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Effect of Water Stress on Cell Division and Cdc2-Like Cell Cycle
Kinase Activity in Wheat Leaves1
Ute Schuppler,
Ping-Hua He,
Peter C.L. John, and
Rana Munns*
Plant Cell Biology Group, Research School of Biological Sciences,
Australian National University, G.P.O. Box 475 (U.S., P.C.L.J.), and
Commonwealth Scientific and Industrial Research Organization, Plant
Industry, G.P.O. Box 1600 (P.-H.H., R.M.), Canberra 2601, Australia
In wheat (Triticum
aestivum) seedlings subjected to a mild water stress (water
potential of 0.3 MPa), the leaf-elongation rate was reduced by
one-half and the mitotic activity of mesophyll cells was reduced to
42% of well-watered controls within 1 d. There was also a
reduction in the length of the zone of mesophyll cell division to
within 4 mm from the base compared with 8 mm in control leaves.
However, the period of division continued longer in the stressed than
in the control leaves, and the final cell number in the stressed leaves
reached 85% of controls. Cyclin-dependent protein kinase enzymes that
are required in vivo for DNA replication and mitosis were recovered
from the meristematic zone of leaves by affinity for
p13suc1. Water stress caused a reduction in H1 histone
kinase activity to one-half of the control level, although amounts of
the enzyme were unaffected. Reduced activity was correlated with an
increased proportion of the 34-kD Cdc2-like kinase (an enzyme sharing
with the Cdc2 protein of other eukaryotes the same size, antigenic sites, affinity for p13suc1, and H1 histone kinase
catalytic activity) deactivated by tyrosine phosphorylation.
Deactivation to 50% occurred within 3 h of stress imposition in
cells at the base of the meristematic zone and was therefore too fast
to be explained by a reduction in the rate at which cells reached
mitosis because of slowing of growth; rather, stress must have acted
more immediately on the enzyme. The operation of controls slowing the
exit from the G1 and G2 phases is discussed. We suggest that a
water-stress signal acts on Cdc2 kinase by increasing phosphorylation
of tyrosine, causing a shift to the inhibited form and slowing cell
production.
1
This research was funded by the Cooperative
Research Centre for Plant Science, Canberra, Australia.
*
Corresponding author; e-mail rana.munns{at}pi.csiro.au; fax
61-2-62-46-5399.
Plant Physiol. (1998) 117: 667-678
Copyright Clearance Center: 0032-0889/98/117/0667/12
© 1998 American Society of Plant Physiologists
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