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.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Fung, Pui Kwan

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-111805-151810

Advisor

• Weathers, Pamela

Year

• 2005

Date created

• 2005-11-18

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright