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Related Concept Videos

RNA Splicing01:32

RNA Splicing

Splicing is the process by which eukaryotic RNA is edited before its translation into protein. The RNA strand transcribed from eukaryotic DNA is called the primary transcript. The primary transcripts that become mRNAs are called precursor messenger RNAs (pre-mRNAs). Eukaryotic pre-mRNA contains alternating sequences of exons and introns. Exons are nucleotide sequences that code for proteins, whereas introns are the non-coding regions. In RNA splicing, introns are removed and exons are bonded...
RNA Splicing01:32

RNA Splicing

Splicing is the process by which eukaryotic RNA is edited before its translation into protein. The RNA strand transcribed from eukaryotic DNA is called the primary transcript. The primary transcripts that become mRNAs are called precursor messenger RNAs (pre-mRNAs). Eukaryotic pre-mRNA contains alternating sequences of exons and introns. Exons are nucleotide sequences that code for proteins, whereas introns are the non-coding regions. In RNA splicing, introns are removed and exons are bonded...
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Restriction Enzymes01:11

Restriction Enzymes

Restriction enzymes are bacterial enzymes used to cut DNA in a sequence-specific manner. To cleave DNA, they bind to specific palindromic sequences called restriction sites. Such palindromic DNA sequences or inverted repeats are commonly found in regions of functional significance, such as the origin of replication, gene operator sites, and regions containing transcription termination signals.
The host bacteria protect their own genomic DNA from these enzymes by methylating these sites. Some...

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Related Experiment Video

Updated: May 11, 2026

Synthesis of an Intein-mediated Artificial Protein Hydrogel
15:06

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Published on: January 27, 2014

Split Inteins: Nature's Protein Ligases.

Neel H Shah1, Tom W Muir

  • 1Department of Chemistry, Princeton University, 325 Frick Laboratory, Princeton, New Jersey 08544, USA, Telephone: 609-258-5778.

Israel Journal of Chemistry
|April 27, 2013
PubMed
Summary
This summary is machine-generated.

Split inteins enable protein trans-splicing for biotechnology. Further research into split intein structure and function is needed to overcome limitations and expand their practical applications.

Keywords:
protein semisynthesisprotein splicing

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biotechnology

Background:

  • Split inteins are naturally occurring protein fragments that perform protein trans-splicing.
  • This process involves the binding of two fragments to form an active enzyme, which then catalyzes its own excision and the ligation of flanking sequences.
  • Split intein technologies have been developed for various biotechnological applications, primarily for forming native peptide bonds.

Purpose of the Study:

  • To discuss the development and applications of split intein-based technologies.
  • To identify the limitations hindering the widespread practical use of these technologies.
  • To propose that a deeper understanding of split intein structure and function is crucial for future advancements.

Main Methods:

  • Review of existing literature on split intein research.
  • Analysis of current biotechnological applications of protein trans-splicing.
  • Identification of limitations and challenges in split intein technology.

Main Results:

  • Split inteins have been successfully utilized in exogenous systems for protein ligation.
  • Numerous biotechnological applications have emerged, focusing on native peptide bond formation.
  • Several factors currently restrict the broader adoption and practical utility of these technologies.

Conclusions:

  • Split intein-mediated protein trans-splicing offers significant potential in biotechnology.
  • Overcoming current limitations requires a more comprehensive understanding of the fundamental structure and function of split inteins.
  • Future progress hinges on addressing these knowledge gaps to unlock the full capabilities of split intein technologies.