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Improved protein splicing using embedded split inteins.

Josef A Gramespacher1, Adam J Stevens1, Robert E Thompson1

  • 1Department of Chemistry, Princeton University, Frick Laboratory, Princeton, New Jersey.

Protein Science : a Publication of the Protein Society
|December 12, 2017
PubMed
Summary
This summary is machine-generated.

Researchers developed a new strategy to improve protein trans-splicing (PTS) efficiency by stabilizing split intein fragments. This method reduces aggregation in protein engineering applications, expanding the utility of PTS.

Keywords:
chemical biologyintein splicingprotein engineeringprotein semisynthesis

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Naturally split inteins facilitate protein trans-splicing (PTS), a traceless ligation method.
  • PTS efficiency can be limited by aggregation of split intein fusion constructs.

Purpose of the Study:

  • To develop a strategy to mitigate aggregation issues in split intein fusion constructs.
  • To enhance the efficiency and scope of protein trans-splicing in protein engineering.

Main Methods:

  • Designing stabilizing protein sequences to embed split intein fragments.
  • Utilizing these stabilized fragments in protein ligation experiments.

Main Results:

  • The developed strategy effectively stabilizes split intein fragments.
  • This stabilization reduces aggregation, thereby improving PTS efficiency.

Conclusions:

  • Embedding split inteins within stabilizing protein sequences is a viable strategy to overcome aggregation liabilities.
  • This approach broadens the applicability of protein trans-splicing for complex protein engineering tasks.