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Plant and Cell Physiology Advance Access first published online on June 23, 2005
This version published online on June 27, 2005
Plant and Cell Physiology, doi:10.1093/pcp/pci152
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Plant and Cell Physiology 2005 © The Japanese Society of Plant Physiologists (JSPP); all rights reserved.
Received December 9, 2004
Accepted June 8, 2005

Regular Paper

Dissection of the Phosphorylation of Rice DELLA Protein, SLENDER RICE1

Hironori Itoh 1, Akie Sasaki 1, Miyako Ueguchi-Tanaka 1, Kanako Ishiyama 2, Masatomo Kobayashi 2, Yasuko Hasegawa 1, Eiichi Minami 3, Motoyuki Ashikari 1, and Makoto Matsuoka 1*

1 Bioscience and Biotechnology Center, Nagoya University, Nagoya, Aichi 464-8601, Japan
2 BioResources Center, Riken, Tsukuba 305-0074, Japan
3 Department of Biochemistry, National Institute of Agrobiological Sciences, 2-1-2, Kannondai, Tsukuba 305-8602, Japan

* To whom correspondence should be addressed.
Makoto Matsuoka, E-mail: makoto{at}nuagr1.agr.nagoya-u.ac.jp


  Abstract

DELLA proteins are repressors of gibberellin (GA) signaling in plants. Previous our studies have indicated that GA signaling is derepressed by SCFGID2-mediated proteolysis of the DELLA protein, SLENDER RICE1 (SLR1), in rice. In addition, the GA-dependent increase of phosphorylated SLR1 in the loss-of-function gid2 mutant suggests that the SCFGID2-mediated degradation of SLR1 might be initiated by GA-dependent phosphorylation. To confirm the role of phosphorylation of SLR1 in its GA-dependent degradation, we revealed that SLR1 is phosphorylated on an N-terminal serine residue(s) within the DELLA/TVHYNP and polyS/T/V domain. However, GA-induced phosphorylation in these regions was not observed in the gid2 mutant following the constitutive expression of SLR1 under the control of the rice actin1 promoter. Treatment with GA induced both the phosphorylated and non-phosphorylated forms of SLR1 in similar induction kinetics in gid2 mutant cells. Both the phosphorylated and non-phosphorylated SLR1 proteins were degraded by GA treatment with similar half-life in the rice callus cells and both proteins interacted with recombinant GST-GID2. These results demonstrate that the phosphorylation of SLR1 is independent of its degradation and is dispensable for the interaction of SLR1 with the GID2/F-box protein.

Keywords: DELLA protein; F-box protein; gibberellin; phosphorylation; Rice (Oryza sativa L.).
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