Difference between revisions of "Part:BBa K4020008"

 
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==Usage and Biology==
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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).
  
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==References==
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*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
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*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
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*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
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*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
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*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