Part:BBa_K1075017
RBS32-sspB[Core]-LOV-ipaA-TT ipaA forms a tight dimer with Vincolin. LOV is a light-sensitive protein domain which was fused to ipaA. That way the dimerization of ipaA and Vincolin was rendered light-induced.
EcsspB itself regulates the degradation of ssrA tagged proteins through the ClpXP protease in procaryotes. In engineered systems it is used to induce degradation of specifically ssrA tagged proteins. The XB domain of sspB is part of the split system of E. Coli sspB (EcsspB) which was used in fusion with FKBP and FRB to induce the activity of sspB and therefore degradation of proteins with Rapamycins. [1] EcsspB can be functionally divided in three parts: -the N terminal Core domain (113 AA) -the C terminal XB peptide (25 AA) -and a 'flexible linker' in between the first parts ( We used the same domain structure as is used within the Rapamycin inducable split system. While the Core domain is responsible for dimerization of sspB and binding of ssrA the XB domain binds the protease ClpXP. The flexible linker is called flexible because it was found that an increase or reduction in size or amino acid composition does not influence the function of sspB as much as it would in the other domains.
The part can be used to regulate the dimerization of the two parts of the split sspB. The binding of ipaA to Vincolin is regulated via the light-sensitive LOV domain. Therefore the two sspB parts only come together when the LOV domain was activated with blue light.
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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