Evidence That Gal11 Protein Is a Target of the Gal4 Activation Domain in the Mediator†

Biochemistry ◽  
2001 ◽  
Vol 40 (31) ◽  
pp. 9421-9427 ◽  
Author(s):  
Choon-Ju Jeong ◽  
Sang-Hwa Yang ◽  
Yueqing Xie ◽  
Lei Zhang ◽  
Stephen Albert Johnston ◽  
...  
Keyword(s):  
Activation Domain ◽  
Gal4 Activation Domain

scholarly journals Biochemical Characterization of the TATA-binding Protein-Gal4 Activation Domain Complex

2000 ◽  
Vol 275 (41) ◽  
pp. 31914-31920 ◽  
Author(s):  
Yueqing Xie ◽  
Carilee Denison ◽  
Sang-Hwa Yang ◽  
David A. Fancy ◽  
Thomas Kodadek
Keyword(s):  
Biochemical Characterization ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Activation Domain ◽  
Gal4 Activation Domain

scholarly journals The Gal4 Activation Domain Binds Sug2 Protein, a Proteasome Component,in Vivoandin Vitro

2001 ◽  
Vol 276 (33) ◽  
pp. 30956-30963 ◽  
Author(s):  
Cathy Chang ◽  
Fernando Gonzalez ◽  
Beverly Rothermel ◽  
Liping Sun ◽  
Stephen Albert Johnston ◽  
...  
Keyword(s):  
Protein A ◽  
Activation Domain ◽  
Gal4 Activation Domain

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

2017 ◽  
Author(s):  
Martin Piskacek ◽  
Marek Havelka ◽  
Martina Rezacova ◽  
Andrea Knight
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Small Region ◽  
Inhibitory Effect ◽  
Prediction Algorithm ◽  
Transactivation Domain ◽  
Activation Domain ◽  
Activation Domains ◽  
Gal4 Activation Domain ◽  
Inhibitory Domain

AbstractThe 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.SummaryThe 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.

Identification of Gal4 activation domain-binding proteins in the 26S proteasome by periodate-triggered cross-linking

2005 ◽  
Vol 1 (5-6) ◽  
pp. 366 ◽  
Author(s):  
Chase T. Archer ◽  
Lyle Burdine ◽  
Thomas Kodadek
Keyword(s):  
Binding Proteins ◽  
26S Proteasome ◽  
Cross Linking ◽  
Activation Domain ◽  
Gal4 Activation Domain

Activation domain requirements for disruption of Epstein-Barr virus latency by ZEBRA.

1997 ◽  
Vol 71 (9) ◽  
pp. 6547-6554 ◽  
Author(s):  
S Asković ◽  
R Baumann
Keyword(s):  
Epstein Barr Virus ◽  
Activation Domain ◽  
Barr Virus ◽  
Virus Latency ◽  
Epstein Barr
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