ArticleACS chemical biology2016
Construction of Lasso Peptide Fusion Proteins.
Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Precursor gene engineering expands the loop region of the lasso peptide microcin J25.RSC chemical biology · 2026Article
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Repositioning the Leader Peptide in Graspetide Biosynthesis.Journal of the American Chemical Society · 2026Article
- AlphaLasso-a web server to identify loop and lasso motifs in 3D structure of biopolymers.Nucleic acids research · 2025Article
- Lasso peptides: A focus on therapeutic index.World journal of microbiology & biotechnology · 2025Review
- Substrate interactions guide cyclase engineering and lasso peptide diversification.Nature chemical biology · 2025Article
- Advances in lasso peptide discovery, biosynthesis, and function.Trends in genetics : TIG · 2024Review
- Article
- Utilization of lasso peptides for biodegradation of polycyclic aromatic hydrocarbons.Environmental microbiology reports · 2024Article
- Lasso Peptides: Exploring the Folding Landscape of Nature's Smallest Interlocked Motifs.Journal of the American Chemical Society · 2024Article
- A single-domain protein catenane of dihydrofolate reductase.National science review · 2023Article
- Multicopy Chromosome Integration and Deletion of Negative Global Regulators Significantly Increased the Heterologous Production of Aborycin inMarine drugs · 2023Article
- Selection for constrained peptides that bind to a single target protein.Nature communications · 2021Article
- Engineering of new-to-nature ribosomally synthesized and post-translationally modified peptide natural products.Current opinion in biotechnology · 2021Review
- Cell-Free Biosynthesis to Evaluate Lasso Peptide Formation and Enzyme-Substrate Tolerance.Journal of the American Chemical Society · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Recent Advances and Perspectives on Expanding the Chemical Diversity of Lasso Peptides.Frontiers in bioengineering and biotechnology · 2021Review
- How to harness biosynthetic gene clusters of lasso peptides.Journal of industrial microbiology & biotechnology · 2020Review
- Lasso Peptides: Heterologous Production and Potential Medical Application.Frontiers in bioengineering and biotechnology · 2020Review
- Pandonodin: A Proteobacterial Lasso Peptide with an Exceptionally Long C-Terminal Tail.ACS chemical biology · 2019Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Lasso peptides are a family of ribosomally synthesized and post-translationally modified peptides (RiPPs) typified by an isopeptide-bonded macrocycle between the peptide N-terminus and an aspartate or glutamate side chain. The C-terminal portion of the peptide threads through the N-terminal macrocycle to give the characteristic lasso fold. Because of the inherent stability, both proteolytic and often thermal, of lasso peptides, we became interested in whether proteins could be fused to the free C-terminus of lasso peptides. Here, we demonstrate fusion of two model proteins, the artificial leucine zipper A1 and the superfolder variant of GFP, to the C-terminus of the lasso peptide astexin-1. Successful lasso cyclization of the N-terminus of these fusion proteins requires a flexible linker in between the C-terminus of the lasso peptide and the N-terminus of the protein of interest. The ability to fuse lasso peptides to a protein of interest is an important step toward phage and bacterial display systems for the high-throughput screening of lasso peptide libraries for new functions.
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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.