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Vol. 96, Issue 24, 13720-13725, November 23, 1999
Laboratories of * Biochemistry and Molecular Biology, and
Contributed by Robert G. Roeder, September 9, 1999
The TATA-binding protein (TBP)-related factor TRF1, has been
described in Drosophila and a related protein, TRF2, has
been found in a variety of higher eukaryotes. We report that human (h)TRF2 is encoded by two mRNAs with common protein coding but distinct
5' nontranslated regions. One mRNA is expressed ubiquitously (hTRF2-mRNA1), whereas the other (hTRF2-mRNA2) shows a restricted expression pattern and is extremely abundant in testis. In addition, we
show that hTRF2 forms a stable stoichiometric complex with hTFIIA, but
not with TAFs, in HeLa cells stably transfected with flag-tagged hTRF2.
Neither recombinant human (rh)TRF2 nor the native flag·hTRF2-TFIIA
complex is able to replace TBP or TFIID in basal or activated
transcription from various RNA polymerase II promoters. Instead,
rhTRF2, but not the flag·hTRF2-TFIIA complex, moderately inhibits
basal or activated transcription in the presence of rhTBP or
flag·TFIID. This effect is either completely (TBP-mediated transcription) or partially (TFIID-mediated transcription) counteracted by addition of free TFIIA. Neither rhTRF2 nor flag·hTRF2-TFIIA has any effect on the repression of TFIID-mediated transcription by
negative cofactor-2 (NC2) and neither substitutes for TBP in RNA
polymerase III-mediated transcription.
Copyright © 1999 by The National Academy of Sciences 0027-8424/99/9613720-6$2.00/0
Biochemistry
Human TATA-binding protein-related factor-2 (hTRF2) stably
associates with hTFIIA in HeLa cells
,, and
Mass Spectrometry and Gaseous Ion Chemistry, The
Rockefeller University, New York, NY 10021
To whom reprint requests should be addressed. E-mail:
roeder{at}rockvax.rockefeller.edu.
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