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A promiscuous split intein with expanded protein engineering applications.

Adam J Stevens1, Giridhar Sekar2, Neel H Shah1

  • 1Department of Chemistry, Frick Laboratory, Princeton University, Princeton, NJ 08544.

Proceedings of the National Academy of Sciences of the United States of America
|July 26, 2017
PubMed
Summary
This summary is machine-generated.

We engineered protein trans-splicing (PTS) inteins to reduce extein dependence, enhancing their utility in protein cyclization and semisynthesis. These promiscuous inteins offer broader applications in biotechnology and chemical biology.

Keywords:
chemical biologyintein splicingprotein engineeringprotein semisynthesis

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biotechnology

Background:

  • Protein trans-splicing (PTS) relies on split inteins for joining protein fragments.
  • Naturally split inteins exhibit extein dependence, limiting their versatility due to sequence-specific splicing efficiencies.

Purpose of the Study:

  • To engineer split inteins with minimal extein dependence for broader PTS applications.
  • To develop more robust and generally applicable reagents for protein engineering.

Main Methods:

  • Mechanism-guided protein engineering of ultrafast DnaE split inteins.
  • Assessing splicing efficiency across various extein contexts.
  • Application of engineered inteins in protein cyclization and semisynthesis.

Main Results:

  • Developed "promiscuous" split inteins with significantly reduced extein dependence.
  • Demonstrated superior performance in protein cyclization and semisynthesis compared to existing inteins.
  • Successfully modified native cellular chromatin using the engineered inteins.

Conclusions:

  • The engineered promiscuous inteins enhance the applicability of PTS methods.
  • This work provides a foundation for engineering promiscuity into other split inteins.
  • Opens new avenues for protein modification and engineering in biological systems.