TFIIE
The fifth factor to bind to this
large complex is TFIIE, a protein with 1 large and 1 small sub-unit (56kD
and 34kD in humans) (Brody, 2001). This protein exists as a tetramer
in solution (2 molecules of each sub-unit bind together). The large
sub-unit contains a Zinc-finger domain, a common DNA binding motif in proteins
(Buratowski, 1999). Through DNA footprinting experiments, it has been
shown that TFIIE binds DNA between -80 and –30 base pairs from the start
site (McClean, 1997). Its main role in the transcriptional complex
is to recruit TFIIH
to the site, then regulate the helicase and kinase activities of TFIIH.
TFIIE is also necessary for RNA Polymerase II to switch into elongation
mode (Buratowski, 1999).
Structure of the TFIIE beta central core domain
Primary citation: Okuda, M., Watanabe, Y., Okamura, H.,
Hanaoka, F., Ohkuma, Y., Nishimura, Y.: Structure of the Central Core
Domain of Tfiie Beta with a Novel Double- Stranded DNA-Binding Surface
Embo J. 19 pp. 1346 (2000)
http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1D8K
Image on this page was obtained from the Structure database
from the
NCBI
Website.
The image was captured using
Cn3D 3.0
Click on the following links to view a specific transcription factor.
TFIIA
, TFIIB
, TFIID
, TFIIE
, TFIIF
, TFIIH
, TFII I
, TFIIS
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