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PLANT PHYSIOLOGY , Vol 104, Issue 4 1351-1357, Copyright © 1994 by American Society of Plant Biologists
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MOLECULAR BIOLOGY AND GENE REGULATION |
cDNA Cloning of Carrot (Daucus carota) Soluble Acid [beta]-Fructofuranosidases and Comparison with the Cell Wall Isoenzyme
C. Unger, M. Hardegger, S. Lienhard and A. Sturm
Friedrich Miescher-Institut, Postfach 2543, CH-4002 Basel, Switzerland
Carrot (Daucus carota), like most other plants, contains various isoenzymes
of acid [beta]-fructofuranosidase ([beta]F) (invertase), which either
accumulate as soluble polypeptides in the vacuole (isoenzymes I and II) or
are ionically bound to the cell wall (extracellular [beta]F). Using
antibodies against isoenzyme I of carrot soluble [beta]F, we isolated
several cDNA clones encoding polypeptides with sequences characteristic of
[beta]Fs, from bacteria, yeast, and plants. The cDNA-derived polypeptide of
one of the clones contains all partial peptide sequences of the purified
isoenzyme I and thus codes for soluble acid [beta]F isoenzyme I. A second
clone codes for a related polypeptide (63% identity and 77% similarity)
with characteristics of isoenzyme II. These two soluble [beta]Fs, have
acidic isoelectric points (3.8 and 5.7, respectively) clearly different
from the extracellular enzyme, which has a basic isoelectric point of 9.9.
Marked differences among the three nucleotide sequences as well as
different hybridization patterns on genomic DNA gel blots prove that these
three isoenzymes of carrot acid [beta]F are encoded by different genes and
do not originate from differential splicing of a common gene, as is the
case in the yeast Saccharomyces cerevisiae. All three carrot acid [beta]Fs,
are preproenzymes with signal peptides and N-terminal propeptides. A
comparison of the sequences of the soluble enzymes with the sequence of the
extracellular protein identified C-terminal extensions with short
hydrophobic amino acid stretches that may contain the information for
vacuolar targeting.
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