ArticleScientific reports2015
A dual-intein autoprocessing domain that directs synchronized protein co-expression in both prokaryotes and eukaryotes.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Standard Intein Gene Expression Ramps (SIGER) for Protein-Independent Expression Control.ACS synthetic biology · 2023Article
- SufB intein splicing in Mycobacterium tuberculosis is influenced by two remote conserved N-extein histidines.Bioscience reports · 2022Article
- The Effects of Self-cleavage Intein-ELK16 Tag in the Transcript Steric Hindrance of IFN.Indian journal of clinical biochemistry : IJCB · 2021Article
- Gold Nanoparticles Augment N-Terminal Cleavage and Splicing Reactions inFrontiers in bioengineering and biotechnology · 2021Article
- Development and Applications of Superfolder and Split Fluorescent Protein Detection Systems in Biology.International journal of molecular sciences · 2019Review
- Intein-mediated assembly of tunable scaffoldins for facile synthesis of designer cellulosomes.Applied microbiology and biotechnology · 2018Article
- Coordinated protein co-expression in plants by harnessing the synergy between an intein and a viral 2A peptide.Plant biotechnology journal · 2017Article
- Article
- Polycistronic Expression of Multi-Subunit Complexes in the Eukaryotic Environment: A Narrative Review.Iranian journal of parasitologyReview
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
Being able to coordinate co-expression of multiple proteins is necessary for a variety of important applications such as assembly of protein complexes, trait stacking, and metabolic engineering. Currently only few options are available for multiple recombinant protein co-expression, and most of them are not applicable to both prokaryotic and eukaryotic hosts. Here, we report a new polyprotein vector system that is based on a pair of self-excising mini-inteins fused in tandem, termed the dual-intein (DI) domain, to achieve synchronized co-expression of multiple proteins. The DI domain comprises an Ssp DnaE mini-intein N159A mutant and an Ssp DnaB mini-intein C1A mutant connected in tandem by a peptide linker to mediate efficient release of the flanking proteins via autocatalytic cleavage. Essentially complete release of constituent proteins, GFP and RFP (mCherry), from a polyprotein precursor, in bacterial, mammalian, and plant hosts was demonstrated. In addition, successful co-expression of GFP with chloramphenicol acetyltransferase, and thioredoxin with RFP, respectively, further substantiates the general applicability of the DI polyprotein system. Collectively, our results demonstrate the DI-based polyprotein technology as a highly valuable addition to the molecular toolbox for multi-protein co-expression which finds vast applications in biotechnology, biosciences, and biomedicine.
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