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Gal4 activation domain 9aaTAD could be inactivated by adjacent mini-inhibitory domain and reactivated by distal re-activation domain

Martin Piskacek, Marek Havelka, Martina Rezacova, Andrea Knight
doi: https://doi.org/10.1101/110882
Martin Piskacek
1Laboratory of Cancer Biology and Genetic, Department of Pathological Physiology, Faculty of Medicine, Masaryk University Brno, Kamenice 5, 625 00 Brno, Czech Republic Laboratory
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  • For correspondence: Piskacek@med.muni.cz
Marek Havelka
1Laboratory of Cancer Biology and Genetic, Department of Pathological Physiology, Faculty of Medicine, Masaryk University Brno, Kamenice 5, 625 00 Brno, Czech Republic Laboratory
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Martina Rezacova
1Laboratory of Cancer Biology and Genetic, Department of Pathological Physiology, Faculty of Medicine, Masaryk University Brno, Kamenice 5, 625 00 Brno, Czech Republic Laboratory
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Andrea Knight
2Gamma Delta T Cell Laboratory, Department of Pathological Physiology, Faculty of Medicine, Masaryk University Brno, Kamenice 5, 625 00 Brno, Czech Republic Laboratory
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Abstract

The characterisation of the activation domains started three decades ago with Gcn4 and Gal4 activators. The amorphous character of the activation domains strongly hindered their definition. Moreover, during the attempts to localise the Gal4 activation domain, the artificial peptides, an unintended consequence of cloning, were responsible for artificial transcriptional activity of the several Gal4 constructs. These artefacts produced enormous experimental bias and misconception. The presence of inhibitory domains in some Gal4 constructs made the misperception even worse. Previously, we reported that the nine amino acid transactivation domain, 9aaTAD, is the exclusive activation domain in the Gal4 protein. The activation domain 9aaTAD could be identified in Gal4 paralogs Oaf1, Pip2, Pdr1, Pdr3 and other activators p53, E2A and MLL. Surprisingly, the activation domain 9aaTAD was reported as misconception for Gal4 activator. Here we demonstrated that small region of 10 amino acids adjacent to the Gal4 activation domain 9aaTAD is an inhibitory domain, which the authors included in their constructs. Moreover, we identified Gal4 region, which was able to the reverse the inhibitory effect. The 9aaTAD re-activation domain was localized to the 13 amino acid long region. In this report we clarified the numerous confusions and rebutted supposed 9aaTAD misconception.

Summary The activation domain 9aaTAD has decisive function in Gal4 activation. Gal4 activation domain 9aaTAD could be inhibited by adjacent region of 10 amino acids. The inhibited Gal4 activation domain 9aaTAD could be reactivated by 13 amino acid long Gal4 region. The activation domains 9aaTAD could be identified by our 9aaTAD prediction algorithm, especially in the Gal4 family.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted February 22, 2017.
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Gal4 activation domain 9aaTAD could be inactivated by adjacent mini-inhibitory domain and reactivated by distal re-activation domain
Martin Piskacek, Marek Havelka, Martina Rezacova, Andrea Knight
bioRxiv 110882; doi: https://doi.org/10.1101/110882
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Gal4 activation domain 9aaTAD could be inactivated by adjacent mini-inhibitory domain and reactivated by distal re-activation domain
Martin Piskacek, Marek Havelka, Martina Rezacova, Andrea Knight
bioRxiv 110882; doi: https://doi.org/10.1101/110882

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