| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
|
Plant Physiol. (1998) 117: 687-693
Wound Signaling in Tomato Plants1
|
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
 |
ABSTRACT |
|---|
Top
Abstract
Introduction
Methods
Results & Discussion
References
|
|---|
The effects of abscisic acid (ABA) on the accumulation of proteinase inhibitors I (Inh I) and II (Inh II) in young, excised tomato (Lycopersicon esculentum L.) plants were investigated. When supplied to excised plants through the cut stems, 100 µM ABA induced the activation of the ABA-responsive le4 gene. However, under the same conditions of assay, ABA at concentrations of up to 100 µM induced only low levels of proteinase-inhibitor proteins or mRNAs, compared with levels induced by systemin or jasmonic acid over the 24 h following treatment. In addition, ABA only weakly induced the accumulation of mRNAs of several other wound-response proteins. Assays of the ABA concentrations in leaves following wounding indicated that the ABA levels increased preferentially near the wound site, suggesting that ABA may have accumulated because of desiccation. The evidence suggests that ABA is not a component of the wound-inducible signal transduction pathway leading to defense gene activation but is likely involved in the general maintenance of a healthy plant physiology that facilitates a normal wound response.
In response to herbivory or pathogen invasion, tomato
(Lycopersicon esculentum L.) plants activate a signal
transduction cascade that leads to the synthesis of more than 15 swrps
(Bergey et al., 1996 The phytohormones auxin, ethylene, and ABA have been shown to exert
various effects on the activation of defensive genes. Auxin was shown
to inhibit the activation of an Inh II-CAT chimeric gene
(Kernan and Thornberg, 1989 Evidence has been presented that ABA acts as a primary signal in the
systemic wound-signaling cascade in both tomato and potato plants,
namely: (a) ABA-deficient potato and tomato mutants fail to accumulate
Inh II mRNA in response to wounding when assayed at either 6 (Herde et
al., 1996 However, it was reported much earlier (Ryan, 1974 To further examine these discrepancies and more clearly understand the
role of ABA in the wound response, we have undertaken a detailed study
of the effects of ABA on the accumulation of Inh I and II transcripts
and proteins in leaves of young tomato plants. These results do not
support a role for ABA as a primary component of the signal
transduction pathway for defense gene activation in tomato
plants in response to wounding or elicitors. Instead, the
cumulative evidence suggests that ABA is required to maintain the
physiological condition of the plants in a healthy state that allows
the wound response to be functional.
Materials and Plant Growth Conditions
INTRODUCTION
Top
Abstract
Introduction
Methods
Results & Discussion
References
). Two of these genes encode the well-characterized
swrps, the Inh I and II proteins. An 18-amino acid peptide isolated
from tomato leaves, called systemin, is a powerful inducer of swrps when supplied to excised tomato plants (Pearce et al., 1991), and it
has been shown to be mobile in the phloem when applied to wounds on
tomato leaves. Systemin has been proposed to function as a systemic
signal in the activation of defense genes by activating the release of
linolenic acid from membrane lipids of target cells (Conconi et al.,
1996), presumably through interaction with a membrane receptor. The
linolenic acid released is converted to JA through the octadecanoid
pathway (Vick and Zimmerman, 1984). Leaves of intact tomato plants
accumulate JA 1 to 2 h following wounding (Doares et al., 1995;
Conconi et al., 1996), whereas the accumulation of Inh I and II mRNAs
following wounding or systemin treatment is usually detectable within 3 to 4 h, peaking within 9 h, and declining thereafter (Graham
et al., 1986; McGurl et al., 1992). Proteinase-inhibitor proteins can
be detected as early as 4 h after wounding (Graham et al., 1986)
and remain at the maximum levels for days, because they are sequestered
in the central vacuoles of leaf cells (Shumway et al., 1970, 1976).
) in tobacco calli, but the physiological significance of the inhibition is not known. Ethylene alone does not
induce proteinase-inhibitor genes (Ryan, 1974; Kernan and Thornberg,
1989) or other wound-inducible genes (Paradies et al., 1980; Mauch et
al., 1984), but recent reports suggest that wound-induced ethylene
production is required for maximal expression of defense genes (Weiss
and Bevan, 1991; O'Donnell et al., 1996) and requires the presence of
JA (Xu et al., 1994; O'Donnell et al., 1996).
) or 24 h after wounding (Peña-Cortés et al.,
1989, 1996); (b) excised leaves of tomato plants accumulated Inh II
mRNA when treated with ABA for 24 h (Peña-Cortés et
al., 1989, 1993, 1996; Wasternack et al., 1996); and (c) ABA levels increased 2- to 50-fold in tomato leaves 6 h after wounding
(Peña-Cortés et al., 1989, 1996; Herde et al., 1996). As a
consequence of these observations, a hypothesis evolved that ABA is a
key component in the signal transduction cascade leading to defense
gene activation (Peña-Cortés et al., 1996; Wasternack and
Parthier, 1997).
) that ABA was unable
to induce accumulation of Inh I and II proteins in young tomato plants
when it was supplied through their cut stems, a result consistently
repeated using young, excised tomato plants (Schaller and Ryan, 1995).
Additionally, it has been reported that ABA-treated tobacco calli
(Kernan and Thornberg, 1989) and suspension cells (Rickauer et al.,
1992) do not accumulate proteinase inhibitors.
MATERIALS AND METHODS
Top
Abstract
Introduction
Methods
Results & Discussion
References
2 s1 of light
and 7-h nights at 18°C in total darkness. RH was maintained at 80%.
Plants were watered at the beginning of each day. All experiments were
performed with 15-d-old plants that had two expanding leaves and one
small apical leaf.
).
JA was prepared from methyl jasmonate as described by Farmer et al.
(1992). (±)-ABA was purchased from Sigma and (+)-ABA was a gift from
S. Abrams (National Research Council, Saskatoon, Saskatchewan, Canada).
No differences were observed in any experiment between the effects of
(±)-ABA and (+)-ABA. Stocks of each compound were diluted into 10 mM NaH2PO4
buffer (pH 6.5) just prior to use. The ABA-4
-BSA conjugate was a gift from M.K. Walker-Simmons (U.S. Department of Agriculture-Agricultural Research Service, Washington State University, Pullman).
Plant Treatments and Proteinase-Inhibitor Bioassay
Systemin, JA, and ABA were each supplied to excised plants through their cut stems. Pairs of excised plants were placed in 0.6-mL tubes containing 250 µL of buffer alone (10 mM NaH2PO4, pH 6.5) or in buffered solutions of each elicitor or in ABA and incubated for about 30 min at 25°C under 300 µE m2
s1 of light. After about 100 µL of the
solutions had been taken up (approximately 50 µL/plant), plants were
transferred to 20-mL glass vials containing distilled water and
enclosed in a Plexiglas box containing a beaker of 10 M
NaOH as a CO2 trap. Plants were continuously
illuminated under 300 µE m2
s1 of light at 25°C for the duration of each
experiment. Wounding was accomplished by crushing the leaves with a
hemostat three times perpendicular to the midvein on the distal end of
the terminal leaflet of the lower leaf of intact plants. The wounded
and the unwounded control plants were continuously illuminated under
300 µE m2 s1 of light
at 28°C and 80% RH for the duration of each experiment. Inh I and II
protein content was quantified in expressed leaf juice by radial
immunodiffusion (Ryan, 1967; Trautman et al., 1971) using pure Inh I
and II as the standards.
RNA Gel-Blot Analysis
Leaf tissue was frozen in liquid N2, immediately ground to a fine powder in the presence of phenol, and stored at
80°C until tissues from all times were collected. Total
RNA was isolated and fractionated by electrophoresis in a
formaldehyde-agarose gel (12 µg per lane) as described by McGurl et
al. (1995). Gels were stained with ethidium bromide to ensure even
loading of RNA. After fractionation, RNA was blotted onto
nitrocellulose (Schleicher & Schuell) and identified with appropriately
labeled probes. All cDNAs were labeled with a T7 Quickprime Kit
(Pharmacia Biotech, Uppsala, Sweden), according to the
manufacturer's instructions. The following tomato cDNAs were used as
probes: Inh I (Graham et al., 1985a), Inh II (Graham et al., 1985b),
prosystemin (McGurl et al., 1992), cathepsin D inhibitor (Schaller et
al., 1995), Cys proteinase inhibitor (gift from D. Bergey, Washington
State University, Pullman), polyphenol oxidase (Constabel et al.,
1995), and le4 (gift from E.A. Bray, University of
California, Riverside; Cohen and Bray, 1990). Ubiquitin cDNA was a gift
from A. Conconi (Washington State University, Pullman). Nitrocellulose
filters were prehybridized for 4 h at 65°C in 5× SSC (1× SSC
is 150 mM sodium chloride and 15 mM sodium
citrate, pH 7.0), 1% SDS, 5× Denhardt's solution (1× Denhardt's
solution is 0.02% Ficoll, 0.02% PVP, and 0.02% BSA), and 100 µg/mL
denatured herring sperm DNA. Hybridization was performed for at least
12 h at 65°C using the same buffer containing 2 ng/mL
radiolabeled probe. Blots were washed three times for 15 min in 0.5×
SSC and 1% SDS at 65°C and exposed to Kodak XAR film at 80°C
with an intensifying screen.
Extraction and Quantification of ABA
At intervals, leaf tissue was frozen in liquid N2, weighed, lyophilized, and weighed dry. ABA was extracted as follows by a procedure adapted from Walker-Simmons (1987). Powdered tissue was suspended in methanol containing 0.5 g/L
citric acid monohydrate and 100 mg/L butylated hydroxytoluene at a
ratio of 10 mg of dry tissue per 0.1 mL of methanol solution.
Suspensions were stirred in sealed tubes for 36 h at 4°C in the
dark and centrifuged at 1500g. The supernatants were
recovered, adjusted to 70% methanol using a 62.5% solution of the
extracting methanol, and passed through a Sep-Pak
C18 cartridge (Waters). The eluates were dried, resuspended in TBS, diluted as described (Walker-Simmons, 1987), and
stored at 4°C in the dark until assayed. ABA was assayed as described
previously (Walker-Simmons, 1987) using an indirect ELISA method with a
rabbit monoclonal antibody prepared against cis,
trans (+)-ABA (Idetek, Inc., San Bruno, CA).
99%. Additionally, the accuracy of the indirect
ELISA method was verified previously by HPLC and GC-MS (Walker-Simmons, 1987; Munns and King, 1988).
| |
RESULTS AND DISCUSSION |
|---|
|
Top
Abstract
Introduction
Methods
Results & Discussion
References
|
|---|
Accumulation of Proteinase-Inhibitor Proteins and mRNAs in Plants Treated with ABA
ABA in buffer was supplied to young tomato plants at various concentrations and leaves were analyzed 6 h later for the accumulation of Inh I and II mRNA or 24 h later for the accumulation of Inh I and II protein. Figure 1A shows that plants continuously supplied with systemin accumulated high levels of Inh I and II proteins, whereas plants continuously supplied with 100 µM ABA accumulated only slightly more Inh I and II protein than the control plants that were supplied with buffer alone. Northern blots of identically treated plants (Fig. 1B) revealed that ABA only weakly induced the accumulation of mRNAs encoding Inh I and II 6 h after treatment compared with induction by systemin. To ensure that ABA was taken up by plants, the cDNA of an ABA-inducible gene, le4 (Cohen and Bray, 1990), was used as a probe in
northern blotting. Cohen and Bray (1990) previously reported that 100 µM ABA is the lowest concentration that results in a
strong induction of the le4 gene in tomato leaves.
Consistent with their observation, Figure 1B shows that sufficient ABA
is taken up by young plants supplied with 100 µM ABA to
strongly induce the le4 gene. For this reason, all
subsequent experiments were performed with ABA at this concentration.
|
Effects of ABA on the Accumulation of mRNAs Encoding Other Defense
Proteins
Accumulation of ABA in Leaves in Response to Wounding
; Pearce et al., 1991; Schaller et al.,
1995; Schaller and Ryan, 1996), treatment of excised plants with either
systemin or JA for 30 min resulted in a marked accumulation of
inhibitor proteins with time (Fig. 2). However, supplying excised
plants with ABA throughout the incubation time only weakly induced
inhibitor protein accumulation (Fig. 2), and this level remained low
even when the incubation time was extended to 48 h (data not
shown). Likewise, ABA treatment induced only a weak accumulation of Inh II transcript compared with the responses induced by systemin and JA
during the 24 h following treatment (Fig.
3). These results are consistent with
reports that show ABA does not strongly induce Inh I and
II genes in tomato (Ryan, 1974; Schaller and Ryan, 1995) and tobacco (Kernan and Thornberg, 1989; Rickauer et al., 1992).
View larger version (21K):
[in a new window]
Figure 2.
Time course of Inh I and II protein accumulation
in young tomato plants supplied with buffer ( 
) or with buffer plus
ABA (100 µM, 
), JA (40 µM, 
), or
systemin (28 nM, 
). At 4-h intervals, leaf juice was
expressed and assayed for proteinase inhibitors by radial
immunodiffusion. Each data point represents the average of 14 plants ± SE.
View larger version (59K):
[in a new window]
Figure 3.
Time course of Inh II mRNA accumulation in young
tomato plants in response to ABA, JA, and systemin (Sys). The plants
were supplied with buffer or with buffer plus ABA, JA, or systemin as
shown. At the indicated times, leaves from six plants per treatment were frozen for RNA extraction and assayed by northern blotting. Three
independent experiments were performed and results from one
representative experiment are shown.
,
1986), oligosaccharides (Bishop et al., 1984; Walker-Simmons and Ryan,
1986), and systemin (Pearce et al., 1991, 1993; McGurl et al., 1992;
Constabel et al., 1995; Schaller et al., 1995), and the octadecanoid
pathway components linolenic acid (Farmer and Ryan, 1992;
Peña-Cortés et al., 1996), phytodienoic acid (Farmer and
Ryan, 1992), and JA (Farmer and Ryan, 1992; Peña-Cortés et
al., 1996; Wasternack et al., 1996), are only weakly activated by ABA
or not activated at all.
View larger version (55K):
[in a new window]
Figure 4.
Induction of genes encoding several swrps in young
tomato plants in response to buffer or to buffer plus ABA, JA, or
systemin (Sys). After 12 h, leaves from six plants per treatment
were frozen for RNA extraction. mRNA detection was achieved by northern
blotting, and hybridization was achieved with radiolabeled probes
prepared from cDNAs encoding Inh I, cathepsin D inhibitor (CDI), Cys
proteinase inhibitor (Cys), Leu amino peptidase (LAP), polyphenol
oxidase (PPO), or prosystemin (proSys). Three independent experiments were performed, which were in full agreement. Results from one representative experiment are shown.
; Doares et al., 1995).
This model was modified to include ABA accumulation as an obligatory
component between systemin and JA (Peña-Cortés et al.,
1996; Wasternack and Parthier, 1997). This modification was supported
by several reports, all of which indicated that ABA was both necessary
and sufficient for activating defense genes (Peña-Cortés et
al., 1989, 1993, 1996; Herde et al., 1996; Wasternack et al., 1996).
The modified model also predicted that ABA accumulates in response to
wounding and that this accumulation parallels or slightly precedes the
wound-induced accumulation of JA. This was supported by data showing
that ABA accumulated in intact tomato plants 6 h after wounding
(Herde et al., 1996). However, since the accumulation of JA in intact
tomato plants peaks approximately 1 h after wounding and returns
to the original level several hours later (Doares et al., 1995; Conconi
et al., 1996), it was unclear how the accumulation of ABA at 6 h
was exerting a direct effect on gene activation occurring at 3 h
following wounding.
Received September 24, 1997;
accepted March 11, 1998.
Abbreviations:
Inh I and II, proteinase inhibitors I and II,
respectively.
JA, jasmonic acid.
swrps, systemic wound-response
proteins.
We thank Sue Vogtman and Thom Koehler for growing and
maintaining the plants used in this study, Dr. M.K. Walker-Simmons
(U.S. Department of Agriculture-Agricultural Research Service,
Washington State University, Pullman) for her help and guidance with
assaying ABA, and Dr. Elizabeth Bray (University of California,
Riverside) for her generous gift of the le4 cDNA.
Bergey DR,
Howe GA,
Ryan CA
(1996)
Polypeptide signaling for plant defensive genes exhibits analogies to defense signaling in animals.
Proc Natl Acad Sci USA
93:
12053-12058
Bishop PD,
Pearce G,
Bryant JE,
Ryan CA
(1984)
Isolation and characterization of the proteinase inhibitor-inducing factor from tomato leaves: identity and activity of poly- and oligogalacturonide fragments.
J Biol Chem
259:
13172-13176
Cohen A,
Bray EA
(1990)
Characterization of three mRNAs that accumulate in wilted tomato leaves in response to elevated levels of endogenous abscisic acid.
Planta
182:
27-33
Conconi A,
Miquel M,
Browse JA,
Ryan CA
(1996)
Intracellular levels of free linolenic and linoleic acids increase in tomato leaves in response to wounding.
Plant Physiol
111:
797-803
[Abstract]
Constabel CP,
Bergey DR,
Ryan CA
(1995)
Systemin activates synthesis of wound-inducible tomato leaf polyphenol oxidase via the octadecanoid defense signaling pathway.
Proc Natl Acad Sci USA
92:
407-411
Doares SH,
Syrovets T,
Weiler EW,
Ryan CA
(1995)
Oligogalacturonides and chitosan activate plant defensive genes through the octadecanoid pathway.
Proc Natl Acad Sci USA
92:
4095-4098
Farmer EE,
Johnson RR,
Ryan CA
(1992)
Regulation of proteinase inhibitor genes by methyl jasmonate and jasmonic acid.
Plant Physiol
98:
995-1002
Farmer EE,
Ryan CA
(1990)
Interplant communication: airborne methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves.
Proc Natl Acad Sci USA
87:
7713-7716
Farmer EE,
Ryan CA
(1992)
Octadecanoid precursors of jasmonic acid activate the synthesis of wound-inducible proteinase inhibitors.
Plant Cell
4:
129-134
Graham JS,
Hall G,
Pearce G,
Ryan CA
(1986)
Regulation of synthesis of proteinase inhibitors I and II mRNAs in leaves of wounded tomato plants.
Planta
169:
399-405
[CrossRef][Web of Science]
Graham JS,
Pearce G,
Merryweather J,
Titani K,
Ericsson L,
Ryan CA
(1985a)
Wound-induced proteinase inhibitors from tomato leaves. I. The cDNA-deduced primary structure of pre-inhibitor I and its post-translational processing.
J Biol Chem
260:
6555-6560
Graham JS,
Pearce G,
Merryweather J,
Titani K,
Ericsson L,
Ryan CA
(1985b)
Wound-induced proteinase inhibitors from tomato leaves. II. The cDNA-deduced primary structure of pre-inhibitor II.
J Biol Chem
260:
6561-6564
Herde O,
Atzorn R,
Fisahn J,
Wasternack C,
Willmitzer L,
Peña-Cortés H
(1996)
Localized wounding by heat initiates the accumulation of proteinase inhibitor II in abscisic acid-deficient plants by triggering jasmonic acid biosynthesis.
Plant Physiol
112:
853-860
[Abstract]
Kernan A,
Thornberg RW
(1989)
Auxin levels regulate the expression of a wound-inducible proteinase inhibitor II-chloram-phenicol acetyl transferase gene fusion in vitro and in vivo.
Plant Physiol
91:
73-78
Mauch F,
Hadwiger LA,
Boller T
(1984)
Ethylene. Symptom, not signal for the induction of chitinase and
McGurl B,
Mukherjee S,
Kahn M,
Ryan CA
(1995)
Characterization of two proteinase inhibitor (ATI) cDNAs from alfalfa leaves (Medicago sativa var. Vernema): the expression of ATI genes in response to wounding and soil microorganisms.
Plant Mol Biol
27:
995-1001
[Medline]
McGurl B,
Pearce G,
Orozco-Cardenas M,
Ryan CA
(1992)
Structure, expression, and antisense inhibition of the systemin precursor gene.
Science
255:
1570-1573
Munns R,
King RW
(1988)
Abscisic acid is not the only stomatal inhibitor in the transpiration stream of wheat plants.
Plant Physiol
88:
703-708
O'Donnell PJ,
Calvert C,
Atzorn R,
Wasternack C,
Leyser HMO,
Bowles DJ
(1996)
Ethylene as a signal mediating the wound response of tomato plants.
Science
274:
1914-1917
Paradies I,
Konze JR,
Elstner EF
(1980)
Ethylene. Indicator but not inducer of phytoalexin synthesis in soybean.
Plant Physiol
66:
1106-1109
Pearce G,
Johnson S,
Ryan CA
(1993)
Structure-activity of deleted substituted systemin, an 18-amino acid polypeptide inducer of plant defensive genes.
J Biol Chem
268:
212-216
Pearce G,
Strydom D,
Johnson S,
Ryan CA
(1991)
A polypeptide from tomato leaves induces wound-inducible proteinase inhibitor proteins.
Science
253:
895-898
Peña-Cortés H,
Albrecht T,
Prat S,
Weiler EW,
Willmitzer L
(1993)
Aspirin prevents wound-induced gene expression in tomato leaves by blocking jasmonic acid biosynthesis.
Planta
191:
123-128
[Web of Science]
Peña-Cortés H,
Prat S,
Atzorn R,
Wasternack C,
Willmitzer L
(1996)
Abscisic acid-deficient plants do not accumulate proteinase inhibitor II following systemin treatment.
Planta
198:
447-451
[CrossRef]
Peña-Cortés H,
Sánchez-Serrano JJ,
Mertens R,
Willmitzer L,
Prat S
(1989)
Abscisic acid is involved in the wound-induced expression of the proteinase inhibitor II gene in potato and tomato.
Proc Natl Acad Sci USA
86:
9851-9855
Rickauer M,
Bottin A,
Esquerre-Tugaye M
(1992)
Regulation of proteinase inhibitor production in tobacco cells by fungal elicitors, hormonal factors and methyl jasmonate.
Plant Physiol Biochem
30:
579-584
Ryan CA
(1967)
Quantitative determination of soluble cellular proteins by radial diffusion in agar gels containing antibodies.
Anal Biochem
19:
434-440
[CrossRef][Web of Science][Medline]
Ryan C
(1974)
Assay and biochemical properties of the proteinase inhibitor-inducing factor, a wound hormone.
Plant Physiol
54:
328-332
Schaller A,
Bergey DR,
Ryan CA
(1995)
Induction of wound response genes in tomato leaves by bestatin, an inhibitor of aminopeptidases.
Plant Cell
7:
1893-1898
[Abstract]
Schaller A,
Ryan CA
(1995)
Systemin
Schaller A,
Ryan CA
(1996)
Molecular cloning of a tomato leaf cDNA encoding an aspartic protease, a systemic wound response protein.
Plant Mol Biol
31:
1073-1077
[CrossRef][Web of Science][Medline]
Shumway LK,
Rancour JM,
Ryan CA
(1970)
Vacuolar protein bodies in tomato leaf cells and their relationship to storage of chymotrypsin inhibitor I protein.
Planta
93:
1-14
[CrossRef]
Shumway LK,
Vie Yang V,
Ryan CA
(1976)
Evidence for the presence of proteinase inhibitor I in vacuolar protein bodies of plant cells.
Planta
129:
161-165
[CrossRef]
Trautman R,
Cowan KM,
Wagner GG
(1971)
Data processing for immunodiffusion.
Immunochemistry
8:
901-906
[CrossRef][Web of Science][Medline]
Vick BA,
Zimmerman DC
(1984)
Biosynthesis of jasmonic acid by several plant species.
Plant Physiol
75:
458-461
Walker-Simmons M
(1987)
ABA levels and sensitivity in developing wheat embryos of sprouting resistant and susceptible cultivars.
Plant Physiol
84:
61-66
Walker-Simmons M,
Ryan CA
(1984)
Proteinase inhibitor synthesis in tomato leaves. Induction by chitosan oligomers and chemically modified chitosan and chitin.
Plant Physiol
76:
787-790
Walker-Simmons M,
Ryan CA
(1986)
Proteinase inhibitor I accumulation in tomato suspension cultures. Induction by plant and fungal cell wall fragments and an extracellular polysaccharide secreted into the medium.
Plant Physiol
80:
68-71
Wasternack C,
Atzorn R,
Peña-Cortés H,
Parthier B
(1996)
Alteration of gene expression by jasmonate and ABA in tobacco and tomato.
J Plant Physiol
147:
503-510
[Web of Science]
Wasternack C,
Parthier B
(1997)
Jasmonate-signaled plant gene expression.
Trends Plant Sci
2:
302-307
[CrossRef]
Weiss C,
Bevan M
(1991)
Ethylene and a wound signal modulate local and systemic transcription of win2 genes in transgenic potato plants.
Plant Physiol
96:
943-951
Xu Y,
Chang PL,
Liu D,
Narasimhan ML,
Raghothama KG,
Hasegawa PM,
Bressan RA
(1994)
Plant defense genes are synergistically induced by ethylene and methyl jasmonate.
Plant Cell
6:
1077-1085
[Abstract]
View larger version (23K):
[in a new window]
Figure 5.
Time course of the accumulation of ABA in young
tomato plants in response to wounding and wilting with respect to
tissue dry (top) and fresh (bottom) weight. Leaves or leaf subsections
were collected at the indicated times as illustrated in the sketch. At
each interval, the leaves of four plants per treatment were individually assayed for ABA content by an indirect ELISA method and
each assay was performed in triplicate. The means ± SE are plotted. Wilting was performed by exposing excised
lower leaves to air at 28°C and 80% RH. The hatch marks on the
wounded leaflet represent the locations of hemostat-crushed tissue.
Arrows indicate wilted leaves.
View larger version (22K):
[in a new window]
Figure 6.
Time course of the accumulation of ABA and
corresponding water loss in leaves of young tomato plants in response
to wounding. A, The illustration shows the location of tissues tested
with respect to the site of injury. The hatch marks on the wounded leaflet represent the locations of hemostat-crushed tissue. B, At each
interval, leaves from six plants per treatment were assayed in pairs
for ABA content by an indirect ELISA method, and each assay was
performed in triplicate. The means ± SE are plotted. C, Water loss from tissues used in B was monitored by plotting the dry
weight percentage of fresh weight (FW) over time. Wilting was performed
as described in Figure 5.
View larger version (39K):
[in a new window]
Figure 7.
Time-course accumulation of le4
mRNA upon wounding. Six leaves per treatment were collected at the
indicated times and divided into sections as illustrated. Sectioned
tissue was frozen for RNA analysis by northern blotting and
hybridization with radiolabeled probes prepared from cDNAs encoding
le4 and ubiquitin (UBQ). Two independent experiments
were performed and results from one representative experiment are
shown. The hatch marks on the wounded leaflet represent the locations
of hemostat-crushed tissue. Con, Leaves of intact, untreated plants;
Wlt, excised leaves collected 4 h after being allowed to wilt to
88% of their original fresh weight.
, 1996). We
obtained similar results using cv Moneymaker and will report the
results elsewhere (G.F. Birkenmeier and C.A. Ryan, unpublished data).
, 1996; Herde et al., 1996) indicates that the presence of
physiological levels of ABA may be required to potentiate the wound-signaling cascade, but the specific manner in which this may
occur is unknown. However, since ABA does not behave as a primary
component of the systemic wound-signal transduction cascade in tomato,
its role appears to be in maintaining the physiological condition of
the plants so that the wound response is functional.
1
This research was supported in part by the
Washington State University College of Agriculture (project no. 1791),
the National Science Foundation (grant nos. IBN-9184542 and
IBN-9117795) to C.A.R., and a fellowship from the Charlotte Y. Martin
Foundation to G.F.B.
FOOTNOTES
*
Corresponding author; fax 1-509-335-7643.
ABBREVIATIONS
ACKNOWLEDGMENTS
LITERATURE CITED
Top
Abstract
Introduction
Methods
Results & Discussion
References
-1,3-glucanase in pea pods by pathogens and elicitors.
Plant Physiol
76:
607-611
a polypeptide defense signal in plants.
Bioessays
18:
27-33
Copyright Clearance Center: 0032-0889/98/117/0687/07
© 1998 American Society of Plant Physiologists
This article has been cited by other articles:
|
|
 |
|
  C. Ribot, C. Zimmerli, E. E. Farmer, P. Reymond, and Y. Poirier Induction of the Arabidopsis PHO1;H10 Gene by 12-Oxo-Phytodienoic Acid But Not Jasmonic Acid via a CORONATINE INSENSITIVE1-Dependent Pathway Plant Physiology, June 1, 2008; 147(2): 696 - 706. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. He, Y. Tarui, and M. Iino A Novel Receptor Kinase Involved in Jasmonate-mediated Wound and Phytochrome Signaling in Maize Coleoptiles Plant Cell Physiol., June 1, 2005; 46(6): 870 - 883. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. C. Castillo, C. Martinez, A. Buchala, J.-P. Metraux, and J. Leon Gene-Specific Involvement of {beta}-Oxidation in Wound-Activated Responses in Arabidopsis Plant Physiology, May 1, 2004; 135(1): 85 - 94. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Zhu-Salzman, R. A. Salzman, J.-E. Ahn, and H. Koiwa Transcriptional Regulation of Sorghum Defense Determinants against a Phloem-Feeding Aphid Plant Physiology, January 1, 2004; 134(1): 420 - 431. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. A. Schmelz, J. Engelberth, H. T. Alborn, P. O'Donnell, M. Sammons, H. Toshima, and J. H. Tumlinson III Simultaneous analysis of phytohormones, phytotoxins, and volatile organic compounds in plants PNAS, September 2, 2003; 100(18): 10552 - 10557. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C.-T. Wu and K. J. Bradford Class I Chitinase and {beta}-1,3-Glucanase Are Differentially Regulated by Wounding, Methyl Jasmonate, Ethylene, and Gibberellin in Tomato Seeds and Leaves Plant Physiology, September 1, 2003; 133(1): 263 - 273. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Denekamp and S. C. Smeekens Integration of Wounding and Osmotic Stress Signals Determines the Expression of the AtMYB102 Transcription Factor Gene Plant Physiology, July 1, 2003; 132(3): 1415 - 1423. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. A. Perez-Amador, J. Leon, P. J. Green, and J. Carbonell Induction of the Arginine Decarboxylase ADC2 Gene Provides Evidence for the Involvement of Polyamines in the Wound Response in Arabidopsis Plant Physiology, November 1, 2002; 130(3): 1454 - 1463. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Z.-J. Xu, M. Nakajima, Y. Suzuki, and I. Yamaguchi Cloning and Characterization of the Abscisic Acid-Specific Glucosyltransferase Gene from Adzuki Bean Seedlings Plant Physiology, July 1, 2002; 129(3): 1285 - 1295. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Audenaert, G. B. De Meyer, and M. M. Hofte Abscisic Acid Determines Basal Susceptibility of Tomato to Botrytis cinerea and Suppresses Salicylic Acid-Dependent Signaling Mechanisms Plant Physiology, February 1, 2002; 128(2): 491 - 501. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Leon, E. Rojo, and J. J. Sanchez-Serrano Wound signalling in plants J. Exp. Bot., January 1, 2001; 52(354): 1 - 9. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. Reymond, H. Weber, M. Damond, and E. E. Farmer Differential Gene Expression in Response to Mechanical Wounding and Insect Feeding in Arabidopsis PLANT CELL, May 1, 2000; 12(5): 707 - 720. [Abstract] [Full Text]
|
|
|
|
 |
|
 G. A. Howe and C. A. Ryan Suppressors of Systemin Signaling Identify Genes in the Tomato Wound Response Pathway Genetics, November 1, 1999; 153(3): 1411 - 1421. [Abstract] [Full Text]
|
|
|
|
|
|
W. S. Chao, Y.-Q. Gu, V. Pautot, E. A. Bray, and L. L. Walling Leucine Aminopeptidase RNAs, Proteins, and Activities Increase in Response to Water Deficit, Salinity, and the Wound Signals Systemin, Methyl Jasmonate, and Abscisic Acid Plant Physiology, August 1, 1999; 120(4): 979 - 992. [Abstract] [Full Text]
|
|
|
|
|
|
G. Rea, O. Metoui, A. Infantino, R. Federico, and R. Angelini Copper Amine Oxidase Expression in Defense Responses to Wounding and Ascochyta rabiei Invasion Plant Physiology, March 1, 2002; 128(3): 865 - 875. [Abstract] [Full Text] [PDF]
|
|
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| ASPB Publications | PLANT PHYSIOLOGY® | THE PLANT CELL | |
|---|---|---|---|
