Part:BBa_K4200780
Ssp GyrB S11 split intein
Ssp GyrB S11 split intein consists of N-extein that is responsible for splicing at the N-terminal.
Usage and Biology
The intein is derived from the Synechocystis sp GyrB protein. The split intein was derived by its comparison with other similar inteins and selection of only the conserved region, which was believed to be involved in trans-splicing. The split intein can also carry out N-terminus cleavage in presence of strong nucleophilic chemicals such as Dithiothreitol(DTT). Thus the intein can be used to produce small peptides in Escherichia coli. The small peptides are unstable due to their susceptibility to degradation. The addition of carrier proteins can generally stabilize such peptides. In our case, not only does the split intein stabilize the peptides being produced from Escherichia coli, but it also has the additional function of being able to cleave itself from the peptide. It has been reported in the literature that this cleavage doesn't occur in vivo, thus eliminating the possibility of reduced yield. The cleavage is only induced in the presence of 6 amino acid long C-extein and small amounts of DTT. It can also be induced using higher quantities of DTT.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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