Part:BBa_K2387071
Constitutive TEV protease
This TEV protease is an optimized TEV protease with anti-self cleavage mutation S219V for expression in E. coli. This enzyme is a 27kDa molecule whose encoding sequence contains the S219V anti-self cleavage mutation.
The TEV Protease is a highly sequence specific cysteine protease from the Tobacco Edge Virus (TEV). The TEV protease cuts in a consensus sequence (ENLYFQ-S) being - the cleaved peptide bond. This cutting sequence BBa_K131901) is the optimal cleavage site which shows the highest activity. However, the protease is also active at different extents on a range of substrates. The TEV protease gene is expressed under the pLac promoter which is active in a constitutive level as Lactose is not expressed by the plasmid.
This construct was tested in the construction of a two-interdependent component system mechanism. In this mechanism, two bacterial cell populations were combined. One of them encoding for a consecutively expressed GFP quenched by a quenching molecule (two mechanisms were tested) and the second one encoding for the constitutivelly expressed TEV protease. The results can be seen here.
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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