Part:BBa_K2923013:Design

Properties

This protein specifically recognizes the LexA operator sequence, which contains a mutated half-site (CCGT) with the LexA domain and links MS2-MS2-Aptazyme-PP7-PP7 by its MS2cp domain. LexA mutated repressor did not contain stop-codon.

Sources

This part corresponds to selected LexA mutated repressor (WT sequence coming from E. coli strain JL1434) [Dimitrova, M., Younès-Cauet, G., Oertel-Buchheit, P., Porte, D., Schnarr, M., and Granger-Schnarr, M. (1998). A new LexA-based genetic system for monitoring and analyzing protein heterodimerization in Escherichia coli. Molecular and General Genetics MGG 257, 205–212.] PP7cp was amplified with overlapping sequences for Gibson assembly from BH3 plasmids [Berry, K.E., and Hochschild, A. (2018). A bacterial three-hybrid assay detects Escherichia coli Hfq-sRNA interactions in vivo. Nucleic Acids Research 46]

References

Berry, K.E., and Hochschild, A. (2018). A bacterial three-hybrid assay detects Escherichia coli Hfq-sRNA interactions in vivo. Nucleic Acids Research 46 Dimitrova, M., Younès-Cauet, G., Oertel-Buchheit, P., Porte, D., Schnarr, M., and Granger-Schnarr, M. (1998). A new LexA-based genetic system for monitoring and analyzing protein heterodimerization in Escherichia coli. Molecular and General Genetics MGG 257, 205–212. Daines DA, Granger-Schnarr M, Dimitrova M, Silver RP. 2002. Use of LexA-based system to identify protein-protein interactions in vivo. Methods Enzymol 358:153–161. Daines DA, Silver RP. 2000. Evidence for multimerization of Neu proteins involved in polysialic acid synthesis in Escherichia coli K1 using improved LexA-based vectors. J Bacteriol 182:5267–5270