E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer (original) (raw)
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- Published: 04 September 2005
Nature Structural & Molecular Biology volume 12, pages 933–934 (2005)Cite this article
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Abstract
During ubiquitin ligation, an E2 conjugating enzyme receives ubiquitin from an E1 enzyme and then interacts with an E3 ligase to modify substrates. Competitive binding experiments with three human E2-E3 protein pairs show that the binding of E1s and of E3s to E2s are mutually exclusive. These results imply that polyubiquitination requires recycling of E2 for addition of successive ubiquitins to substrate.
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Acknowledgements
We thank P. Howley and J. Huibregtse for clones of the E6AP-HECT domain and UbcH7. B.K. acknowledges funding from the US National Institutes of Health (NIH), the Searle Scholar's Program and the Beckman Foundation. B.A.S. acknowledges funding from American Lebanese Syrian Associated Charities (ALSAC), the NIH (P30CA21765, R01GM69530), the Philip and Elizabeth Gross Foundation, the Beckman Foundation and the Pew Scholar's Program. D.M.D. acknowledges support from the American Cancer Society.
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Author notes
- Ziad M Eletr and Danny T Huang: These authors contributed equally to the work.
Authors and Affiliations
- Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, 27599-7260, North Carolina, USA
Ziad M Eletr & Brian Kuhlman - Department of Structural Biology and Department of Genetics and Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, 38105, Tennessee, USA
Danny T Huang, David M Duda & Brenda A Schulman
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- Ziad M Eletr
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Correspondence toBrian Kuhlman.
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Eletr, Z., Huang, D., Duda, D. et al. E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer.Nat Struct Mol Biol 12, 933–934 (2005). https://doi.org/10.1038/nsmb984
- Received: 03 June 2005
- Accepted: 09 August 2005
- Published: 04 September 2005
- Issue Date: 01 October 2005
- DOI: https://doi.org/10.1038/nsmb984