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(Received for publication, July 25, 1997, and in revised form, August 29, 1997)
and
From the Botanical Institute, Technical University of Braunschweig,
38023 Braunschweig, Germany and the The molybdenum cofactor is an essential part of
all eukaryotic molybdoenzymes. It is a molybdopterin (MPT) revealing
the same core structure in all organisms. The plant protein Cnx1 from
Arabidopsis thaliana is involved in the multi-step
biosynthesis of molybdenum cofactor. Previous studies (Stallmeyer, B.,
Nerlich, A., Schiemann, J., Brinkmann, H., and Mendel, R. R. (1995) Plant J. 8, 751-762) suggested a function of Cnx1
in a late step of cofactor biosynthesis distal to the formation of MPT,
i.e. conversion of MPT into molybdenum cofactor. Here we
present the first biochemical evidences confirming this assumption. The
protein Cnx1 consists of two domains (E and G) homologous to two
distinct Escherichia coli proteins involved in cofactor
synthesis. Binding studies with recombinantly expressed and purified
Cnx1 and with its single domains revealed a high affinity of the G
domain to MPT (kD = 0.1 µM) with
equimolar binding. In contrast, the E domain of Cnx1 binds MPT with
lower affinity (kD = 1.6 µM) and in a
cooperative manner (nH = 1.5). The entire Cnx1
showed a tight and cooperative MPT binding. Based on these data
providing a common link between both domains that matches the previous
characterization of plant and bacterial Cnx1 homologous mutants, we
present a model for the function of Cnx1.
Department of
Biochemistry, University of Dundee, Dundee
DD 4HN, Scotland, United Kingdom
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