A new vertebrate SUMO enzyme family reveals insights into SUMO-chain assembly

Eisenhardt, Nathalie; Chaugule, Viduth K.; Koidl, Stefanie; Droescher, Mathias; Dogan, Esen; Rettich, Jan; Sutinen, Päivi; Imanishi, Susumu Y.; Hofmann, Kay; Palvimo, Jorma J.; Pichler, Andrea

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A new vertebrate SUMO enzyme family reveals insights into SUMO-chain assembly

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Eisenhardt, Nathalie
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Chaugule, Viduth K.
University of Dundee and Sabanci University Nanotechnology Research and Application Center;
Department of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Koidl, Stefanie
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Droescher, Mathias
Department of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Dogan, Esen
University of Dundee and Sabanci University Nanotechnology Research and Application Center;
Department of Cellular and Molecular Immunology, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Rettich, Jan
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Pichler, Andrea
Department of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Citation

Eisenhardt, N., Chaugule, V. K., Koidl, S., Droescher, M., Dogan, E., Rettich, J., et al. (2015). A new vertebrate SUMO enzyme family reveals insights into SUMO-chain assembly. Nature Structural Molecular & Biology, 22(12), 959-967.

Cite as: https://hdl.handle.net/someHandle/test/escidoc:902500

Abstract

SUMO chains act as stress-induced degradation tags or repair factor-recruiting signals at DNA lesions. Although E1 activating, E2 conjugating and E3 ligating enzymes efficiently assemble SUMO chains, specific chain-elongation mechanisms are unknown. E4 elongases are specialized E3 ligases that extend a chain but are inefficient in the initial conjugation of the modifier. We identified ZNF451, a representative member of a new class of SUMO2 and SUMO3 (SUMO2/3)-specific enzymes that execute catalysis via a tandem SUMO-interaction motif (SIM) region. One SIM positions the donor SUMO while a second SIM binds SUMO on the back side of the E2 enzyme. This tandem-SIM region is sufficient to extend a back side-anchored SUMO chain (E4 elongase activity), whereas efficient chain initiation also requires a zinc-finger region to recruit the initial acceptor SUMO (E3 ligase activity). Finally, we describe four human proteins sharing E4 elongase activities and their function in stress-induced SUMO2/3 conjugation.