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J Biol Chem, Vol. 274, Issue 14, 9795-9802, April 2, 1999
From the Institut de Génétique et Microbiologie,
Unité Mixte de Recherche CNRS no 8621, Université Paris-Sud
XI, Bâtiment 409, Centre Universitaire d'Orsay,
F-91405 Orsay Cedex, France
AlcR is the transcriptional activator in
Aspergillus nidulans, necessary for the induction of the
alc gene cluster. It belongs to the
Zn2Cys6 zinc cluster protein family, but
contains some striking differences compared with other proteins of this
group. In this report, we show that no dimerization element is present in the entire AlcR protein which occurs in solution as a monomer and
binds also to its cognate sites as a monomer. Another important feature
of AlcR is its unique specificity for single sites occurring naturally
as inverted or direct repeats and sharing a common motif, 5'-(T/A)GCGG-3'. Like most other Zn2Cys6
proteins, AlcR contacts directly with the CGG triplet and, in addition,
the upstream adjacent guanine is required for high affinity binding. We
also establish that the flanking regions outside the core play an
essential role in tight binding. From our in vitro
analysis, we propose an optimal AlcR-binding site which is
5'-PuNGCGG-AT rich 3'.
Unique DNA Binding Specificity of the Binuclear Zinc AlcR
Activator of the Ethanol Utilization Pathway in Aspergillus
nidulans
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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