Role(s) for Acidic Domains?

Yasha Hartberg Yasha at bioch.tamu.edu
Wed Jul 5 08:33:17 EST 1995


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



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