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Area of Science:

  • Biochemistry
  • Chemical Biology
  • Protein Engineering

Background:

  • Semisynthetic proteins with non-coded elements, such as post-translational modifications (PTMs), are valuable tools for studying biological processes.
  • Existing methods for creating such proteins can be limited in scope and accessibility.

Purpose of the Study:

  • To develop a versatile, one-pot chemoenzymatic method for broad access to chemically modified proteins.
  • To demonstrate the utility of this method for introducing PTMs and biochemical probes into various proteins and native chromatin.

Main Methods:

  • A tandem transamidation reaction cascade integrating intein-mediated protein splicing with enzyme-mediated peptide ligation.
  • Application of the method to engineer Cas9 nuclease, MeCP2 (a transcriptional regulator implicated in Rett syndrome), and histone proteins.

Main Results:

  • Successful introduction of PTMs and biochemical probes into diverse proteins using the developed method.
  • Demonstration of chemical tailoring of histone proteins within a native chromatin environment.
  • Broad applicability of the chemoenzymatic approach for protein engineering.

Conclusions:

  • The developed one-pot chemoenzymatic method provides efficient and versatile access to semisynthetic proteins with non-coded elements.
  • This approach expands the capabilities of protein engineering and facilitates the study of complex biological systems.
  • The method holds promise for advancing research in areas such as epigenetics and gene regulation.