Nucleic Acids Research, Vol 25, Issue 2 410-416, Copyright © 1997 by Oxford University Press
P Huhn, GJ Pruijn, WJ van Venrooij and M Bachmann
During the analysis of the La (SS-B) autoantigen for catalytic activities
an ATP-dependent double-stranded RNA unwinding activity was detected. Both
native and recombinant La proteins from different species displayed this
activity, which could be inhibited by monospecific anti-La antibodies. La
protein was able to melt dsRNA substrates with either two 3'-overhangs or a
single 3'- and a 5'- overhang. Double-stranded RNAs with two 5'-overhangs
were not unwound, indicating that at least one 3'-overhang is required for
unwinding. Sequence elements of the La protein that might be involved in
dsRNA unwinding, such as an evolutionarily conserved putative ATP-binding
motif and an element that is homologous to the double-stranded RNA binding
protein kinase PKR, are discussed.
ARTICLES
Characterization of the autoantigen La (SS-B) as a dsRNA unwinding enzyme
Institut fur Physiologische Chemie, Johannes-Gutenberg Universitat, Duesbergweg 6, D-55099 Mainz, Germany.
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