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A more recent version of this article appeared on November 1, 2005
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Submitted on June 15, 2005
Revised on July 25, 2005
Accepted on August 16, 2005
*Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, 1649-028 Lisboa, Portugal; MRC Human Genetics Unit, Western General Hospital, Edinburgh EH4 2XU, Scotland, United Kingdom; Biomolecular Sciences Building, University of St. Andrews, St. Andrews, Fife KY19 9ST, Scotland, United Kingdom
Monitoring Editor: Peter Walter
We identify ADAR1, an RNA editing enzyme with transient nucleolar localization, as a novel substrate for sumoylation. We show that ADAR1 colocalizes with SUMO-1 in a subnucleolar region that is distinct from the fibrillar center, the dense fibrillar component and the granular component. Our results further show that human ADAR1 is modified by SUMO-1 on lysine residue 418. An arginine substitution of K418 abolishes SUMO-1 conjugation and although it does not interfere with ADAR1 proper localization it stimulates the ability of the enzyme to edit RNA both in vivo and in vitro. Moreover, modification of wild type recombinant ADAR1 by SUMO-1 reduces the editing activity of the enzyme in vitro. Taken together these data suggest a novel role for sumoylation in regulating RNA editing activity.
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