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A matrix metalloproteinase gene is expressed at the boundary
of senescence and programmed cell death in
cucumber.
Delorme VG, McCabe PF, Kim DJ, Leaver
CJ.
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.
PMID: 10889240
[PubMed - indexed for MEDLINE]
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