ArticleThe Journal of biological chemistry2015
An Unprecedented Combination of Serine and Cysteine Nucleophiles in a Split Intein with an Atypical Split Site.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
- A Protein Editing Method to Modify Proteins in Live Mammalian Cells.Current protocols · 2026Article
- Generating Ultra-Fast Protein trans-Splicing of a Cysteine-Less and Semisynthetic Split Intein for Chemical Protein Labeling.Chembiochem : a European journal of chemical biology · 2026Article
- An enhanced split intein-mediated ligation (SIML) platform for rapid discovery and functional screening of circular bacteriocins.Frontiers in bioengineering and biotechnology · 2026Article
- Three-Segment Protein Labeling Using a Highly Efficient and Cysteine-Less Split Intein Identified with Computational Prediction of Aggregation Properties.Angewandte Chemie (International ed. in English) · 2025Article
- A Genetically Encoded Homocysteine Precursor to Probe Protein Active Sites and to Addict Escherichia coli to a Noncanonical Amino Acid Directly Involved in Catalysis.Angewandte Chemie (International ed. in English) · 2025Article
- A cysteine-less and ultra-fast split intein rationally engineered from being aggregation-prone to highly efficient in protein trans-splicing.Nature communications · 2025Article
- Conditional Split Inteins: Adaptable Tools for Programming Protein Functions.International journal of molecular sciences · 2025Review
- Systemic delivery of full-length dystrophin in Duchenne muscular dystrophy mice.Nature communications · 2024Article
- Ligation of multiple protein domains using orthogonal inteins with non-native splice junctions.Protein science : a publication of the Protein Society · 2024Article
- Structural and biochemical analysis of a novel atypically split intein reveals a conserved histidine specific to cysteine-less inteins.Chemical science · 2023Article
- Nature-inspired protein ligation and its applications.Nature reviews. Chemistry · 2023Review
- A Conserved Histidine Residue Drives Extein Dependence in an Enhanced Atypically Split Intein.Journal of the American Chemical Society · 2022Article
- SufB intein splicing in Mycobacterium tuberculosis is influenced by two remote conserved N-extein histidines.Bioscience reports · 2022Article
- Increased Protein Encapsulation in Polymersomes with Hydrophobic Membrane Anchoring Peptides in a Scalable Process.International journal of molecular sciences · 2021Article
- Model-guided design of mammalian genetic programs.Science advances · 2021Article
- Biochemical and Structural Characterization of an Unusual and Naturally Split Class 3 Intein.Chembiochem : a European journal of chemical biology · 2021Article
- In Cellulo Protein Semi-Synthesis from Endogenous and Exogenous Fragments Using the Ultra-Fast Split Gp41-1 Intein.Angewandte Chemie (International ed. in English) · 2020Article
- Live-cell protein engineering with an ultra-short split intein.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- A mesophilic cysteine-less split intein for proteinProceedings of the National Academy of Sciences of the United States of America · 2019Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Protein splicing mediated by inteins is a self-processive reaction leading to the excision of the internal intein domain from a precursor protein and the concomitant ligation of the flanking sequences, the extein-N and extein-C parts, thereby reconstituting the host protein. Most inteins employ a splicing pathway in which the upstream scissile peptide bond is consecutively rearranged into two thioester or oxoester intermediates before intein excision and rearrangement into the new peptide bond occurs. The catalytically critical amino acids involved at the two splice junctions are cysteine, serine, or threonine. Notably, the only potential combination not observed so far in any of the known or engineered inteins corresponds to the transesterification from an oxoester to a thioester, which suggested that this formal uphill reaction with regard to the thermodynamic stability might be incompatible with intein-mediated catalysis. We show that corresponding mutations also led to inactive gp41-1 and AceL-TerL inteins. We report the novel GOS-TerL split intein identified from metagenomic databases as the first intein harboring the combination of Ser1 and Cys+1 residues. Mutational analysis showed that its efficient splicing reaction indeed follows the shift from oxoester to thioester and thus represents a rare diversion from the canonical pathway. Furthermore, the GOS-TerL intein has an atypical split site close to the N terminus. The Int(N) fragment could be shortened from 37 to 28 amino acids and exchanged with the 25-amino acid Int(N) fragment from the AceL-TerL intein, indicating a high degree of promiscuity of the Int(C) fragment of the GOS-TerL intein.
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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.