SUMO modification of the ubiquitin-conjugating enzyme E2-25K
Research output: Contribution to journal › Journal article › Research › peer-review
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 (PsiKXE), and functions only in the context of an alpha-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.
Original language | English |
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Journal | Nature Structural and Molecular Biology |
Volume | 12 |
Issue number | 3 |
Pages (from-to) | 264-9 |
Number of pages | 5 |
ISSN | 1545-9993 |
DOIs | |
Publication status | Published - 2005 |
Externally published | Yes |
Bibliographical note
Keywords: Amino Acid Sequence; Consensus Sequence; Crystallization; Hela Cells; Humans; Molecular Sequence Data; Protein Interaction Mapping; Protein Processing, Post-Translational; Protein Structure, Secondary; SUMO-1 Protein; Ubiquitin-Conjugating Enzymes
ID: 19160390