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J. Biol. Chem., Vol. 281, Issue 23, 16117-16127, June 9, 2006

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Specification of SUMO1- and SUMO2-interacting Motifs^*

Christina-Maria Hecker¹², Matthias Rabiller¹, Kaisa Haglund, Peter Bayer³, and Ivan Dikic⁴

From the Institute for Biochemistry II, Goethe University Medical School, Theodor-Stern-Kai 7, 60590 Frankfurt, Germany and the Universität Duisburg-Essen, Fachbereich Biologie und Geografie, Strukturelle und Medizinische Biochemie, Universitätsstrasse, 45117 Essen, Germany

SUMO proteins are ubiquitin-related modifiers implicated in the regulation of gene transcription, cell cycle, DNA repair, and protein localization. The molecular mechanisms by which the sumoylation of target proteins regulates diverse cellular functions remain poorly understood. Here we report isolation and characterization of SUMO1- and SUMO2-binding motifs. Using yeast two-hybrid system, bioinformatics, and NMR spectroscopy we define a common SUMO-interacting motif (SIM) and map its binding surfaces on SUMO1 and SUMO2. This motif forms a -strand that could bind in parallel or antiparallel orientation to the ₂-strand of SUMO due to the environment of the hydrophobic core. A negative charge imposed by a stretch of neighboring acidic amino acids and/or phosphorylated serine residues determines its specificity in binding to distinct SUMO paralogues and can modulate the spatial orientation of SUMO-SIM interactions.

Received for publication, November 29, 2005 , and in revised form, March 7, 2006.

^* This work was supported by grants from the Deutsche Forschungsgemeinschaft (DI 931/1-1) and Boehringer Ingelheim Fonds (to I. D.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1–3.

¹ These authors contributed equally to this work.

² Fellow of the Hessian Ministry for Science and Arts.

³ To whom correspondence may be addressed. E-mail: Peter.Bayer{at}uni-due.de. ⁴ To whom correspondence may be addressed. E-mail: Ivan.Dikic{at}biochem2.de.

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