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Protein  trans -splicing by split inteins has many uses in protein production and research. Splicing proteins with synthetic peptides, which employs atypical split inteins, is particularly useful for site-specific protein modifications and labeling, because the synthetic peptide can be made to contain a variety of unnatural amino acids and chemical modifications. For this purpose, atypical split inteins need to be engineered to have a small N-intein or C-intein fragment that can be more easily included in a synthetic peptide that also contains a small extein to be  trans -spliced onto target proteins. Here we have successfully engineered multiple atypical split inteins capable of protein  trans -splicing, by modifying and testing more than a dozen natural inteins. These included both S1 split inteins having a very small (11–12 aa) N-intein fragment and S11 split inteins having a very small (6 aa) C-intein fragment. Four of the new S1 and S11 split inteins showed high efficiencies (85–100%) of protein  trans -splicing both in  E. coli  cells and  in vitro . Under  in vitro  conditions, they exhibited reaction rate constants ranging from ∼1.7×10 −4  s −1  to ∼3.8×10 −4  s −1 , which are comparable to or higher than those of previously reported atypical split inteins. These findings should facilitate a more general use of  trans -splicing between proteins and synthetic peptides, by expanding the availability of different atypical split inteins. They also have implications on understanding the structure-function relationship of atypical split inteins, particularly in terms of intein fragment complementation.

Protein Trans-Splicing of Multiple Atypical Split Inteins Engineered from Natural Inteins