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Vol. 16, Issue 11, 5115-5126, November 2005

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SUMO-1 Modification Alters ADAR1 Editing Activity

Joana M.P. Desterro ^*, Liam P. Keegan , Ellis Jaffray , Ron T. Hay , Mary A. O'Connell , and Maria Carmo-Fonseca ^*

^* 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; and Biomolecular Sciences Building, University of St. Andrews, St. Andrews, Fife KY19 9ST, Scotland, United Kingdom

Submitted June 15, 2005; Revised July 25, 2005; Accepted August 16, 2005
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.

Abbreviations used: SUMO, small ubiquitin modifier; ADAR, adenosine deaminase that act on RNA; SAE, SUMO-activating enzyme; UBC9, SUMO-conjugating enzyme.

Address correspondence to: Joana M. Pinto Desterro (joanadesterro{at}fm.ul.pt).

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