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  Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler

Liwocha, J., Krist, D. T., van der Heden van Noort, G., Hansen, F. M., Truong, V., Karayel, O., et al. (2020). Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler. Nature Chemical Biology. doi:10.1038/s41589-020-00696-0.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0007-9767-B Version Permalink: http://hdl.handle.net/21.11116/0000-0007-9768-A
Genre: Journal Article

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 Creators:
Liwocha, Joanna1, Author              
Krist, David T.1, Author              
van der Heden van Noort, G.J.2, Author
Hansen, Fynn M.3, Author              
Truong, V.H.2, Author
Karayel, Ozge3, Author              
Purser, N.2, Author
Houston, D.2, Author
Burton, N.2, Author
Bostock, M.J.2, Author
Sattler, M.2, Author
Mann, Matthias3, Author              
Harrison, J.S.2, Author
Kleiger, G.2, Author
Ovaa, H.2, Author
Schulman, Brenda A.1, Author              
Affiliations:
1Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society, ou_2466699              
2External Organizations, ou_persistent22              
3Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: Enzyme mechanisms; Enzymes; Protein design
 Abstract: Virtually all aspects of cell biology are regulated by a ubiquitin code where distinct ubiquitin chain architectures guide the binding events and itineraries of modified substrates. Various combinations of E2 and E3 enzymes accomplish chain formation by forging isopeptide bonds between the C terminus of their transiently linked donor ubiquitin and a specific nucleophilic amino acid on the acceptor ubiquitin, yet it is unknown whether the fundamental feature of most acceptors—the lysine side chain—affects catalysis. Here, use of synthetic ubiquitins with non-natural acceptor site replacements reveals that the aliphatic side chain specifying reactive amine geometry is a determinant of the ubiquitin code, through unanticipated and complex reliance of many distinct ubiquitin-carrying enzymes on a canonical acceptor lysine. [Figure not available: see fulltext.] © 2020, The Author(s), under exclusive licence to Springer Nature America, Inc.

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Language(s): eng - English
 Dates: 2020-122020
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1038/s41589-020-00696-0
BibTex Citekey: Liwocha2020
 Degree: -

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Project name : NEDD8Activate
Grant ID : 789016
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)
Project name : SCHU 3196/1-1
Grant ID : -
Funding program : -
Funding organization : Deutsche Forschungsgemeinschaft

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Title: Nature Chemical Biology
  Other : Nat. Chem. Biol.
Source Genre: Journal
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Publ. Info: New York, NY : Nature Pub. Group
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ISSN: 1552-4450
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000021290_1