gallois, unpubl.).
3.2.5. Cleavage of the poly(ADP-ribose)
polymerase (PARP)
Another feature of animal PCD is the cleavage of
key proteins by caspases. PARP is among the first
target proteins shown to be specifically cleaved by
caspases [27]. PARP is believed to be involved in the
regulation of repair of DNA strand breaks and in cell
 A. Danon et al. / Plant. Physiol. Biochem. 38 (2000) 647–655
recovery from DNA damage [8]. Even if the role of the
early PARP cleavage in animal PCD is not established,
it has been proposed that the products of this cleavage
could contribute to the process of self-destruction of
the cell [11]. In soybean cell culture, it has been
recently reported that PARP inhibitors or PARP over-
expression could respectively inhibit or activate the
rate of cell death induced by H2O2, depending on the
intensity of the death stimulus [3]. Despite the fact that
the authors have not reported a DNA ladder, these
results could indicate that, as in animals, the PARP
protein could also participate in the death mechanism
in the event of irreparable DNA damage [11]. Addi-
tionally, it has been reported that a 116-kDa protein
reacting with a PARP antibody is cleaved into a
84-kDa fragment during menadione induced PCD in
tobacco protoplasts [45]. This cleavage could be sup-
pressed using caspase activity inhibitors. This is simi-
lar to the cleavage of PARP described in animal
apoptotic cells.
4. PLANT HOMOLOGUES OF ANIMAL
GENES IMPLICATED IN APOPTOSIS
In animals, different kinds of genes have been found
as either inducing (BAX, caspases) or inhibiting (BCL-2)
programmed cell death [40]. Up till now cloning of
plant homologues of such key animal gene families
has not been reported. Recently a functional test has
been carried out expressing the murine BAX gene in
tobacco. This induces a cell death with HR hallmarks
[26]. PCD hallmarks have however not been reported.
It should be noted that the same type of results were
found in yeast [59], but surprisingly in this case, the
sequence of the whole genome did not reveal any
putative BAX homologues. The lethal effect of the
expression in plants of the animal BAX protein could
be simply due to its ability to make pores in the
mitochondrial membrane and may not involve any
regulatory function. So far the lethal over-expression
of an animal BAX gene is therefore not sufficient to
prove that a homologue exists in plants. Antibodies
against human BCL-2 can detect an epitope in tobacco
extracts using western blot analysis. Additionally immu-
nocytochemical studies suggested a localisation in
mitochondria, plastids and nuclear membranes as it
could be expected from animal data [10]. Neverthe-
less, the question of the existence of a BCL-2 homo-
logue in plants remains to be established, since cloning
of the corresponding sequence has not yet been reported.
Recently, a mammalian suppressor of PCD, Bcl-XL,
651
was over-expressed in tobacco plants [29]. Bcl-XL
expression confers a protection against UV or paraquat-
induced cell death. It disturbs the HR cell death in
pathogen-infected leaves and thereby allows spread of
the pathogen. Similar disturbance of the HR is also
observed by over-expressing Ced-9, the C. elegans
homologue of Bcl-XL. This indicates that animal
suppressors can function in inhibiting cell death in
plants.
Bax-Inhibitor I (BI-1) is a new animal suppressor
and has plant homologues. BI-1 is able to suppress cell
death induced by BAX over-expression in both yeast
and animal cells [59]. An Arabidopsis homologue,
AtBI-1, was identified from the genome sequencing
project. The identity level initially reported is low
(29 %) due to inaccurate computer prediction of puta-
tive exons in this particular gene. Once this is taken
into account, the identity level reaches 37.5 % (N.
Mailhac, unpubl.). Nevertheless, a death suppressor
function of the plant homologue remains to be estab-
lished in plant cells.
Plant homologues of the Defender against Apoptotic
Death 1 (DAD1) gene have been reported. DAD1 has
been discovered in hamster cells where the corre-
sponding mutant cell line dies via apoptosis [32]. The
suppressor function of this protein was further sug-
gested in Caenorhabditis elegans, where its over-
expression protects some of the cells destined to die by
apoptosis during development [44]. At least two A.
thaliana homologues have been found, and the trans-
formation of the mutant hamster cell line with one of
them, demonstrates that the function of the protein is
conserved between plants and animals [14]. Other
experiments have shown that DAD1 is a subunit of the
mammalian oligosaccharyltransferase complex [22].
In mice, over-expression of DAD1 does not have any
protecting function against apoptosis but affects cell
cycle [20]. All these results together make the role of
this gene in animal apoptosis unclear, whereas its
putative suppressor role in plants is still not estab-
lished.
A. thaliana NADPH oxidoreductases are homolo-
gous to PIG3 (P53 Induced Gene). It has been recently
demonstrated that PIG3 is tightly correlated with
p53-mediated apoptosis in cancer cells [50]. No such
function has yet been assigned to the plant homo-
logues.
Aside from whole gene similarity, database searches
have identified several motifs of similarities between
CED-4 and APAF-1, which regulates cell death in
animal, and proteins encoded by resistance genes
regulating HR in plants. The conserved domain has
652 A. Danon et al. / Plant. Physiol. Biochem. 38 (2000) 647–655
been coined NB-ARC [47]. This interesting homology
awaits further experiments to shed light on its physi-
ological significance.
5. CONCLUSION
The emerging picture is that, despite differences, a
degree of conservation exists between plants and
animals in the PCD process. The case of cell death
induced by HR against pathogen attack is an illustra-
tion of the fact that some components of animal PCD
are also relevant to plant PCD. The HR process
includes the induction of the death of a few cells
limited to the infection site. Lesion-mimic mutants for
which a similar localised cell death is triggered vali-
date the concept of a genetically controlled cell death
in plants (reviewed in [30, 39]). Interestingly, some
animal PCD hallmarks, such as DNA ladder or caspase-
like activities, have also been described after HR
induction [9, 33, 41, 51].
Figure 2 shows the specific apoptotic and PCD
hallmarks defined in animals that have also been
described in plants. One of the simplest hallmarks
found in many situations in plants is the DNA ladder.
When demonstrated in a specific aspect of the plant
life cycle, this feature implies the occurrence of a
controlled cell death. This is because a DNA ladder is
the product of chromatin digestion by nuclease(s),
without concurrent protease activities (no histone diges-
tion). Concurrent nuclease and protease activity would
result in the appearance of a DNA smear on agarose
gel [57]. Therefore, a DNA ladder suggests that cell
structures, such as vacuoles or lysosomes, are pre-
served at least during part of the cell death process.
Even if some cloned cysteine proteases have been
described as potentially playing a role in a PCD
response in plants [42, 58], no caspase homologues
have yet been reported in plants. As mentioned earlier,
animal caspases are characterised by both a very
conserved catalytic site and an affinity for specific
target sequences such as DEVD or YVAD. It has been
possible to measure the corresponding DEVDase and
YVADase activities recently in plants, and to specifi-
cally inhibit them. Moreover DEVDase and YVADase
inhibitions both have a physiological effect on HR and
UV-C response by inhibiting PCD ([9]; Danon and
Gallois, unpubl.). DEVDase and YVADase activities
have not been detected together in the same PCD
response (YVADase in HR and DEVDase after UV
radiation), suggesting at least two different pathways
for PCD in plant cells. These results suggest a role for
Figure 2. Chosen examples of treatments triggering different animal
or plant PCD hallmarks in plant cell. Question marks indicate events
that have been shown in animals and have not been detected in plants.
DEVDase and YVADase in plants. Cloning of the
enzymes corresponding to these activities will show
whether their sequences present similarities with cys-
teine proteases making them true caspases.
Some of the specific morphological changes of
animal apoptosis occur in plants [7, 31, 51], but
apoptosis has been defined using cytological criteria
that include cell fragmentation and phagocytosis of the
remaining apoptotic bodies [24]. The fact that these
two criteria have not been described in plants makes
the term apoptosis unsuitable to qualify plant PCD at
the morphological level, so the term apoptotic-like
should be used. It would be of interest to demonstrate
whether nuclear fragmentation is or not the last nucleus
stage during the time course of nuclear morphological
changes occurring in plant PCD. It would also be very
interesting to know how plants dispose of the cell
corpse, this being one of the expected differences
between plants (no phagocytosis due to presence of a
cell wall) and animals.
An evolutionary point of view can also be used to
support the idea of some conservation of PCD molecu-
lar mechanisms between the plant and animal king-
doms. We know that in animals the mitochondrion is a
key organelle from where PCD execution is triggered.
The ancestor of the mitochondria is thought to be an
α-proteobacterium that has been captured by a proto-
eukaryotic host [17]. A hypothesis concerning the
central role of mitochondria in PCD execution is that
the molecular regulation of self-destruction derives
from a prokaryotic defence mechanism present in the
ancestor of mitochondria [1]. In this context, it has
 A. Danon et al. / Plant. Physiol. Biochem. 38 (2000) 647–655
been reported that some prokaryotes and some unicel-
lular eukaryotes such as Trypanosoma cruzi or Dicty-
ostelium sp. can also die by PCD [2, 6, 60], adding to
the possibility of a PCD mechanism already present in
a common eukaryotic ancestor. This illustrates the idea
that PCD might be necessary and present in almost all
species, with adaptations resulting from the particular
characteristics and complexities of the considered
organism.
Some plant homologues of animal genes implicated
in PCD have been isolated recently, and some addi-
tional ones will certainly be found during the comple-
tion of the genome sequence of the model plant
Arabidopsis thaliana. It is not known whether these
plant homologues carry out in plant cells a function
similar to that of their animal counterpart. The recent
development of many experimental systems for detect-
ing and studying plant PCD should allow clarification
of this point. We are at a turning point in understanding
PCD mechanism in plant cells since the molecular
mechanisms are about to be elucidated. It is expected
that the determination of the sequences of genes
regulating directly PCD in plants will reveal the true
similarities and differences of the core regulation of
PCD in plants and animals. And this in turn will show
what are the specific pathways that plants have evolved.
Acknowledgments. The CNRS and the MESR funded
this work. AD and NM are holding a MESR PhD
grant. We thank Dr Michel Delseny director of the
CNRS UMR 5096, for scientific support of this work.
We thank our colleagues Dr JP Reichheld and Dr G.
Hull for critical reading and improvement of the
manuscript before submission.
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