Title page for E-project-111805-151810

Project Type MQP

Submission date 2005-11-18

Author
Pui Kwan Fung, BIO

URN E-project-111805-151810

Title Computational Analysis of 1-Deoxy-D-xylulose-5-phosphate reductoisomerase in 15 Plant Species

Advisor
Weathers, Pamela, BB

Availability unrestricted

Abstract
The enzyme, 1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR), is a key regulatory step in the non-mevalonate terpenoid biosynthetic pathway in plastids. To investigate the molecular evolution of the enzyme and to predict its location in the chloroplast, a computational analysis was performed on 15 plant DXR sequences that have a full-length cDNA. Results revealed that DXR has an N-terminal transit domain that is likely bipartite, consisting of a chloroplast transit peptide (cTP) and a lumen transit peptide (lTP). Several features were observed in the lTP which suggest that while DXR is targeted to the chloroplast, it is in fact localized to the thylakoid lumen. These features include a twin arginine motif, a hydrophobic region and a proline-rich region. In addition, the functional domain of DXR is found to be highly conserved between prokaryotic and eukaryotic species.

Files
DXR.pdf

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Project Type	MQP
Submission date	2005-11-18
Author	Pui Kwan Fung, BIO
URN	E-project-111805-151810
Title	Computational Analysis of 1-Deoxy-D-xylulose-5-phosphate reductoisomerase in 15 Plant Species
Advisor	Weathers, Pamela, BB
Availability	unrestricted
Abstract The enzyme, 1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR), is a key regulatory step in the non-mevalonate terpenoid biosynthetic pathway in plastids. To investigate the molecular evolution of the enzyme and to predict its location in the chloroplast, a computational analysis was performed on 15 plant DXR sequences that have a full-length cDNA. Results revealed that DXR has an N-terminal transit domain that is likely bipartite, consisting of a chloroplast transit peptide (cTP) and a lumen transit peptide (lTP). Several features were observed in the lTP which suggest that while DXR is targeted to the chloroplast, it is in fact localized to the thylakoid lumen. These features include a twin arginine motif, a hydrophobic region and a proline-rich region. In addition, the functional domain of DXR is found to be highly conserved between prokaryotic and eukaryotic species.
Files	DXR.pdf