Difference between revisions of "Part:BBa K4020000"
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==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 |
*Jonker, H. R. A., Wechselberger, R. W., Boelens, R., Folkers, G. E., & Kaptein, R. (2005). Structural Properties of the Promiscuous VP16 Activation Domain. Biochemistry, 44(3), 827–839. https://doi.org/10.1021/bi0482912 | *Jonker, H. R. A., Wechselberger, R. W., Boelens, R., Folkers, G. E., & Kaptein, R. (2005). Structural Properties of the Promiscuous VP16 Activation Domain. Biochemistry, 44(3), 827–839. https://doi.org/10.1021/bi0482912 | ||
*Thliveris, A. T., & Mount, D. W. (1992). Genetic identification of the DNA binding domain of Escherichia coli LexA protein. Proceedings of the National Academy of Sciences, 89(10), 4500–4504. https://doi.org/10.1073/PNAS.89.10.4500 | *Thliveris, A. T., & Mount, D. W. (1992). Genetic identification of the DNA binding domain of Escherichia coli LexA protein. Proceedings of the National Academy of Sciences, 89(10), 4500–4504. https://doi.org/10.1073/PNAS.89.10.4500 | ||
*Zhang, A. P. P., Pigli, Y. Z., & Rice, P. A. (2010). Structure of the LexA-DNA complex and implications for SOS box measurement. Nature, 466(7308), 883. https://doi.org/10.1038/NATURE09200 | *Zhang, A. P. P., Pigli, Y. Z., & Rice, P. A. (2010). Structure of the LexA-DNA complex and implications for SOS box measurement. Nature, 466(7308), 883. https://doi.org/10.1038/NATURE09200 | ||
*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 04:20, 21 October 2021
Usage and Biology
LexA binding domain - VP16 activation domain is a synthetic transcription factor. LexA Binding Domain is a sequence in the LexA protein, a transcriptional repressor (Zhang et al., 2010) of the SOS regulon in Escherichia coli that allows the binding of different regulatory molecules (Thliveris & Mount, 1992). VP16 is a transcription factor from herpes simplex virus (HSV) type 1 that is involved in the activation of the viral immediate-early (IE) genes (Hirai et al., 2010). The N-terminal region of the protein confers specificity for the IE genes, whilst the C-terminal part contains two functional regions, VP16ad/c and VP16ad/n, that are required for transcriptional activation (Jonker et al., 2005). 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
- Jonker, H. R. A., Wechselberger, R. W., Boelens, R., Folkers, G. E., & Kaptein, R. (2005). Structural Properties of the Promiscuous VP16 Activation Domain. Biochemistry, 44(3), 827–839. https://doi.org/10.1021/bi0482912
- Thliveris, A. T., & Mount, D. W. (1992). Genetic identification of the DNA binding domain of Escherichia coli LexA protein. Proceedings of the National Academy of Sciences, 89(10), 4500–4504. https://doi.org/10.1073/PNAS.89.10.4500
- Zhang, A. P. P., Pigli, Y. Z., & Rice, P. A. (2010). Structure of the LexA-DNA complex and implications for SOS box measurement. Nature, 466(7308), 883. https://doi.org/10.1038/NATURE09200
- 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