Degree Type

Thesis

Date of Award

2016

Degree Name

Master of Science

Department

Biochemistry, Biophysics and Molecular Biology

Major

Molecular, Cellular and Developmental Biology

First Advisor

Basil J. Nikolau

Abstract

Very-long-chain fatty acids (VLCFAs) consist of greater than 18 carbon atoms and have diverse biological functions including energy storage, protection from biotic and abiotic stresses, signaling, and are components of the plasma membrane. The biosynthesis of VLCFAs occurs by the iterative extension of fatty acyl-CoAs through a series of reactions catalyzed by four enzyme components known as fatty acid elongase (FAE). The FAE enzyme 3-ketoacyl CoA synthase (KCS) is hypothesized to be responsible for the substrate specificity of FAE, controlling the amount and identity of VLCFAs produced in specific cell types and tissues. The KCS gene family consists of multiple homologs in plant species, including 21 paralogs in Arabidopsis thaliana. This manuscript details the identification and analysis of KCS condensing enzymes from Zea mays. The genetic redundancy within FAE along with the membrane-bound nature of KCS and other FAE enzymes are challenges when studying this enzyme system. Because of these obstacles, heterologous expression in yeast was employed for the characterization of maize KCS enzymes. The fatty acid composition of yeast strains was determined using GC-MS, revealing KCS-dependent differences in VLCFAs and uncovering new questions about the synthesis of VLCFAs in maize.

DOI

https://doi.org/10.31274/etd-180810-5535

Copyright Owner

Kayla S. Flyckt

Language

en

File Format

application/pdf

File Size

82 pages

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