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Investigation of Starch Synthesis in a TILLING Mutant of Maize

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dc.contributor.advisor Emes, Michael
dc.contributor.author Massey, Sarah
dc.date.accessioned 2014-05-06T16:20:31Z
dc.date.available 2014-05-06T16:20:31Z
dc.date.copyright 2014-04
dc.date.created 2014-05-02
dc.date.issued 2014-05-06
dc.identifier.uri http://hdl.handle.net/10214/8067
dc.description.abstract Starch is an important polymer made up of amylose and amylopectin. ADP-glucose pyrophosphorylase (AGPase), starch synthases (SS), starch branching enzymes (SBE), and starch debranching enzymes (SDE) are involved in starch synthesis. SSI, SSIIa and SBEIIb associate in phosphorylation-dependent multi-subunit complexes in maize. This investigation aimed to characterize new mutations in the SBEIIb gene using a TILLING technique. A single nucleotide substitution (G>A) in the SBEIIb gene was generated, translating to a cysteine to tyrosine amino acid change (C663Y) in a putative protein-protein interaction domain. C663Y SBEIIb appears to have reduced activity compared to the reference genotype, and the SBEIIb-SSIIa interaction is weakened. Starch granules from the C663Y mutant appear to possess SBEIIb as well as another branching isoform, SBEI, which is not normally found in the starch granule. The work presented here suggests altered protein-protein interactions in the C663Y mutant resulting in a change in starch structure. en_US
dc.description.sponsorship Ontario Ministry of Agriculture, Food and Rural Affairs en_US
dc.language.iso en en_US
dc.subject Starch en_US
dc.subject Starch Branching Enzyme en_US
dc.subject Protein-Protein Interactions en_US
dc.subject Resistant Starch en_US
dc.subject Protein Complexes en_US
dc.subject Maize en_US
dc.title Investigation of Starch Synthesis in a TILLING Mutant of Maize en_US
dc.type Thesis en_US
dc.degree.programme Molecular and Cellular Biology en_US
dc.degree.name Master of Science en_US
dc.degree.department Department of Molecular and Cellular Biology en_US
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