Faculty Advisor

Weathers, Pamela


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.


Worcester Polytechnic Institute

Date Accepted

November 2005


Biology and Biotechnology


Mathematical Sciences

Project Type

Major Qualifying Project



Advisor Department

Biology and Biotechnology