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First published online March 8, 2002; 10.1105/tpc.010454

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The Plant Cell, Vol. 14, 619-628, March 2002, Copyright © 2002,
American Society of Plant Biologists

Rice SPK, a Calmodulin-Like Domain Protein Kinase, Is Required for Storage Product Accumulation during Seed Development

Phosphorylation of Sucrose Synthase Is a Possible Factor

Takayuki Asano1,a, Noriko Kunieda1,2,,a, Yuhi Omura1,3,,a, Hirokazu Ibea, Tsutomu Kawasaki4,b, Makoto Takanoc, Miho Satoc, Hideyuki Furuhashia, Toshiyuki Mujina, Fumio Takaiwac, Chuan-yin Wuc, Yuichi Tadad, Tomomi Satozawad, Masahiro Sakamoto5,d and Hiroaki Shimada6,a

a Department of Biological Science and Technology, Science University of Tokyo, 2641 Yamazaki, Noda 278-8510, Japan
b Mitsui Plant Biotechnology Research Institute, Tsukuba 305, Japan
c National Institute of Agrobiological Sciences, 2-1-2 Kan-non-dai, Tsukuba 305-8602, Japan
d Life Science Institute, Mitsui Chemicals, Inc., Mobara 278-0017, Japan

6 To whom correspondence should be addressed. E-mail shimadah{at}rs.noda.sut.ac.jp; fax 81-471-25-1841

Suc, an end product of photosynthesis, is metabolized by Suc synthase in sink organs as an initial step in the biosynthesis of storage products. Suc synthase activity is known to be regulated by reversible phosphorylation, but the details of this process are unclear at present. Rice SPK, a calcium-dependent protein kinase, is expressed uniquely in the endosperm of immature seed, and its involvement in the biosynthetic pathways of storage products was suggested. Antisense SPK transformants lacked the ability to accumulate storage products such as starch, but produced watery seed with a large amount of Suc instead, as the result of an inhibition of Suc degradation. Analysis of in vitro phosphorylation indicated that SPK phosphorylated specifically a Ser residue in Suc synthase that has been shown to be important for its activity in the degradation of Suc. This finding suggests that SPK is involved in the activation of Suc synthase. It appears that SPK is a Suc synthase kinase that may be important for supplying substrates for the biosynthesis of storage products.




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