SUMO modification of the ubiquitin-conjugating enzyme E2-25K
Post-translational modification with small ubiquitin-related modifier (SUMO) alters the function of many proteins, but the molecular mechanisms and consequences of this modification are still poorly defined. During a screen for novel SUMO1 targets, we identified the ubiquitin-conjugating enzyme E2-2...
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| Main Authors: | , , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
20 February 2005
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| In: |
Nature structural & molecular biology
Year: 2005, Volume: 12, Issue: 3, Pages: 264-269 |
| ISSN: | 1545-9985 |
| DOI: | 10.1038/nsmb903 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nsmb903 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nsmb903 
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| Author Notes: | Andrea Pichler, Puck Knipscheer, Edith Oberhofer, Willem J. van Dijk, Roman Körner, Jesper Velgaard Olsen, Stefan Jentsch, Frauke Melchior & Titia K. Sixma |
MARC
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| 520 | |a Post-translational modification with small ubiquitin-related modifier (SUMO) alters the function of many proteins, but the molecular mechanisms and consequences of this modification are still poorly defined. During a screen for novel SUMO1 targets, we identified the ubiquitin-conjugating enzyme E2-25K (Hip2). SUMO attachment severely impairs E2-25K ubiquitin thioester and unanchored ubiquitin chain formation in vitro. Crystal structures of E2-25K(1-155) and of the E2-25K(1-155)-SUMO conjugate (E2-25K*SUMO) indicate that SUMO attachment interferes with E1 interaction through its location on the N-terminal helix. The SUMO acceptor site in E2-25K, Lys14, does not conform to the consensus site found in most SUMO targets (ΨKXE), and functions only in the context of an α-helix. In contrast, adjacent SUMO consensus sites are modified only when in unstructured peptides. The demonstration that secondary structure elements are part of SUMO attachment signals could contribute to a better prediction of SUMO targets. | ||
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