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Liwocha, J.* ; Krist, D.T.* ; van der Heden van Noort, G.J.* ; Hansen, F.M.* ; Truong, V.H.* ; Karayel, O.* ; Purser, N.* ; Houston, D.* ; Burton, N.* ; Bostock, M.J. ; Sattler, M. ; Mann, M.* ; Harrison, J.S.* ; Kleiger, G.* ; Ovaa, H.* ; Schulman, B.A.*

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

Nat. Chem. Biol. 17, 272–279 (2021)
Postprint Research data DOI PMC
Open Access Green
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.]
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Publication type Article: Journal article
Document type Scientific Article
Keywords Structural Basis; Molecular-basis; Mechanism; Reveals; Conjugation; Complex; Ligases; Polyubiquitination; Determinants; Degradation
Language english
Publication Year 2021
Prepublished in Year 2020
HGF-reported in Year 2020
ISSN (print) / ISBN 1552-4450
e-ISSN 1552-4469
Journal Nature Chemical Biology
Quellenangaben Volume: 17, Issue: , Pages: 272–279 Article Number: , Supplement: ,
Publisher Nature Publishing Group
Publishing Place Basingstoke
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-503000-001
Grants Deutsche Forschungsgemeinschaft (DFG, German Research foundation)
Max Planck Society
National Institutes of Health
NWO (VIDI)
NWO (Off-Road)
VICI grant from the Netherlands Foundation for Scientific Research (NWO)
German Research Foundation DFG
European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme
DOI 10.1038/s41589-020-00696-0
WOS ID WOS:000599030300001
Scopus ID 85097243724
PubMed ID 33288957
Erfassungsdatum 2020-12-14
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