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dc.contributor.author
Hofmann, Raphael
dc.contributor.author
Akimoto, Gaku
dc.contributor.author
Wucherpfennig, Thomas G.
dc.contributor.author
Zeymer, Cathleen
dc.contributor.author
Bode, Jeffrey W.
dc.date.accessioned
2020-11-13T08:58:58Z
dc.date.available
2020-10-01T07:12:18Z
dc.date.available
2020-10-02T09:27:06Z
dc.date.available
2020-11-13T08:58:58Z
dc.date.issued
2020-11
dc.identifier.issn
1755-4349
dc.identifier.issn
1755-4330
dc.identifier.other
10.1038/s41557-020-0528-y
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/443781
dc.description.abstract
Enzymes are powerful tools for protein labelling due to their specificity and mild reaction conditions. Many protocols, however, are restricted to modifications at protein termini, rely on non-peptidic metabolites or require large recognition domains. Here we report a chemoenzymatic method, which we call lysine acylation using conjugating enzymes (LACE), to site-specifically modify folded proteins at internal lysine residues. LACE relies on a minimal genetically encoded tag (four residues) recognized by the E2 small ubiquitin-like modifier-conjugating enzyme Ubc9, and peptide or protein thioesters. Together, this approach obviates the need for E1 and E3 enzymes, enabling isopeptide formation with just Ubc9 in a programmable manner. We demonstrate the utility of LACE by the site-specific attachment of biochemical probes, one-pot dual-labelling in combination with sortase, and the conjugation of wild-type ubiquitin and ISG15 to recombinant proteins.
en_US
dc.language.iso
en
en_US
dc.publisher
Nature Publishing Group
en_US
dc.title
Lysine acylation using conjugating enzymes for site-specific modification and ubiquitination of recombinant proteins
en_US
dc.type
Journal Article
dc.date.published
2020-09-14
ethz.journal.title
Nature Chemistry
ethz.journal.volume
12
en_US
ethz.journal.issue
11
en_US
ethz.journal.abbreviated
Nat Chem
ethz.pages.start
1008
en_US
ethz.pages.end
1015
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
London
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.::02514 - Laboratorium für Organische Chemie / Laboratory of Organic Chemistry::03861 - Bode, Jeffrey W. / Bode, Jeffrey W.
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.::02514 - Laboratorium für Organische Chemie / Laboratory of Organic Chemistry::03861 - Bode, Jeffrey W. / Bode, Jeffrey W.
ethz.relation.isPartOf
10.3929/ethz-b-000475966
ethz.date.deposited
2020-10-01T07:12:27Z
ethz.source
WOS
ethz.eth
yes
en_US
ethz.availability
Metadata only
en_US
ethz.rosetta.installDate
2020-11-13T08:59:10Z
ethz.rosetta.lastUpdated
2021-02-15T20:44:48Z
ethz.rosetta.versionExported
true
ethz.COinS
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