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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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Hauptverfasser: Pichler, Andrea (VerfasserIn) , Knipscheer, Puck (VerfasserIn) , Oberhofer, Edith (VerfasserIn) , van Dijk, Willem J. (VerfasserIn) , Körner, Roman (VerfasserIn) , Olsen, Jesper Velgaard (VerfasserIn) , Jentsch, Stefan (VerfasserIn) , Melchior, Frauke (VerfasserIn) , Sixma, Titia K. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 20 February 2005
In: Nature structural & molecular biology
Year: 2005, Jahrgang: 12, Heft: 3, Pages: 264-269
ISSN:1545-9985
DOI:10.1038/nsmb903
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nsmb903
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nsmb903
Volltext
Verfasserangaben:Andrea Pichler, Puck Knipscheer, Edith Oberhofer, Willem J. van Dijk, Roman Körner, Jesper Velgaard Olsen, Stefan Jentsch, Frauke Melchior & Titia K. Sixma
Beschreibung
Zusammenfassung: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.
Beschreibung:Gesehen am 04.09.2023
Beschreibung:Online Resource
ISSN:1545-9985
DOI:10.1038/nsmb903

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