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J Biol Chem, Vol. 273, Issue 6, 3236-3246, February 6, 1998

Activation of 2-5 Oligoadenylate Synthetase by Single-stranded and Double-stranded RNA Aptamers

Rune Hartmann^§, Peder L. Nørby, Pia M. Martensen, Poul Jørgensen, Marion C. James^§, Christian Jacobsen^¶, Soren K. Moestrup^¶, Michael J. Clemens^§, and Just Justesen

From the  Department of Molecular and Structural Biology, University of Aarhus, C. F. Møllers Allé, Building 130, DK-8000 Aarhus C, Denmark, the ^§ Division of Biochemistry, Department of Cellular and Molecular Sciences, St. George's Hospital Medical School, Cranmer Terrace, London SW 17 ORE, United Kingdom, and the ^¶ Department of Medical Biochemistry, University of Aarhus, Ole Worms Allé, Building 170, DK-8000 Aarhus C, Denmark

A number of small RNA molecules that are high affinity ligands for the 46-kDa form of human 2-5 oligoadenylate synthetase have been identified by the SELEX method. Surface plasmon resonance analysis indicates that these RNAs bind to the enzyme with dissociation constants in the nanomolar range. Competition experiments indicate that the binding site for the small RNAs on the 2-5 oligoadenylate synthetase molecule at least partially overlaps that for the synthetic double-stranded RNA, poly(I)·poly(C). Several of the RNAs function as potent activators of 2-5 oligoadenylate synthetase in vitro, although there is no correlation between binding affinity and ability to activate. The RNA aptamers having the strongest activation potential appear to have few base-paired regions. This suggests that 2-5 oligoadenylate synthetase, which has previously been believed to be activated only by double-stranded RNA, can also be activated by RNA ligands with little secondary structure. Since 2-5 oligoadenylate synthetase possesses no homology to other known RNA-binding proteins, the development of small specific ligands by SELEX should facilitate studies of RNA-protein interactions and may reveal novel features of the structure-function relationships involving this enzyme.

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