In the case of the N-terminal fusion vectors (pTYB11 and 12), which residues at the N-terminal of the target protein may inhibit cleavage or cause in vivo cleavage?
The data in the table below is based on analysis of cleavage reactions using the MYT4 fusion system in which the Sce VMA intein was fused between E. coli maltose-binding protein (MBP; as the N-extein) and phage T4 DNA ligase (as the C-extein). To investigate the effect of the N-termial residue of a target protein on cleavage in the C-terminal fusion vectors, amino acid substitutions at the first C-extein residue Cys455 were made. In summary, the data indicate that Pro, Cys and Ser are not favourable for thiol-induced cleavage. However, this is not to say that all proteins will behave in the same manner when fused to the intein-chitin binding domain. In each case, the effect of different N-terminal residues on the cleavage reaction has to be evaluated.
Related Questions
- In the case of the N-terminal fusion vectors, pTYB21, pTYB22, pTYB11 and 12, which residues at the N-terminus of the target protein may inhibit cleavage or cause in vivo cleavage?
- In the case of the N-terminal fusion vectors (pTYB11 and 12), which residues at the N-terminal of the target protein may inhibit cleavage or cause in vivo cleavage?
- In the case of the C-terminal fusion vectors (pTYB1,2,3 and 4), which residues at the C-terminal of the target protein may inhibit cleavage or cause in vivo cleavage?
