Analysis of the isopentenyl diphosphate isomerase gene family from Arabidopsis thaliana
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Two Arabidopsis thaliana cDNAs (IPP1 and IPP2) encoding isopentenyl diphosphate isomerase (IPP isomerase) were isolated by complementation of an IPP isomerase mutant strain of Saccharomyces cerevisiae. Both cDNAs encode enzymes with an amino terminus that may function as a transit peptide for localization in plastids. At least 31 amino acids from the amino terminus of the IPP1 protein and 56 amino acids from the amino terminus of the IPP2 protein are not essential for enzymatic activity. Genomic DNA blot analysis confirmed that IPP1 and IPP2 are derived from a small gene family in A. thaliana. Based on northern analysis expression of both cDNAs occurs predominantly in roots of mature A. thaliana plants grown to the pre-flowering stage.
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Plant Molecular Biology
Volume 36, Issue 2 , pp 323-328
- Cover Date
- Print ISSN
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- Kluwer Academic Publishers
- Additional Links
- isoprenoid biosynthetic pathway
- functional complementation
- isopentenyl diphosphate isomerase
- higher plants
- Industry Sectors
- Author Affiliations
- 1. Division of Science, Pennsylvania State University-Erie, The Behrend College, Erie, PA 16563, USA
- 2. Department of Chemistry, University of Utah, Salt, Lake City, UT, 84112, USA
- 3. Center for Agricultural Molecular Biology, Rutgers University, New Brunswick, NJ, 08903, USA