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Vol. 273, Issue 2, 1099-1106, January 9, 1998
From the To study transporters involved in regulating
intracellular Ca2+, we isolated a full-length
cDNA encoding a Ca2+-ATPase from a model plant,
Arabidopsis, and named it ACA2
(Arabidopsis Ca2+-ATPase, isoform
2). ACA2p is most similar to a "plasma membrane-type" Ca2+-ATPase, but is smaller (110 kDa), contains a unique
N-terminal domain, and is missing a long C-terminal calmodulin-binding
regulatory domain. In addition, ACA2p is localized to an endomembrane
system and not the plasma membrane, as shown by aqueous-two phase
fractionation of microsomal membranes. ACA2p was expressed in yeast as
both a full-length protein (ACA2-1p) and an N-terminal truncation
mutant (ACA2-2p;
A Novel Calmodulin-regulated Ca2+-ATPase
(ACA2) from Arabidopsis with an N-terminal
Autoinhibitory Domain
,,,,,
, and Department of Cell Biology, The Scripps
Research Institute, La Jolla, California 92037, ¶ Department of
Plant Biology, University of Maryland, College Park, Maryland
20742-5815, and Institute of Molecular Biology, Copenhagen
University, Oster Farimagsgade 2A, DK-1353 Copenhagen K, Denmark
residues 2-80). Only the truncation mutant
restored the growth on Ca2+-depleted medium of a yeast
mutant defective in both endogenous Ca2+ pumps, PMR1 and
PMC1. Although basal Ca2+-ATPase activity of the
full-length protein was low, it was stimulated 5-fold by calmodulin
(50% activation around 30 nM). In contrast, the truncated
pump was fully active and insensitive to calmodulin. A
calmodulin-binding sequence was identified within the first 36 residues
of the N-terminal domain, as shown by calmodulin gel overlays on fusion
proteins. Thus, ACA2 encodes a novel calmodulin-regulated Ca2+-ATPase distinguished by a unique N-terminal regulatory
domain and a non-plasma membrane localization.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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