Tra1 as a screening target for transcriptional activation domain discovery.
There is tremendous interest in developing activator artificial transcription factors that functionally mimic endogenous transcriptional activators for use as mechanistic probes, as components of synthetic cell circuitry, and in transcription-targeted therapies. Here, we demonstrate that a phage display selection against the transcriptional activation domain binding motif of the coactivator Tra1(TRRAP) produces distinct sequences that function with similar binding modes and potency as natural activators. These findings set the stage for binding screens with small molecule libraries against TAD binding motifs to yield next-generation small molecule TADs.
Majmudar
Chinmay Y
CY
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Labut
Anne E
AE
Mapp
Anna K
AK
D000595:Amino Acid Sequence; D001665:Binding Sites; D051548:Histone Acetyltransferases / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D008969:Molecular Sequence Data; D019151:Peptide Library; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism; D015534:Trans-Activators / Q000737:chemistry*; D015533:Transcriptional Activation
D008024:Ligands; D019151:Peptide Library; D029701:Saccharomyces cerevisiae Proteins; C491364:TRA1 protein, S cerevisiae; D015534:Trans-Activators; D051548:Histone Acetyltransferases