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MBC in Press, published online ahead of print May 3, 2006
Mol. Biol. Cell 10.1091/mbc.E06-02-0162

A more recent version of this article appeared on July 1, 2006
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Submitted on February 27, 2006
Revised on March 31, 2006
Accepted on April 21, 2006

Substrate-dependent Contribution of Double-stranded RNA-binding Motifs to ADAR2 Function

Ming Xu,* K. Sam Wells,{dagger} and Ronald B. Emeson*{dagger}

Departments of *Pharmacology and {dagger}Molecular Physiology and Biophysics, School of Medicine, Vanderbilt University, Nashville, TN 37232-8548

Monitoring Editor: Karsten Weis

ADAR2 is a double-stranded RNA-specific adenosine deaminase involved in the editing of mammalian RNAs by the site-specific conversion of adenosine to inosine (A-to-I). ADAR2 contains two tandem double-stranded RNA-binding motifs (dsRBMs) that are not only important for efficient editing of RNA substrates, but also necessary for localizing ADAR2 to nucleoli. The sequence and structural similarity of these motifs have raised questions regarding the role(s) that each dsRBM plays in ADAR2 function. Here we demonstrate that the dsRBMs of ADAR2 differ in both their ability to modulate subnuclear localization as well as to promote site-selective A-to-I conversion. Surprisingly, dsRBM1 contributes to editing activity in a substrate-dependent manner, indicating that dsRBMs recognize distinct structural determinants in each RNA substrate. While dsRBM2 is essential for the editing of all substrates examined, a point mutation in this motif affects editing for only a subset of RNAs, suggesting that dsRBM2 utilizes unique sets of amino acid(s) for functional interactions with different RNA targets. The dsRBMs of ADAR2 are interchangeable for subnuclear targeting, yet such motif alterations do not support site-selective editing, indicating that the unique binding preferences of each dsRBM differentially contribute to their pleiotropic function.

Address correspondence to: Ronald B. Emeson (ron.emeson{at}vanderbilt.edu)




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