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J. Biol. Chem., Vol. 276, Issue 44, 40381-40384, November 2, 2001
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From the Botanical Institute, Technical University of
Braunschweig, 38023 Braunschweig, Germany
The xanthine oxidase class of
molybdenum enyzmes requires a terminal sulfur ligand at the
active site. It has been proposed that a special sulfurase catalyzes
the insertion of this ligand thereby activating the enzymes. Previous
analyses of mutants in plants indicated that the genetic locus
aba3 is involved in this step leading to activation of the
molybdenum enzymes aldehyde oxidase and xanthine dehydrogenase. Here we
report the cloning of the aba3 gene from Arabidopsis
thaliana and the biochemical characterization of the purified
protein. ABA3 is a two-domain protein with a N-terminal NifS-like
sulfurase domain and a C-terminal domain that might be involved in
recognizing the target enzymes. Molecular analysis of three
aba3 mutants identified mutations in both domains. ABA3
contains highly conserved binding motifs for pyridoxal phosphate and
for a persulfide. The purified recombinant protein possesses a cysteine
desulfurase activity, is yellow in color, and shows a NifS-like change
in absorbance in the presence of L-cysteine. Pretreatment
of ABA3 with a thiol-specific alkylating reagent inhibited its
desulfurase activity. These data indicate a transsulfuration reaction
similar to bacterial NifS. In a fully defined in vitro
system, the purified protein was able to activate aldehyde oxidase by
using L-cysteine as sulfur donor. Finally, we show
that the expression of the aba3 gene is inducible by
drought-stress.
To whom correspondence should be addressed: Botanical Inst.,
Technical University of Braunschweig, 38023 Braunschweig, Germany. Tel.: 49-531-391-5870; Fax: 49-531-391-8128; E-mail:
R.Mendel@tu-bs.de.
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