TFIIF
TFII – F is comprised of two subunits: RNA polymerase II-associate protein–30
(RAP30) and RNA polymerase II-associate protein – 74 (RAP74) (Langelier
et al, 2001). The molecular weights of the subunits are 30kD and 74kD,
respectively (Langelier et al, 2001). The major function of TFII –
F is to weaken interactions between RNA pol II and nonspecific binding sites
of DNA (Weaver, 2002 and Papavassiliou, 1997). TFII – F also has the
ability to bind to RNA pol II, thereby guiding the complex to the promoters
(Weaver, 2002). In addition to its ability to initiate transcription,
TFII – F can also participate in the process of RNA elongation by “suppressing
transient pausing of the polymerase” (Hampsey, 1998).
TFII – F possesses homologous characteristics of bacterial sigma factors
(Hampsey, 1998 and Weaver, 2002). Previous experiments showed that
“RAP30 [and] RAP74 [of TFII – F can bind to the] E. coli RNA polymerase”
(Hampsey, 1998). However, s70 of E. coli can kick out TFII – F because
it is able to bind to the RNA polymerase more tightly (Hampsey, 1998, Weaver,
2002). Homologies with bacterial sigma factor can also be demonstrated
by TFII-F’s ability to bind to the RNA pol II and prevent the RNA pol II
from binding to nonspecific DNA binding sites (Papavassiliou, 1997, Hampsey,
1998 and Weaver, 2002).
Structure of Rap74 Subunit Of Human Transcription
Factor Iif (Tfiif) C-Terminal Domain
Primary citation: Kamada, K., De Angelis, J., Roeder,
R. G., Burley, S. K.: Crystal Structure of the C-Terminal Domain of the
RAP74 Subunit of Human Transcription Factor Iif Proc.Nat.Acad.Sci.USA 98
pp. 3115 (2001)
http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1I27
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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