In article <DB7tH5.Gwu at rockyd.rockefeller.edu>,
myersm at rockyj.rockefeller.edu (Michael Myers) wrote:
> 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.
I have recently been doing some literature searches into a similar
question. From what I have found so far I conclude that not a lot of
resaerch has been done to elucidate the roles of these or other
homopolymeric repeats or amino acid rich regions in proteins. For
instance, a number of developmentally regulated proteins contain
homopolymeric repeats. G-box Binding Factor from Dictyostelium is nearly
50% Gln, Asn, and Ser by composition. I find these repeats remarkable and
have been frustrated about the lack of information about their roles in
protein structure and function. I may have some references you would find
useful and would be happy to email them to you if you are interested.
Yasha Hartberg
Texas A&M University
"The most beautiful thing in Tokyo is McDonald's." Andy Warhol
