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Papers In Press, published online ahead of print March 8, 2006
Institute for Biochemistry 2,, Goethe University Medical School, Frankfurt a.M. 60596
Corresponding Author: ivan.dikic{at}biochem2.de
SUMO proteins are ubiquitin (Ub)-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 ß-strand that could bind in parallel or anti-parallel orientation to the ß2-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.
J. Biol. Chem, 10.1074/jbc.M512757200
Submitted on November 29, 2005
Revised on March 7, 2006
Accepted on March 8, 2006
Specification of SUMO1 and SUMO2 interacting motifs
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