A Ca2+-dependent protein kinase that endows rice plants with cold- and salt-stress tolerance functions in vascular bundles

Yusuke Saijo, Natsuko Kinoshita, Keiki Ishiyama, Shingo Hata, Junko Kyozuka, Toshihiko Hayakawa, Teiji Nakamura, Ko Shimamoto, Tomoyuki Yamaya, Katsura Izui

Research output: Contribution to journalArticlepeer-review

85 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1228-1233
Number of pages6
JournalPlant and Cell Physiology
Issue number11
Publication statusPublished - 2001


  • CDPK
  • Gene engineering
  • Immunohistochemical localization
  • Rice
  • Stress tolerance
  • Vascular tissues

ASJC Scopus subject areas

  • Physiology
  • Plant Science
  • Cell Biology


Dive into the research topics of 'A Ca<sup>2+</sup>-dependent protein kinase that endows rice plants with cold- and salt-stress tolerance functions in vascular bundles'. Together they form a unique fingerprint.

Cite this