Nucleic Acids Research, Vol 26, Issue 19 4382-4388, Copyright © 1998 by Oxford University Press
E Hitti, A Neunteufl and MF Jantsch
RNA-annealing activity is a common feature of several RNA-binding proteins.
The Xenopus RNA-binding protein X1rbpa is composed of three tandemly
arranged double-stranded RNA-binding domains (dsRBDs) but lacks any other
catalytic or functional domains, therefore making the assessment of
biological functions of this protein rather difficult. Here we show that
full-length X1rbpa but also isolated dsRBDs from this protein can
facilitate RNA strand annealing. RNA annealing can be efficiently inhibited
by heparin. However, dsRBDs with a neutral pI still promote strand
annealing, suggesting that charged residues within the dsRBD are important
for strand annealing. Additionally, mutant versions of the dsRBD, unable to
bind dsRNA in northwestern assays, were tested. Of these, some show
RNA-annealing activity while others fail to do so, indicating that RNA
annealing and dsRNA binding are separable functions. Our data, together
with the previously reported association of the protein with most cellular
RNAs, suggests an RNA chaperone-like function of X1rbpa.
ARTICLES
The double-stranded RNA-binding protein X1rbpa promotes RNA strand annealing
Department of Cytology and Genetics, Institute of Botany, University of Vienna, Rennweg 14, A-1030 Vienna, Austria.
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