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Plant and Cell Physiology Advance Access published online on May 23, 2006
Plant and Cell Physiology, doi:10.1093/pcp/pcj062
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Plant and Cell Physiology 2006 © The Japanese Society of Plant Physiologists (JSPP); all rights reserved.
Received March 2, 2006
Accepted May 13, 2006

Regular Paper

ACT Domain Repeat Protein 7, ACR7, Interacts with a Chaperon HSP18.0-CII in Rice Nuclei

Toshihiko Hayakawa 1 *, Toru Kudo 1, Takashi Ito 1, Nobuyuki Takahashi 1, and Tomoyuki Yamaya 2

1 Graduate School of Agricultural Science, Tohoku University, 1-1 Tsutsumidori-Amamiyamachi, Aoba-ku, Sendai, 981-8555 Japan
2 Graduate School of Agricultural Science, Tohoku University, 1-1 Tsutsumidori-Amamiyamachi, Aoba-ku, Sendai, 981-8555 Japan; CREST, JST (Japan Science and Technology Agency), 4-1-8 Honcho, Kawaguchi, Saitama, 332-0012 Japan

* To whom correspondence should be addressed.
Toshihiko Hayakawa, E-mail: toshi{at}biochem.tohoku.ac.jp


  Abstract

The regulatory ACT domains serve as amino acid-binding sites in some amino acid metabolic enzymes and transcriptional regulators in bacteria. To elucidate the molecular entities of the glutamine (Gln)-sensing system on nitrogen (N) metabolism in plants, we isolated six expressing genes encoding ACT domain repeat proteins (ACR1, and ACR5 to ACR9) from rice (Oryza sativa L.) using genomic information on the primary composed of four copies of the domain homologous to those of bacteria Gln sensor GLND. Since expression of ACR7 was the most abundant in the six ACR orthologous genes, we focused on this ACR in the current study. Gene products of ACR7 were most abundant in young developing leaf blades of rice and ACR7 protein is specifically localized in the nucleus of the phloem- and xylem-parenchyma cells in the vascular bundles. Yeast two-hybrid screen identified a small heat stress protein (HSP18.0-CII), as an interactive protein with the ACR7. Transient expression analysis of HSP18.0-CII:sGFP in cultured rice cells, followed by co-immunoprecipitation suggests that the nuclear ACR7 indeed interacted with nucleocytoplasmic HSP18.0-CII in vivo. The potential ability of nuclear protein ACR7 to bind Gln and the possibility of the protein acting as a Gln sensor in rice leaves are discussed.

Keywords: ACT domain repeat protein; Glutamine sensing; Heat stress protein; Rice; Yeast two-hybrid analysis.
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