Multiple effects of the starch synthase II mutation in developing wheat endosperm
Behjat Kosar-Hashemi A B , Zhongyi Li A B , Oscar Larroque B , Ahmed Regina A B , Makoto Yamamori C , Matthew K. Morell A B and Sadequr Rahman A B DA CSIRO Food Futures National Research Flagship, PO Box 93, North Ryde, NSW 1670, Australia.
B CSIRO Plant Industry, GPO Box 1600, Canberra, ACT 2601, Australia.
C National Agriculture Research Centre for Tohoku Region, Morioka, Iwate 020-0198, Japan.
D Corresponding author. Email: sadequr.rahman@csiro.au
Functional Plant Biology 34(5) 431-438 https://doi.org/10.1071/FP06288
Submitted: 6 November 2006 Accepted: 27 March 2007 Published: 17 May 2007
Abstract
A line of wheat (Triticum aestivum L.), sgp-1, that does not express starch synthase II (SSII, also known as SGP-1) has previously been reported. In this study, F1 derived doubled haploid lines with homozygous wild type or mutant alleles for SGP-1 genes were identified from a cross between the original mutant and a wild type Australian cultivar. Analysis of the starch granules showed that in the mutant lines they are markedly distorted from 15 days postanthesis during grain development. Starch branching patterns showed an increase in the proportion of short chains (DP 6–10) at an earlier stage, but this increase became much more pronounced at 15 days postanthesis and persisted until maturity. There was also a consistent and drastic reduction throughout seed development in the relative amounts of starch branching enzyme II (SBEII, comprising SBEIIa and SBEIIb) and starch synthase I (SSI) bound to the starch granules. In the soluble phase, however, there was relatively little change in the amount of SBEIIb, SBEIIa or SSI protein. Therefore loss of SSII specifically leads to the loss of SBEIIb, SBEIIa and SSI protein in the granule-bound phase and the effect of this mutation is clearly manifest from the mid-stage of endosperm development in wheat.
Additional keywords: SGP-1 null mutant, starch branching enzymes, starch synthases, soluble and granule-bound enzymes.
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