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Plant Physiol, July 2000, Vol. 123, pp. 917-928
A Matrix Metalloproteinase Gene Is Expressed at the Boundary of
Senescence and Programmed Cell Death in
Cucumber1
Valérie G.R.
Delorme,23
Paul F.
McCabe,2
Dae-Jae
Kim,4 and
Christopher J.
Leaver*
Department of Plant Sciences, University of Oxford, South Parks
Road, Oxford OX1 3RB, United Kingdom
Cell-cell and extracellular cell matrix (ECM) interactions provide
cells with information essential for controlling morphogenesis, cell-fate specification, and cell death. In animals, one of the major
groups of enzymes that degrade the ECM is the matrix metalloproteinases (MMPs). Here, we report the characterization of the cucumber
(Cucumis sativus L. cv Marketmore)
Cs1-MMP gene encoding such an enzyme likely to play a
role in plant ECM degradation. Cs1-MMP has all the hallmark motif
characteristics of animal MMPs and is a pre-pro-enzyme having a signal
peptide, propeptide, and zinc-binding catalytic domains. Cs1-MMP also
displays functional similarities with animal MMPs. For example, it has
a collagenase-like activity that can cleave synthetic peptides and
type-I collagen, a major component of animal ECM. Cs1-MMP activity is
completely inhibited by a hydroxamate-based inhibitor that binds at the
active site of MMPs in a stereospecific manner. The
Cs1-MMP gene is expressed de novo at the end stage of
developmental senescence, prior to the appearance of DNA laddering in
cucumber cotyledons leaf discs and male flowers. As the steady-state level of Cs1-MMP mRNA peaks late in senescence and the
pro-enzyme must undergo maturation and activation, the protease is
probably not involved in nutrient remobilization during senescence but may have another function. The physiological substrates for Cs1-MMP remain to be determined, but the enzyme represents a good candidate for
plant ECM degradation and may be involved in programmed cell death
(PCD). Our results suggest that PCD occurs only at the culmination of
the senescence program or that the processes are distinct with PCD
being triggered at the end of senescence.
1
This work was supported by Rhône Poulenc
(Paris). P.F.M. was funded by a Biotechnology and Biological Science
Research Council research grant (to C.J.L.).
2
These authors contributed equally to the paper.
3
Present address: Laboratoire de Physiologie et Biologie
Moléculaire des Plantes, Unité Mixte de Recherche, Centre
National de la Recherche Scientifique 5545, Université de
Perpignan, 52 Avenue de Villeneuve, 66860 Perpignan cedex, France.
4
Present address: Chungbuk National
University, College of Education, School of Science Education, 48 Gaeshin-Dong, Heungduk-Gu, Cheong Ju, 361-763, Chungbuk, Korea.
*
Corresponding author; e-mail
chris.leaver{at}plants.ox.ac.uk; fax 44-1865-275144.
© 2000 American Society of Plant Physiologists
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