Part:BBa_K4020003

Usage and Biology

The DNA sequence encodes for a highly sequence-specific cysteine protease, a 27‐kDa catalytic domain of the polyprotein nuclear inclusion a (NIa) in tobacco etch virus (Nam et al., 2020). Its target substrate is the sequence ENLYFQS/G and it cleaves between Q and G/S (Nam et al., 2020), all the while requiring a Gly or Ser residue to be in the P1' position so as to process the substrate with reasonable efficiency (Kapust et al., 2002). Located at the interior of the domain, His46, Asp81, and Cys151 comprise the catalytic triad of the TEV protease (Nam et al., 2020). It was acquired from the DualMembrane Kit 3 (Thaminy et al., 2003).

References

• Kapust, R. B., Tözsér, J., Copeland, T. D., & Waugh, D. S. (2002). The P1′ specificity of tobacco etch virus protease. Biochemical and Biophysical Research Communications, 294(5), 949–955. https://doi.org/https://doi.org/10.1016/S0006-291X(02)00574-0
• Nam, H., Hwang, B. J., Choi, D., Shin, S., & Choi, M. (2020). Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self‐cleavage exhibits enhanced enzymatic activity. FEBS Open Bio, 10(4), 619. https://doi.org/10.1002/2211-5463.12828
• Thaminy, S., Auerbach, D., Arnoldo, A., & Stagljar, I. (2003). Identification of Novel ErbB3-Interacting Factors Using the  Split-Ubiquitin Membrane Yeast Two-Hybrid System. Genome Research, 13(7), 1744. https://doi.org/10.1101/GR.1276503