From: David Iain Greig
     To: All
Subject: TATA-Binding Protein (or TFIID-tau, if you like)

From: greig@medusa.oci.utoronto.ca (David Iain Greig)
Organization: NMR Core Facility, Dept. of Biochemistry, University of Ediacara

We were privileged enough to get Steven Burley to give a seminar here in
Toronto last week, and he spoke on his work on the 3D structure of TATA
Binding Protein(1).  One interesting overhead he showed has of sequence
homology in the 180 amino acid C-terminal domain of TBP.

The homology of hTBP and other species TBP(2):

Species		      % Amino Acid Identity (NOT homology!)
Mouse			            100%
Drosophila		          88%
Arabidopsis thaliana     83%
Maize			             84%
Potato			          82%
S. pombe (yeast)	       80%
S. cervisiae		       81% (we're related to beer-making yeast!)
Acanthamoeba castellani  84%
Dictyostelium discoideum 75%
Plasmodium falciparum    38%

and

"some archaebacteria"    40%  (S.K. Burley, pers. comm.)

Not bad to have a 40% sequence identity from archaebacteria to us, eh?


Refs:
-----
(1) Kim, J.L., Nikolov, D.B. and Burley, S.K. (1993) "Co-crystal structure of
TBP
recognizing the minor groove of a TATA element", Nature 365:520-527.

(2) Hernandez, N. (1993) "TBP, a universal eukaryotic transcription factor?",
Genes & Development, 7:1291-1308.

Regards
Dave