Skip to main content
. Author manuscript; available in PMC: 2019 Mar 15.
Published in final edited form as: Bioorg Med Chem. 2017 Sep 6;26(6):1212–1219. doi: 10.1016/j.bmc.2017.09.002

Table 1.

The Npu DnaE split-intein shows high sequence tolerance at the N- and C-extein/intein junctions while keeping high protein trans-splicing activity. The table shows the N- and C-extein sequences found in the Npu Dna split-intein and in several protein constructs used for the production of different backbone cyclized polypeptides. Only the last and first five residues of the N- and C-extein are shown, respectively. The first and last residues of the IN and IC polypeptides, respectively, are highlighted in bold.

Spliced protein IC/C-extein
junction		 N-extein/IN
junction		 Splicing
efficiency		 References
Npu DnaE pola N-CFNKS EVFEY-C ≈80%a 27,28
MCoTI-Ib N-CGSGS RGNGY-C >98% 29,30
SFTI-Ib N-CTKSI FPDGR-C >98% 31
N-CFPDG SIPPI-C >98%
RTD-1b N-CRCLC CTRGF-C ≥95% This work
a

Intermolecular protein trans-splicing results in the production of full-length DnaE Pol

b

Intramolecular protein trans-splicing results in the production of backbone cyclized polypeptides