Plant and Cell Physiology, 2001, Vol. 42, No. 11 1228-1233
© 2001 Oxford University Press
A Ca2+-Dependent Protein Kinase that Endows Rice Plants with Cold- and Salt-Stress Tolerance Functions in Vascular Bundles
1 Laboratory of Plant Physiology, Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto, 606-8502 Japan 2 Department of Applied Plant Science, Graduate School of Agricultural Science, Tohoku University, Aoba-ku, Sendai, 981-8555 Japan 3 Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, 630-0101 Japan 4 Department of Plant Production Sciences, Graduate School of Agricultural Science, Tohoku University, Aoba-ku, Sendai, 981-8555 Japan 5 Plant Science Center, RIKEN (The Institute of Physical and Chemical Research), Hirosawa 2-1, Wako, Saitama, 351-0198 Japan
A rice Ca2+-dependent protein kinase, OsCDPK7, is a positive regulator commonly involved in the tolerance to cold and salt/drought. We carried out in situ detection of the transcript and immunolocalization of the protein. In the wild-type rice plants under both stress conditions, OsCDPK7 was expressed predominantly in vascular tissues of crowns and roots, vascular bundles and central cylinder, respectively, where water stress occurs most severely. This enzyme was also expressed in the peripheral cylinder of crown vascular bundles and root sclerenchyma. Similar localization patterns with stronger signals were observed in stress-tolerant OsCDPK7 over-expressing transformants with the cauliflower mosaic virus 35S promoter. The transcript of a putative target gene of the OsCDPK7 signaling pathway, rab16A, was also detected essentially in the same tissues upon salt stress, suggesting that the OsCDPK7 pathway operates predominantly in these regions. We propose that the use of the 35S promoter fortuitously strengthened the localized expression of OsCDPK7, resulting in enhancement of the stress signaling in the inherently operating regions leading to improved stress tolerance.
6 These authors contributed equally to this work.
7 Present address: Department of Molecular, Cellular, and Developmental Biology, Yale University, 165 Prospect Street, OML 352, New Haven, CT 06520-8104, U.S.A.
8 Present address: Institute of Biological Chemistry, Clark Hall 299, Washington State University, Pullman, WA 99164-6340, U.S.A.
9 Corresponding author: E-mail, izui@kais.kyoto-u.ac.jp; Fax, +81-75-753-6470.
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