Difference between revisions of "Part:BBa K4020008"
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==Usage and Biology== | ==Usage and Biology== | ||
| − | SID (TEV site linker included) VP16 activation domain is a sequence that includes SID linker from SALSA protein,Tobacco Etch Virus (TEV) protease recognition site (Nam et al., 2020) and VP-16 activation domain, which is a transcription factor of herpes simplex virus (HSV) type 1 that is involved in the activation of the viral immediate-early genes (Hirai et al., 2010). SIDs are roughly 20-amino-acid-long threonine-serine-proline-rich stretches consisting of a number of glycosylation sites that proposedly render the linkers to extended conformation, spanning 7 nm (Reichhardt et al., 2020; Turenchalk & Xu, 2001). TEV linker codes for the sequence of amino acids ENLYFQG/S, which TEV protease recognizes and cleaves between Q and G/S (Nam et al., 2020). VP16 is involved in the activation of the viral immediate-early genes (Hirai et al., 2010). | + | SID (TEV site linker included) VP16 activation domain is a sequence that includes SID linker from SALSA protein,Tobacco Etch Virus (TEV) protease recognition site (Nam et al., 2020) and VP-16 activation domain, which is a transcription factor of herpes simplex virus (HSV) type 1 that is involved in the activation of the viral immediate-early genes (Hirai et al., 2010). SIDs are roughly 20-amino-acid-long threonine-serine-proline-rich stretches consisting of a number of glycosylation sites that proposedly render the linkers to extended conformation, spanning 7 nm (Reichhardt et al., 2020; Turenchalk & Xu, 2001). TEV linker codes for the sequence of amino acids ENLYFQG/S, which TEV protease recognizes and cleaves between Q and G/S (Nam et al., 2020). VP16 is involved in the activation of the viral immediate-early genes (Hirai et al., 2010). It was acquired from the DualMembrane Kit 3 (Thaminy et al., 2003). |
==References== | ==References== | ||
| − | * | + | *Hirai, H., Tani, T., & Kikyo, N. (2010). Structure and functions of powerful transactivators: VP16, MyoD and FoxA. The International Journal of Developmental Biology, 54, 1589–1596. https://doi.org/10.1387/ijdb.103194hh |
*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 | *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 | ||
*Reichhardt, M. P., Loimaranta, V., Lea, S. M., & Johnson, S. (2020). Structures of SALSA/DMBT1 SRCR domains reveal the conserved ligand-binding mechanism of the ancient SRCR fold. Life Science Alliance, 3(4). https://doi.org/10.26508/LSA.201900502 | *Reichhardt, M. P., Loimaranta, V., Lea, S. M., & Johnson, S. (2020). Structures of SALSA/DMBT1 SRCR domains reveal the conserved ligand-binding mechanism of the ancient SRCR fold. Life Science Alliance, 3(4). https://doi.org/10.26508/LSA.201900502 | ||
*Turenchalk, G. S., & Xu, T. (2001). Lats in Cell-cycle Regulation and Tumorigenesis BT - Encyclopedic Reference of Cancer. Encyclopedic Reference of Cancer, 491–496. https://doi.org/10.1007/3-540-30683-8_944 | *Turenchalk, G. S., & Xu, T. (2001). Lats in Cell-cycle Regulation and Tumorigenesis BT - Encyclopedic Reference of Cancer. Encyclopedic Reference of Cancer, 491–496. https://doi.org/10.1007/3-540-30683-8_944 | ||
*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 | *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 | ||
Latest revision as of 04:45, 21 October 2021
Usage and Biology
SID (TEV site linker included) VP16 activation domain is a sequence that includes SID linker from SALSA protein,Tobacco Etch Virus (TEV) protease recognition site (Nam et al., 2020) and VP-16 activation domain, which is a transcription factor of herpes simplex virus (HSV) type 1 that is involved in the activation of the viral immediate-early genes (Hirai et al., 2010). SIDs are roughly 20-amino-acid-long threonine-serine-proline-rich stretches consisting of a number of glycosylation sites that proposedly render the linkers to extended conformation, spanning 7 nm (Reichhardt et al., 2020; Turenchalk & Xu, 2001). TEV linker codes for the sequence of amino acids ENLYFQG/S, which TEV protease recognizes and cleaves between Q and G/S (Nam et al., 2020). VP16 is involved in the activation of the viral immediate-early genes (Hirai et al., 2010). It was acquired from the DualMembrane Kit 3 (Thaminy et al., 2003).
References
- Hirai, H., Tani, T., & Kikyo, N. (2010). Structure and functions of powerful transactivators: VP16, MyoD and FoxA. The International Journal of Developmental Biology, 54, 1589–1596. https://doi.org/10.1387/ijdb.103194hh
- 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
- Reichhardt, M. P., Loimaranta, V., Lea, S. M., & Johnson, S. (2020). Structures of SALSA/DMBT1 SRCR domains reveal the conserved ligand-binding mechanism of the ancient SRCR fold. Life Science Alliance, 3(4). https://doi.org/10.26508/LSA.201900502
- Turenchalk, G. S., & Xu, T. (2001). Lats in Cell-cycle Regulation and Tumorigenesis BT - Encyclopedic Reference of Cancer. Encyclopedic Reference of Cancer, 491–496. https://doi.org/10.1007/3-540-30683-8_944
- 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