ArticleNature methods2016
A bacterial genetic selection system for ubiquitylation cascade discovery.
Article in Nature methods, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Proximal Co-Translation Facilitates Detection of Weak Protein-Protein Interactions.International journal of molecular sciences · 2024Article
- BLADE-ON-PETIOLE interacts with CYCLOIDEA to fine-tuneScience advances · 2024Article
- K128 ubiquitination constrains RAS activity by expanding its binding interface with GAP proteins.The EMBO journal · 2024Article
- Probing protein ubiquitination in live cells.Nucleic acids research · 2022Article
- The importance of residue-level filtering and the Top2018 best-parts dataset of high-quality protein residues.Protein science : a publication of the Protein Society · 2022Article
- An Integrative Synthetic Biology Approach to Interrogating Cellular Ubiquitin and Ufm Signaling.International journal of molecular sciences · 2020Article
- Protein Engineering in the Ubiquitin System: Tools for Discovery and Beyond.Pharmacological reviews · 2020Review
- Remodeling Membrane Binding by Mono-Ubiquitylation.Biomolecules · 2019Article
- The MALDI-TOF E2/E3 Ligase Assay as Universal Tool for Drug Discovery in the Ubiquitin Pathway.Cell chemical biology · 2018Article
- Identifying the substrate proteins of U-box E3s E4B and CHIP by orthogonal ubiquitin transfer.Science advances · 2018Article
- Structure and evolution of ENTH and VHS/ENTH-like domains in tepsin.Traffic (Copenhagen, Denmark) · 2017Article
- Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism.Nature communications · 2016Article
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Authors and funding
16 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
About one-third of the eukaryotic proteome undergoes ubiquitylation, but the enzymatic cascades leading to substrate modification are largely unknown. We present a genetic selection tool that utilizes Escherichia coli, which lack deubiquitylases, to identify interactions along ubiquitylation cascades. Coexpression of split antibiotic resistance protein tethered to ubiquitin and ubiquitylation target together with a functional ubiquitylation apparatus results in a covalent assembly of the resistance protein, giving rise to bacterial growth on selective media. We applied the selection system to uncover an E3 ligase from the pathogenic bacteria EHEC and to identify the epsin ENTH domain as an ultraweak ubiquitin-binding domain. The latter was complemented with a structure-function analysis of the ENTH-ubiquitin interface. We also constructed and screened a yeast fusion library, discovering Sem1 as a novel ubiquitylation substrate of Rsp5 E3 ligase. Collectively, our selection system provides a robust high-throughput approach for genetic studies of ubiquitylation cascades and for small-molecule modulator screening.
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