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PLANT PHYSIOLOGY , Vol 114, Issue 3 999-1007, Copyright © 1997 by American Society of Plant Biologists
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CELL BIOLOGY AND SIGNAL TRANSDUCTION |
Calmodulin-stimulated Ca2+-ATPases in the Vacuolar and Plasma Membranes in Cauliflower
P. Askerlund
Department of Plant Biochemistry, Lund University, P.O. Box 117, S-221 00 Lund, Sweden
The subcellular locations of Ca2+-ATPases in the membranes of cauliflower
(Brassica oleracea L.) inflorescences were investigated. After continuous
sucrose gradient centrifugation a 111-kD calmodulin (CaM)-stimulated and
CaM-binding Ca2+-ATPase (BCA1; P. Askerlund [1996] Plant Physiol 110:
913-922; S. Malmstrom, P. Askerlund, M.G. Palmgren [1997] FEBS Lett 400:
324-328) comigrated with vacuolar membrane markers, whereas a 116-kD
CaM-binding Ca2+-ATPase co-migrated with a marker for the plasma membrane.
The 116-kD Ca2+-ATPase was enriched in plasma membranes obtained by aqueous
two-phase partitioning, which is in agreement with a plasma membrane
location of this Ca2+-ATPase. Countercurrent distribution of a low-density
intracellular membrane fraction in an aqueous two-phase system resulted in
the separation of the endoplasmic reticulum and vacuolar membranes. The
111-kD Ca2+-ATPase co-migrated with a vacuolar membrane marker after
countercurrent distribution but not with markers for the endoplasmic
reticulum. A vacuolar membrane location of the 111-kD Ca2+-ATPase was
further supported by experiments with isolated vacuoles from cauliflower:
(a) Immunoblotting with an antibody against the 111-kD Ca2+-ATPase showed
that it was associated with the vacuoles, and (b) ATP-dependent Ca2+ uptake
by the intact vacuoles was found to be CaM stimulated and partly
protonophore insensitive.
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