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Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler.
- Source :
-
Nature chemical biology [Nat Chem Biol] 2021 Mar; Vol. 17 (3), pp. 272-279. Date of Electronic Publication: 2020 Dec 07. - Publication Year :
- 2021
-
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.
- Subjects :
- Binding Sites
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli genetics
Escherichia coli metabolism
Gene Expression
Genetic Vectors chemistry
Genetic Vectors metabolism
Humans
Kinetics
Lysine metabolism
Models, Molecular
NEDD8 Protein genetics
NEDD8 Protein metabolism
Nuclear Proteins chemistry
Nuclear Proteins genetics
Nuclear Proteins metabolism
Polyubiquitin genetics
Polyubiquitin metabolism
Protein Binding
Protein Interaction Domains and Motifs
Protein Structure, Secondary
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Substrate Specificity
Transcription Factors chemistry
Transcription Factors genetics
Transcription Factors metabolism
Ubiquitin genetics
Ubiquitin metabolism
Ubiquitin-Conjugating Enzymes chemistry
Ubiquitin-Conjugating Enzymes genetics
Ubiquitin-Conjugating Enzymes metabolism
Ubiquitination
Lysine chemistry
NEDD8 Protein chemistry
Polyubiquitin chemistry
Protein Processing, Post-Translational
Ubiquitin chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1552-4469
- Volume :
- 17
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Nature chemical biology
- Publication Type :
- Academic Journal
- Accession number :
- 33288957
- Full Text :
- https://doi.org/10.1038/s41589-020-00696-0