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Nucleic Acids Res. 1997 Jan 15;25(2):410-6.

Characterization of the autoantigen La (SS-B) as a dsRNA unwinding enzyme.

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Institut für Physiologische Chemie, Johannes-Gutenberg Universität, Duesbergweg 6, D-55099 Mainz, Germany.


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.

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