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Molecular and Cellular Biology, February 2001, p. 1145-1154, Vol. 21, No. 4
Department of Biological Chemistry and
Molecular Pharmacology, Harvard Medical School, Boston,
Massachusetts 02115
Received 11 September 2000/Returned for modification 20 October
2000/Accepted 14 November 2000
TFIID, a multiprotein complex comprising the TATA-binding protein
(TBP) and TBP-associated factors (TAFs), associates specifically with
core promoters and nucleates the assembly the RNA polymerase II
transcription machinery. In yeast cells, TFIID is not generally required for transcription, although it plays an important role at many
promoters. Understanding of the specific functions and physiological
roles of individual TAFs within TFIID has been hampered by the fact
that depletion or thermal inactivation of individual TAFs generally
results in dissociation of the TFIID complex. We describe here
C-terminally deleted derivatives of yeast TAF130 that assemble into
normal TFIID complexes but are transcriptionally inactive in vivo. In
vivo, these mutant TFIID complexes are dramatically reduced in their
ability to associate with all promoters tested. In vitro, a TFIID
complex containing a deleted form of TAF130 associates poorly with DNA,
but it is unaffected for interacting with transcriptional activation
domains. These results suggest that the C-terminal region of TAF130 is
required for TFIID to associate with promoters.
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.4.1145-1154.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Region of Yeast TAF 130 Required for TFIID To
Associate with Promoters
*
Corresponding author. Mailing address: Department of
Biological Chemistry and Molecular Pharmacology, Harvard Medical
School, Boston, MA 02115. Fax: (617) 432-2529. E-mail:
kevin{at}hms.harvard.edu.
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