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J Biol Chem, Vol. 275, Issue 18, 13895-13900, May 5, 2000
From the Department of Molecular Physiology & Biophysics,
Vanderbilt University, School of Medicine, Nashville, Tennessee
37232-0615
Using a combination of ion exchange and
immunoaffinity chromatography we have purified the general
transcription initiation factor TFIID to near homogeneity from
Saccharomyces cerevisiae. Yeast TFIID is composed of TBP,
the TATA box binding protein, and 14 distinct TBP-associated factors
(TAFs), which range in size from 17 to 150 kDa. Twelve of the TAF
subunits have been previously identified, but two, TAF48p and TAF65p,
are novel. TAF48p exhibits significant sequence similarity to the
conserved C-terminal region of Drosophila TAF110p, human
TAF130p, and human TAF105p and is encoded by a previously identified
gene MPT1. TAF65p shows no significant sequence homology to
any previously identified TAFp. The genes encoding TAF48p and TAF65p
are single copy and essential for normal yeast cell growth.
Furthermore, neither TAF48p nor TAF65p are associated with the histone
acetylase Spt-Ada-Gcn5 complex or other non-TFIID TBF·TAF
complexes. The significance of these results in terms of TFIID
structure, function, and organization is discussed.
Identification of Two Novel TAF Subunits of the Yeast
Saccharomyces cerevisiae TFIID Complex*
and
*
This work was supported by National Institutes of Health
Grant GM52461.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Received partial support from National Institutes of Health
Training Grant DK07563-09.
§
To whom correspondence should be addressed. Tel.: 615-322-7007;
Fax: 615-322-7236; E-mail: tony.weil@mcmail.vanderbilt.edu.
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