What is the most recent thought on the function(s) for acidic domains in
proteins? So far I have only found these in the context of transcription
factors such as GCN4, Gal4, and the HMG superfamily member UBF. For the
UBF proteins, these acidic domains are long runs of Asp and/or Glu --
much more dramatic than the "overall acidic" transactivation domains
typified by GCN4. Has it been clearly shown that they interact with TAF
proteins? I'm trying to get a foothold on a protein that shares no
database homologies, but it does have a sizeable acidic domain
(internal). Any comments would be appreciated.
Michael Myers
myersm at rockvax.rockefeller.edu
