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J Biol Chem, Vol. 275, Issue 5, 3137-3143, February 4, 2000
From the Laboratory of Plant Molecular Biology and Physiology,
Department of Horticulture, Washington State University,
Pullman, Washington 99164-6414
The use of 35S-labeled
calmodulin (CaM) to screen a corn root cDNA expression library has
led to the isolation of a CaM-binding protein, encoded by a cDNA
with sequence similarity to small auxin up RNAs (SAURs), a
class of early auxin-responsive genes. The cDNA designated as
ZmSAUR1 (Zea mays SAURs) was expressed in
Escherichia coli, and the recombinant protein was purified
by CaM affinity chromatography. The CaM binding assay revealed that the
recombinant protein binds to CaM in a calcium-dependent
manner. Deletion analysis revealed that the CaM binding site was
located at the NH2-terminal domain. A synthetic peptide of
amino acids 20-45, corresponding to the potential CaM binding region,
was used for calcium-dependent mobility shift assays. The
synthetic peptide formed a stable complex with CaM only in the presence
of calcium. The CaM affinity assay indicated that ZmSAUR1 binds to CaM
with high affinity (Kd ~15 nM) in a
calcium-dependent manner. Comparison of the
NH2-terminal portions of all of the characterized SAURs
revealed that they all contain a stretch of the basic The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF148498.
Molecular and Biochemical Evidence for the Involvement of
Calcium/Calmodulin in Auxin Action*
-amphiphilic
helix similar to the CaM binding region of ZmSAUR1. CaM binds to the
two synthetic peptides from the NH2-terminal regions of
Arabidopsis SAUR-AC1 and soybean 10A5, suggesting that this
is a general phenomenon for all SAURs. Northern analysis was carried
out using the total RNA isolated from auxin-treated corn coleoptile
segments. ZmSAUR1 gene expression began within 10 min,
increased rapidly between 10 and 60 min, and peaked around 60 min after
10 µM -naphthaleneacetic acid treatment. These results
indicate that ZmSAUR1 is an early auxin-responsive gene.
The CaM antagonist
N-(6-aminohexyl)5-chloro-1-naphthalenesulfonamide hydrochloride inhibited the auxin-induced cell elongation but not the
auxin-induced expression of ZmSAUR1. This suggests that calcium/CaM do not regulate ZmSAUR1 at the transcriptional
level. CaM binding to ZmSAUR1 in a calcium-dependent manner
suggests that calcium/CaM regulate ZmSAUR1 at the post-translational
level. Our data provide the first direct evidence for the involvement of calcium/CaM-mediated signaling in auxin-mediated signal transduction.
*
This work was supported in part by National Science
Foundation Grant MCB 96-30337 and National Aeronautics and Space
Administration Grant NAG-10-0061.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 509-335-2487;
Fax: 509-335-8690; E-mail: poovaiah@wsu.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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