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(Received for publication, January 27, 1997, and in revised form, April 14, 1997)
From the The enzyme farnesyl-diphosphate synthase (FPS; EC
2.5.1.1./EC 2.5.1.10) catalyzes the synthesis of farnesyl diphosphate from isopentenyl diphosphate and dimethylallyl diphosphate. FPS is
considered to play a key role in isoprenoid biosynthesis. We have
reported previously that Arabidopsis thaliana contains two differentially expressed genes, FPS1 and FPS2,
encoding two highly similar FPS isoforms, FPS1 and FPS2, (Cunillera,
N., Arró, M., Delourme, D., Karst, F., Boronat, A., and Ferrer,
A. (1996) J. Biol. Chem. 271, 7774-7780). In this
paper we report the characterization of a novel Arabidopsis
FPS mRNA (FPS1L mRNA) derived from the FPS1 gene. A
cDNA corresponding to the FPS1L mRNA was cloned using a reverse
transcription-polymerase chain reaction strategy. Northern blot
analysis showed that the two FPS1-derived mRNAs are
differentially expressed. The FPS1L mRNA accumulates preferentially
in inflorescences, whereas the previously reported FPS1 mRNA (FPS1S
mRNA) is predominantly expressed in roots and inflorescences. FPS1L
mRNA contains an in-frame AUG start codon located 123 nucleotides
upstream of the AUG codon used in the translation of the FPS1S isoform.
Translation of the FPS1L mRNA from the upstream AUG codon generates
a novel FPS1 isoform (FPS1L) with an NH2-terminal extension
of 41 amino acid residues, which has all the characteristics of a
mitochondrial transit peptide. The functionality of the FPS1L
NH2-terminal extension as a mitochondrial transit peptide
was demonstrated by its ability to direct a passenger protein to yeast
mitochondria in vivo and by in vitro import
experiments using purified plant mitochondria. The
Arabidopsis FPS1L isoform is the first FPS reported to
contain a mitochondrial transit peptide.
Volume 272, Number 24,
Issue of June 13, 1997
pp. 15381-15388
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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Unitat de Bioquímica,
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