Biomolecular analyses of starch and starch granule proteins in the high-amylose rice mutant goami 2

Butardo, Vito M., Dara Daygon, Venea, Colgrave, Michelle L., Campbell, Peter M., Resurreccion, Adoracion, Paula Cuevas, Rosa, Jobling, Stephen A., Tetlow, Ian, Rahman, Sadequr, Morell, Matthew and Fitzgerald, Melissa (2012) Biomolecular analyses of starch and starch granule proteins in the high-amylose rice mutant goami 2. Journal of Agricultural and Food Chemistry, 60 46: 11576-11585. doi:10.1021/jf303205p

Author Butardo, Vito M.
Dara Daygon, Venea
Colgrave, Michelle L.
Campbell, Peter M.
Resurreccion, Adoracion
Paula Cuevas, Rosa
Jobling, Stephen A.
Tetlow, Ian
Rahman, Sadequr
Morell, Matthew
Fitzgerald, Melissa
Title Biomolecular analyses of starch and starch granule proteins in the high-amylose rice mutant goami 2
Journal name Journal of Agricultural and Food Chemistry   Check publisher's open access policy
ISSN 0021-8561
Publication date 2012-11
Sub-type Article (original research)
DOI 10.1021/jf303205p
Volume 60
Issue 46
Start page 11576
End page 11585
Total pages 10
Place of publication Washington, DC, United States
Publisher American Chemical Society
Collection year 2013
Language eng
Formatted abstract
Elevated proportions of amylose in cereals are commonly associated with either the loss of starch branching or starch synthase activity. Goami 2 is a high-amylose mutant of the temperate japonica rice variety Ilpumbyeo. Genotyping revealed that Goami 2 and Ilpumbyeo carry the same alleles for starch synthase IIa and granule-bound starch synthase I genes. Analyses of granule-bound proteins revealed that SSI and SSIIa accumulate inside the mature starch granules of Goami 2, which is similar to the amylose extender mutant IR36ae. However, unlike the amylose extender mutants, SBEIIb was still detectable inside the starch granules of Goami 2. Detection of SBEIIb after protein fractionation revealed that most of the SBEIIb in Goami 2 accumulates inside the starch granules, whereas most of it accumulates at the granule surface in Ilpumbyeo. Exhaustive mass spectrometric characterisations of granule-bound proteins failed to detect any peptide sequence mutation or major post-translational modifications in Goami 2. Moreover, the signal peptide was found to be cleaved normally from the precursor protein, and there is no apparent N-linked glycosylation. Finally, no difference was found in the SBEIIb structural gene sequence of Goami 2 compared with Ilpumbyeo. In contrast, a G-to-A mutation was detected in the SBEIIb gene of IR36ae located at the splice site between exon and intron 11, which could potentially introduce a premature stop codon and produce a truncated form of SBEIIb. It is suggested that the mutation responsible for producing high amylose in Goami 2 is not due to a defect in SBEIIb gene as was observed in IR36ae, even though it produces a phenotype analogous to the amylose extender mutation. Understanding the molecular genetic basis of this mutation will be important in identifying novel targets for increasing amylose and resistant starch contents in rice and other cereals
Keyword Amylopectin
Ion trap tandem MS
Goamy 2
Mass spectrometry
Quality Japonica rice
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Agriculture and Food Sciences
Official 2013 Collection
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 11 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 11 times in Scopus Article | Citations
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