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: | , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
October 2004
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| 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 |
| Summary: | 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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| Item Description: | Online veröffentlicht: 19. September 2004 Gesehen am 04.09.2023 |
| Physical Description: | Online Resource |
| ISSN: | 1545-9985 |
| DOI: | 10.1038/nsmb834 |