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A Regulatory Role for 14-3-3 Proteins in the Starch Biosynthetic Pathway of Zea mays

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dc.contributor.advisor Emes, Michael
dc.contributor.author Carswell, Matthew
dc.date.accessioned 2021-01-13T21:17:56Z
dc.date.available 2021-01-13T21:17:56Z
dc.date.copyright 2021-01
dc.date.created 2021-01-08
dc.identifier.uri https://hdl.handle.net/10214/23753
dc.description.abstract Starch derived from cereal endosperm is responsible for supporting humanity’s global caloric requirements and is applied in various industrial applications. Semi-crystalline starch granules are comprised of glucose polymers, amylose and amylopectin, which are synthesized by four classes of enzymes including ADP-glucose pyrophosphorylase (AGPase), starch synthases (SS), starch branching enzymes (SBE), and starch debranching enzymes (DBE). Several SS and SBE isoforms form large phosphorylation-dependent heteromeric protein complexes. A class of eukaryotic proteins called “14-3-3” dimerize and interact with phosphorylated clients to regulate enzymatic activity, localization and protein interactions. A series of bioinformatic and biochemical techniques identified GF14-6 as the only detectable 14-3-3 isoform in maize amyloplasts. Recombinant GF14-6 was shown to interact with SSI, SBEIIa and SBEIIb in affinity bait assays. Reciprocal interactions using recombinant SBEIIb demonstrated phosphorylation-dependent interactions with endogenous 14-3-3s. These results point towards a regulatory role for 14-3-3 proteins regulating starch biosynthesis in maize endosperm. en_US
dc.language.iso en en_US
dc.subject Starch en_US
dc.subject 14-3-3 en_US
dc.subject protein-protein interactions en_US
dc.subject phosphorylation en_US
dc.title A Regulatory Role for 14-3-3 Proteins in the Starch Biosynthetic Pathway of Zea mays 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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