Plant Cell Advance Online Publication
Published on November 26, 2002; 10.1105/tpc.005272
Received June 14, 2002
Accepted September 12, 2002
Abscisic Acid-Induced Transcription Is Mediated by Phosphorylation of an Abscisic
Acid Response Element Binding Factor, TRAB1
Yasuaki Kagaya 1, Tokunori Hobo 1, Michiharu Murata 1, Atushi Ban 1, and Tsukaho Hattori 1*
1
Center for Molecular Biology and Genetics, Mie University, 1515 Kamihama-cho, Tsu
514-8507, Japan
* To whom correspondence should be addressed. E-mail: hattori{at}gene.mie-u.ac.jp.
The rice basic domain/Leu zipper factor TRAB1 binds to abscisic acid (ABA) response
elements and mediates ABA signals to activate transcription. We show that TRAB1 is
phosphorylated rapidly in an in vivo labeling experiment and by phosphatase-sensitive
mobility shifts on SDS-polyacrylamide gels. We had shown previously that a
chimeric promoter containing GAL4 binding sites became ABA inducible when a GAL4
binding domain-TRAB1 fusion protein was present. This expression system allowed
us to assay the ABA response function of TRAB1. Using this system, we show that Ser-102
of TRAB1 is critical for this function. Because no ABA-induced mobility shift was
observed when Ser-102 was replaced by Ala, we suggest that this Ser residue is phosphorylated
in response to ABA. Cell fractionation experiments, as well as fluorescence microscopy
observations of transiently expressed green fluorescent protein-TRAB1 fusion
protein, indicated that TRAB1 was localized in the nucleus independently of ABA.
Our results suggest that the terminal or nearly terminal event of the primary ABA
signal transduction pathway is the phosphorylation in the nucleus of preexisting
TRAB1.
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