ArticleJournal of the American Chemical Society2011
Nonenzymatic assembly of natural polyubiquitin chains of any linkage composition and isotopic labeling scheme.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 93 citations in OpenAlex.
- Synthetic Strategies for Activity-Based Probes to Decode Ubiquitin-Like Modifiers.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- AmideBiomolecular NMR assignments · 2026Article
- Synthesis of Linkage-Specific Polyubiquitin Probes Using Unnatural Amino Acids.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Thioether-mediated protein ubiquitination in constructing affinity- and activity-based ubiquitinated protein probes.Nature protocols · 2025Review
- Investigating the Interaction Profile of Unconjugated Ubiquitin: Chemical Biology and Affinity Enrichment Mass Spectrometric Approaches.Chembiochem : a European journal of chemical biology · 2025Review
- Selective Lysine Ubiquitination Using Activated Phenol Esters.Chembiochem : a European journal of chemical biology · 2025Article
- Genetic Code Expansion Approaches to Decipher the Ubiquitin Code.Chemical reviews · 2024Review
- Co-translational Installation of Posttranslational Modifications by Non-canonical Amino Acid Mutagenesis.Chembiochem : a European journal of chemical biology · 2023Article
- Functional analysis of protein post-translational modifications using genetic codon expansion.Protein science : a publication of the Protein Society · 2023Review
- Generation of site-specific ubiquitinated histones through chemical ligation to probe the specificities of histone deubiquitinases.Frontiers in epigenetics and epigenomics · 2023Article
- One-Step Sortase-Mediated Chemoenzymatic Semisynthesis of Deubiquitinase-Resistant Ub-Peptide Conjugates.ACS omega · 2022Article
- Linkage-Specific Synthesis of Di-ubiquitin Probes Enabled by the Incorporation of Unnatural Amino Acid ThzK.Chembiochem : a European journal of chemical biology · 2022Article
- The chemical biology of ubiquitin.Biochimica et biophysica acta. General subjects · 2022Review
- Chemical methods for protein site-specific ubiquitination.RSC chemical biology · 2021Review
- Development and application of ubiquitin-based chemical probes.Chemical science · 2020Review
- Selenolysine: A New Tool for Traceless Isopeptide Bond Formation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Protein Engineering in the Ubiquitin System: Tools for Discovery and Beyond.Pharmacological reviews · 2020Review
- Enhancing the incorporation of lysine derivatives into proteins with methylester forms of unnatural amino acids.Bioorganic & medicinal chemistry letters · 2020Article
- Ubiquitin Chains Bearing Genetically Encoded Photo-Cross-Linkers Enable Efficient Covalent Capture of (Poly)ubiquitin-Binding Domains.Biochemistry · 2019Article
- Diubiquitin-Based NMR Analysis: Interactions Between Lys6-Linked diUb and UBA Domain of UBXN1.Frontiers in chemistry · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Polymeric chains made of a small protein ubiquitin act as molecular signals regulating a variety of cellular processes controlling essentially all aspects of eukaryotic biology. Uncovering the mechanisms that allow differently linked polyubiquitin chains to serve as distinct molecular signals requires the ability to make these chains with the native connectivity, defined length, linkage composition, and in sufficient quantities. This, however, has been a major impediment in the ubiquitin field. Here, we present a robust, efficient, and widely accessible method for controlled iterative nonenzymatic assembly of polyubiquitin chains using recombinant ubiquitin monomers as the primary building blocks. This method uses silver-mediated condensation reaction between the C-terminal thioester of one ubiquitin and the ε-amine of a specific lysine on the other ubiquitin. We augment the nonenzymatic approaches developed recently by using removable orthogonal amine-protecting groups, Alloc and Boc. The use of bacterially expressed ubiquitins allows cost-effective isotopic enrichment of any individual monomer in the chain. We demonstrate that our method yields completely natural polyubiquitin chains (free of mutations and linked through native isopeptide bonds) of essentially any desired length, linkage composition, and isotopic labeling scheme, and in milligram quantities. Specifically, we successfully made Lys11-linked di-, tri-, and tetra-ubiquitins, Lys33-linked diubiquitin, and a mixed-linkage Lys33,Lys11-linked triubiquitin. We also demonstrate the ability to obtain, by high-resolution NMR, residue-specific information on ubiquitin units at any desired position in such chains. This method opens up essentially endless possibilities for rigorous structural and functional studies of polyubiquitin signals.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.