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Sortase A: A Model for Transpeptidation and Its Biological Applications
Novalia Pishesha1,2, Jessica R Ingram3, Hidde L Ploegh1
1Program in Molecular and Cellular Medicine, Boston Children's Hospital, Boston, Massachusetts 02115, USA;
Annual Review of Cell and Developmental Biology
|August 16, 2018
Summary
Researchers are using transpeptidases, like sortase A, to modify proteins with novel substituents not achievable through genetic engineering. This enzyme-catalyzed approach offers new possibilities for protein engineering in vitro and in living cells.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Engineering
Background:
- Standard and advanced genetic methods have limitations in introducing specific substituents to proteins.
- Nature utilizes transpeptidases and peptide ligases for enzyme-catalyzed peptide bond formation.
- Directed evolution has improved these enzymes for various biological applications.
Purpose of the Study:
- To describe the application of transpeptidases for protein modification.
- To highlight the utility of sortase A as a versatile tool for protein engineering.
Main Methods:
- Utilizing transpeptidases, specifically sortase A, for protein modification.
- Employing enzyme-catalyzed reactions for installing non-genetic substituents.
- Applying these methods both in vitro and within living cellular systems.
Main Results:
- Demonstrated the successful modification of proteins with substituents beyond genetic capabilities.
- Showcased the broad applicability of sortase A in diverse protein engineering tasks.
- Validated the efficacy of transpeptidase-mediated modifications in both cell-free and cellular environments.
Conclusions:
- Transpeptidases, particularly sortase A, provide a powerful platform for novel protein functionalization.
- This enzymatic approach overcomes limitations of traditional genetic engineering for protein modification.
- Sortase A is a valuable and adaptable tool for advanced protein engineering applications.
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