First published online September 20, 2002; 10.1104/pp.002550
Plant Physiol, October 2002, Vol. 130, pp. 675-687
The Calcium-Binding Activity of a Vacuole-Associated,
Dehydrin-Like Protein Is Regulated by
Phosphorylation1
Bruce J.
Heyen,2
Muath K.
Alsheikh,
Elizabeth A.
Smith,
Carl F.
Torvik,
Darren F.
Seals,3 and
Stephen K.
Randall*
Department of Biology, Indiana University-Purdue University
at Indianapolis, 723 West Michigan Street, Indianapolis, Indiana
46202-5132
A vacuole membrane-associated calcium-binding protein with an
apparent mass of 45 kD was purified from celery (Apium
graveolens). This protein, VCaB45, is enriched in highly
vacuolate tissues and is located within the lumen of vacuoles.
Antigenically related proteins are present in many dicotyledonous
plants. VCaB45 contains significant amino acid identity with the
dehydrin family signature motif, is antigenically related to dehydrins,
and has a variety of biochemical properties similar to dehydrins.
VCaB45 migrates anomalously in sodium dodecyl sulfate-polyacrylamide
gel electrophoresis having an apparent molecular mass of 45 kD. The
true mass as determined by matrix-assisted laser-desorption ionization
time of flight was 16.45 kD. VCaB45 has two characteristic dissociation
constants for calcium of 0.22 ± 0.142 mM and
0.64 ± 0.08 mM, and has an estimated 24.7 ± 11.7 calcium-binding sites per protein. The calcium-binding properties
of VCaB45 are modulated by phosphorylation; the phosphorylated protein
binds up to 100-fold more calcium than the dephosphorylated protein.
VCaB45 is an "in vitro" substrate of casein kinase II (a ubiquitous
eukaryotic kinase), the phosphorylation resulting in a partial
activation of calcium-binding activity. The vacuole localization,
calcium binding, and phosphorylation of VCaB45 suggest potential functions.
1
This work was supported in part by Purdue
University (Research Fellowship) and by the U.S. Department of
Agriculture-National Research Initiative Competitive Grants
Program (grant no. 99-35100-7668 to S.K.R.).
2
Present address: Departments of Biology and Chemistry,
Tabor College, 400 South Jefferson, Hillsboro, KS 67063.
3
Present address: Van Andel Institute, 333 Bostwick
Avenue NE, Grand Rapids, MI 49503.
*
Corresponding author; e-mail srandal{at}iupui.edu; fax
317-274-2846.
© 2002 American Society of Plant Physiologists
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