Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2022 Feb 21:10:810180.
doi: 10.3389/fbioe.2022.810180. eCollection 2022.

Protein Splicing of Inteins: A Powerful Tool in Synthetic Biology

Affiliations
Review

Protein Splicing of Inteins: A Powerful Tool in Synthetic Biology

Hao Wang et al. Front Bioeng Biotechnol. .

Abstract

Inteins are protein segments that are capable of enabling the ligation of flanking extein into a new protein, a process known as protein splicing. Since its discovery, inteins have become powerful biotechnological tools for applications such as protein engineering. In the last 10 years, the development in synthetic biology has further endowed inteins with enhanced functions and diverse utilizations. Here we review these efforts and discuss the future directions.

Keywords: inteins; living therapeutics; protein engineering; split inteins; synthetic biology.

PubMed Disclaimer

Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

FIGURE 1
FIGURE 1
Schematic of protein splicing of inteins (trans-splicing and cis-splicing). (A) The translation of the precursor protein and its splicing in cis. (B) Split intein mediated protein splicing in trans. IntN, split N-intein; IntC, split C-intein.
FIGURE 2
FIGURE 2
Conservative motifs of inteins facilitate protein splicing. The motifs A-G are identified in the intein domain. Block C, D and E are noted in the shadow box, where the split sites of naturally occurring split inteins and homing endonuclease domain (HED)are located.
FIGURE 3
FIGURE 3
The protein splicing mechanism of class 1 intein composes four main steps, in which X is referred to an oxygen or sulfur atom.
FIGURE 4
FIGURE 4
Use of inteins in synthetic biology. (A) Applying inteins to implement biocomputing. (B) Chemical modification of peptide or protein by inteins mediated protein splicing. (C) Living therapeutics constructed by the inteins directed splicing. (D) Materials assembly by protein splicing of inteins.

Similar articles

Cited by

References

    1. Belfort M., Stoddard B. L., Wood D. W., Derbyshire V. (2006). Homing Endonucleases and Inteins. Germany: Springer Science & Business Media.
    1. Borra R., Camarero J. A. (2017). Protein Chemical Modification inside Living Cells Using Split Inteins. Methods Mol. Biol. 1495, 111–130. 10.1007/978-1-4939-6451-2_8 - DOI - PMC - PubMed
    1. Bowen C. H., Sargent C. J., Wang A., Zhu Y., Chang X., Li J., et al. (2021). Microbial Production of Megadalton Titin Yields Fibers with Advantageous Mechanical Properties. Nat. Commun. 12, 5182. 10.1038/s41467-021-25360-6 - DOI - PMC - PubMed
    1. Bowen C. H., Reed T. J., Sargent C. J., Mpamo B., Galazka J. M., Zhang F. (2019). Seeded Chain-Growth Polymerization of Proteins in Living Bacterial Cells. ACS Synth. Biol. 8, 2651–2658. 10.1021/acssynbio.9b00362 - DOI - PubMed
    1. Calles B., Lorenzo V. d. (2013). Expanding the Boolean Logic of the Prokaryotic Transcription Factor XylR by Functionalization of Permissive Sites with a Protease-Target Sequence. ACS Synth. Biol. 2, 594–603. 10.1021/sb400050k - DOI - PubMed

LinkOut - more resources