UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids

Dawn M. Wenzel, Alexei Lissounov, Peter S. Brzovic and Rachel E. Klevit ()
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Dawn M. Wenzel: Box 357350, University of Washington
Alexei Lissounov: Box 357350, University of Washington
Peter S. Brzovic: Box 357350, University of Washington
Rachel E. Klevit: Box 357350, University of Washington

Nature, 2011, vol. 474, issue 7349, 105-108

Abstract: E2/E3-mediated ubiquitination Attachment of the small protein ubiquitin (Ub) to substrates is a reversible covalent modification that regulates the stability, activity and localization of target proteins. Assembly of ubiquitin chains requires three enzyme activities: a Ub-activating (E1) enzyme, a Ub-conjugating (E2) enzyme and a Ub ligase (E3). E2 enzymes are responsible both for E3 selection and substrate modification and for much of the diversity of Ub cellular signalling. The E2 UbcH7 shows broad specificity for HECT-type E3, but often fails to function with RING E3s despite its ability to form specific complexes. Rachel Klevit and colleagues demonstrate that UbcH7 exhibits robust activity with a family of E3 ligases that are RING/HECT hybrids: they bind to E2s through a RING domain but transfer Ub through a HECT-like mechanism. They propose that the intrinsic chemical reactivity of an E2 is a powerful predictor in determining with which class of E3 it will function.

Date: 2011
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DOI: 10.1038/nature09966

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