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- Publisher
- Springer Journals
- Copyright
- Copyright © 1997 by Kluwer Academic Publishers
- Subject
- Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
- ISSN
- 0167-4412
- eISSN
- 1573-5028
- DOI
- 10.1023/A:1005898805326
- Publisher site
- See Article on Publisher Site
Abstract
We have cloned a new geranylgeranyl pyrophosphate (GGPP) synthase gene, designated GGPS6/, from Arabidopsis thaliana genomic DNA. Nucleotide sequence analysis revealed that the GGPS6 gene contains an open reading frame coding for a protein of 343 amino acid residues with a calculated molecular mass of 37 507 Da. Also, the gene is not interrupted by an intron. The predicted amino acid sequence of the GGPS6 gene shows significant homology (34.0–57.7%) with other GGPP synthases from Arabidopsis. The GGPS6 protein contains a N-terminal signal peptide which is thought to function as an organelle targeting sequence. In fact, the GGPS6-GFP fusion protein was found to be localized exclusively in mitochondria when expressed in tobacco BY-2 cells. In vitro analysis of the enzyme activity as well as genetic complementation analysis with Erwinia uredovora crt gene cluster expressed in Escherichia coli showed that the GGPS6 gene most certainly encodes a GGPP synthase catalyzing the conversion of farnesyl pyrophosphate to GGPP.
Journal
Plant Molecular Biology – Springer Journals
Published: Sep 30, 2004