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(Received for publication, July 3, 1996, and in revised form, August 9, 1996)
From the Department of Cytology and Genetics, Institute of Botany,
University of Vienna, Rennweg 14, 1030 Vienna, Austria
Xenopus laevis RNA-binding protein A
is a ubiquitously expressed, double-stranded RNA-binding protein that
is associated with the majority of cellular RNAs, ribosomal RNAs, and
hnRNAs. X. laevis RNA-binding protein A contains three
copies of the double-stranded RNA-binding domain (dsRBD) in tandem
arrangement. Two of them, xl1 and xl2, belong to the type A group of
dsRBDs that show strong homologies to the entire length of a defined
consensus sequence. The xl3 domain, in contrast, is a type B dsRBD
which only matches the basic C-terminal end of the dsRBD consensus
sequence. Here we show that only xl2 but neither xl1 nor xl3 are able
to bind double-stranded RNA substrates in vitro, suggesting
that different dsRBD copies have varying RNA binding activities. By
fine mapping mutagenesis of the isolated xl2 domain, we identified at
least two central aromatic amino acids and a C-terminal
Volume 271, Number 45,
Issue of November 8, 1996
pp. 28112-28119
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
-helix that
are indispensable for dsRNA binding. Furthermore, we show that
different charge distributions within the C-terminal -helices of xl1
and xl2 seem responsible for the different RNA binding behaviors of
these two dsRBDs. Analyses of the RNA binding properties of constructs
containing various combinations of different dsRBDs reveal that type A
dsRBDs exhibit a cooperative binding effect, whereas type B dsRBDs show
a rather low binding activity, thus contributing only to a minor extent
to a stable RNA-protein interaction.
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