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Plant Physiol, October 2001, Vol. 127, pp. 459-472
Biochemical and Genetic Analysis of the Effects of
Amylose-Extender Mutation in Rice Endosperm
Aiko
Nishi,
Yasunori
Nakamura,
Naoki
Tanaka, and
Hikaru
Satoh*
Faculty of Agriculture, Kyushu University, Hakozaki, Higashi-ku,
Fukuoka 812-8581, Japan (A.N., H.S.); Faculty of Bioresource Sciences,
Akita Prefectural University, Shimoshinjo-Nakano, Akita-City 010-0195,
Japan (Y.N.); National Institute of Agrobiological Sciences, Kannondai,
Tsukuba, Ibaraki 305-8602, Japan (N.T.); and Japan Science and
Technology Corporation, Honcho, Kawaguchi, Saitama 332-0012, Japan
(N.T.)
Biochemical analysis of amylose-extender
(ae) mutant of rice (Oryza sativa)
revealed that the mutation in the gene for starch-branching enzyme IIb
(BEIIb) specifically altered the structure of amylopectin in the
endosperm by reducing short chains with degree of polymerization of 17 or less, with the greatest decrease in chains with degree of
polymerization of 8 to 12. The extent of such change was correlated with the gelatinization properties of the starch granules, as determined in terms of solubility in urea solution. The
ae mutation caused a dramatic reduction in the activity
of BEIIb. The activity of soluble starch synthase I (SSI) in the
ae mutant was significantly lower than in the wild type,
suggesting that the mutation had a pleiotropic effect on the SSI
activity. In contrast, the activities of BEI, BEIIa, ADP-Glc
pyrophosphorylase, isoamylase, isoamylase, pullulanase, and Suc
synthase were not affected by the mutation. Therefore, it is stressed
that the function of BEIIb cannot be complemented by BEIIa and BEI.
These results strongly suggest that BEIIb plays a specific role in the
transfer of short chains, which might then be extended by SS to form
the A and B1 chains of amylopectin cluster in rice endosperm.
*
Corresponding author; e-mail hsatoh{at}agr.kyushu-u.ac.jp; fax
81-92-642-3056.
© 2001 American Society of Plant Physiologists
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