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The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type

Post-translational modification with the ubiquitin-related protein SUMO1 requires the E1 enzyme Aos1-Uba2 and the E2 enzyme Ubc9. Distinct E3 ligases strongly enhance modification of specific targets. The SUMO E3 ligase RanBP2 (also known as Nup358) has no obvious similarity to RING- or HECT-type en...

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Main Authors: Pichler, Andrea (Author) , Knipscheer, Puck (Author) , Saitoh, Hisato (Author) , Sixma, Titia K. (Author) , Melchior, Frauke (Author)
Format: Article (Journal)
Language:English
Published: October 2004
In: Nature structural & molecular biology
Year: 2004, Volume: 11, Issue: 10, Pages: 984-991
ISSN:1545-9985
DOI:10.1038/nsmb834
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nsmb834
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nsmb834
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Author Notes:Andrea Pichler, Puck Knipscheer, Hisato Saitoh, Titia K. Sixma & Frauke Melchior

MARC

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520 |a Post-translational modification with the ubiquitin-related protein SUMO1 requires the E1 enzyme Aos1-Uba2 and the E2 enzyme Ubc9. Distinct E3 ligases strongly enhance modification of specific targets. The SUMO E3 ligase RanBP2 (also known as Nup358) has no obvious similarity to RING- or HECT-type enzymes. Here we show that RanBP2's 30-kDa catalytic fragment is a largely unstructured protein. Despite two distinct but partially overlapping 79-residue catalytic domains, one of which is sufficient for maximal activity, RanBP2 binds to Ubc9 in a 1:1 stoichiometry. The identification of nine RanBP2 and three Ubc9 side chains that are important for RanBP2-dependent SUMOylation indicates largely hydrophobic interactions. These properties distinguish RanBP2 from all other known E3 ligases, and we speculate that RanBP2 exerts its catalytic effect by altering Ubc9's properties rather than by mediating target interactions. 
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