A sequence-specific transcription activator motif and powerful synthetic variants that bind Mediator using a fuzzy protein interface.

ABSTRACT: Although many transcription activators contact the same set of coactivator complexes, the mechanism and specificity of these interactions have been unclear. For example, do intrinsically disordered transcription activation domains (ADs) use sequence-specific motifs, or do ADs of seemingly different sequence have common properties that encode activation function? We find that the central activation domain (cAD) of the yeast activator Gcn4 functions through a short, conserved sequence-specific motif. Optimizing the residues surrounding this short motif by inserting additional hydrophobic residues creates very powerful ADs that bind the Mediator subunit Gal11/Med15 with high affinity via a "fuzzy" protein interface. In contrast to Gcn4, the activity of these synthetic ADs is not strongly depe

SUBMITTER: Warfield L 

PROVIDER: S-EPMC4151740 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature