Date of Award

2006

Degree Type

Thesis

Degree Name

Master of Science

Program

Biology

Supervisor

Dr. Susanne Kohalmi

Second Advisor

Dr. Mark Bernards

Third Advisor

Dr. Denis Maxwell

Abstract

Six putative arogenate dehydratases (ADT) isoforms have been identified in Arabidopsis thaliana, but are listed online as prephenate dehydratases (PDTs) based on sequence similarity. To determine whether the putative Arabidopsis ADTs recognise arogenate, prephenate, or both, individual isoforms were analysed using a molecular and biochemical approach. An extensive in silico analysis showed that while putative plant ADT sequences form a distinct group from bacterial and yeast sequences, they share all sequence motifs that were identified through mutagenic studies as being essential for function. Putative ADTs were cloned into a Saccharomyces cerevisiae and two Escherichia coli expression systems, and expressed as His-fusion proteins. Putative ADTs were successfully purified and assayed against either arogenate or prephenate to test enzyme specificity, however, results were inconclusive due to apparent non-enzymatic conversion. A second approach tested the function of two putative ADTs by complementation of a PDT knockout in S. cerevisiae. This test showed that ADT1 could complement the PDT of S. cerevisiae while ADT3 could not, suggesting that there may be functional differences between these ADT isoforms.

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