ArticleProtein science : a publication of the Protein Society2013
A conserved threonine spring-loads precursor for intein splicing.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- 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
- Biochemical and Structural Characterization of an Unusual and Naturally Split Class 3 Intein.Chembiochem : a European journal of chemical biology · 2021Article
- Gold Nanoparticles Augment N-Terminal Cleavage and Splicing Reactions inFrontiers in bioengineering and biotechnology · 2021Article
- Inteins in Science: Evolution to Application.Microorganisms · 2020Review
- Spliceosomal Prp8 intein at the crossroads of protein and RNA splicing.PLoS biology · 2019Article
- Structure of an engineered intein reveals thiazoline ring and provides mechanistic insight.Biotechnology and bioengineering · 2019Article
- A functional interplay between intein and extein sequences in protein splicing compensates for the essential block B histidine.Chemical science · 2019Article
- Mycobacterial DnaB helicase intein as oxidative stress sensor.Nature communications · 2018Article
- An Atypical Mechanism of Split Intein Molecular Recognition and Folding.Journal of the American Chemical Society · 2018Article
- Nanobodies: Chemical Functionalization Strategies and Intracellular Applications.Angewandte Chemie (International ed. in English) · 2018Review
- Design of a Split Intein with Exceptional Protein Splicing Activity.Journal of the American Chemical Society · 2016Article
- An Unprecedented Combination of Serine and Cysteine Nucleophiles in a Split Intein with an Atypical Split Site.The Journal of biological chemistry · 2015Article
- Review
- Backbone assignments of mini-RecA intein with short native exteins and an active N-terminal catalytic cysteine.Biomolecular NMR assignments · 2015Article
- Protein splicing: how inteins escape from precursor proteins.The Journal of biological chemistry · 2014Review
- Structural and dynamical features of inteins and implications on protein splicing.The Journal of biological chemistry · 2014Review
- Inteins: Nature's Gift to Protein Chemists.Chemical science · 2014Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
Abstract
Protein splicing is an autocatalytic process where an "intein" self-cleaves from a precursor and ligates the flanking N- and C-"extein" polypeptides. Inteins occur in all domains of life and have myriad uses in biotechnology. Although the reaction steps of protein splicing are known, mechanistic details remain incomplete, particularly the initial peptide rearrangement at the N-terminal extein/intein junction. Recently, we proposed that this transformation, an N-S acyl shift, is accelerated by a localized conformational strain, between the intein's catalytic cysteine (Cys1) and the neighboring glycine (Gly-1) in the N-extein. That proposal was based on the crystal structure of a catalytically competent trapped precursor. Here, we define the structural origins and mechanistic relevance of the conformational strain using a combination of quantum mechanical simulations, mutational analysis, and X-ray crystallography. Our results implicate a conserved, but largely unstudied, threonine residue of the Ssp DnaE intein (Thr69) as the mediator of conformational strain through hydrogen bonding. Further, the strain imposed by this residue is shown to position the splice junction in a manner that enhances the rate of the N-S acyl shift substantially. Taken together, our results not only provide fundamental understanding of the control of the first step of protein splicing but also have important implications in various biotechnological applications that require precursor manipulation.
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