Acta Physiologiae Plantarum

, Volume 33, Issue 6, pp 2103–2116 | Cite as

Biochemical characterization of the Arabidopsis KS-type dehydrin protein, whose gene expression is constitutively abundant rather than stress dependent

  • Masakazu Hara
  • Yuri Shinoda
  • Masayuki Kubo
  • Daiju Kashima
  • Ikuo Takahashi
  • Takanari Kato
  • Tokumasa Horiike
  • Toru Kuboi
Original Paper


Dehydrins are known as plant stress-responsive genes. Arabidopsis thaliana has 10 dehydrin genes. Among them, one of the highly expressed genes is a KS-type dehydrin (At1g54410). However, the gene product, which is a histidine-rich dehydrin whose molecular mass is 11 kDa (AtHIRD11), has not been studied. Thus, we report the biochemical characterization of the AtHIRD11 protein. Although the AtHIRD11 protein was detected in all organs of Arabidopsis, the bolting stem and the flower showed higher accumulation than the other organs, with the AtHIRD11 protein detected in the cambial zone of the stem vasculature. Most of the AtHIRD11 protein was found to be a bound form. The bound AtHIRD11 was solubilized by 1 M NaCl solution. The extracted AtHIRD11 was retained in immobilized metal-affinity chromatography, and eluted by an imidazole gradient. The native AtHIRD11 prepared from Arabidopsis was partially phosphorylated, but further phosphorylated by casein kinase 2 in vitro. Metal-binding assays indicated that Zn2+ may be the best metal for AtHIRD11 binding. These results suggest that AtHIRD11 is a metal-binding dehydrin that shows a house-keeping expression in Arabidopsis.


Arabidopsisthaliana Dehydrin Late embryogenesis abundant proteins Metal binding 



Abscisic acid


Arabidopsisthaliana histidine-rich dehydrin whose molecular mass is 11 kDa


Casein kinase 2


Two-dimensional polyacrylamide gel electrophoresis


Ethylenediaminetetraacetic acid


Expressed sequence tag


Immobilized metal affinity chromatography


Polymerase chain reaction


Reverse transcription-polymerase chain reaction


Shrimp alkaline phosphatase


Sodium dodecyl sulfate


SDS-polyacrylamide gel electrophoresis



This work was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan (19380182).

Supplementary material

11738_2011_749_MOESM1_ESM.pdf (77 kb)
Supplementary figures (PDF 76 kb)


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Copyright information

© Franciszek Górski Institute of Plant Physiology, Polish Academy of Sciences, Kraków 2011

Authors and Affiliations

  • Masakazu Hara
    • 1
  • Yuri Shinoda
    • 1
  • Masayuki Kubo
    • 1
  • Daiju Kashima
    • 1
  • Ikuo Takahashi
    • 1
  • Takanari Kato
    • 1
  • Tokumasa Horiike
    • 2
  • Toru Kuboi
    • 1
  1. 1.Faculty of AgricultureShizuoka UniversityShizuokaJapan
  2. 2.Division of Global Research LeadersShizuoka UniversityShizuokaJapan

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