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J. Biol. Chem., Vol. 269, Issue 48, 30140-30146, Dec, 1994
H Kwon and MR Green
The accurate transcription of human rRNA genes by RNA polymerase I requires
two transcription factors, upstream binding factor (UBF) and promoter
selectivity factor (SL1). Human SL1 (hSL1) is a multisubunit complex, one
of whose components is TATA box-binding protein (TBP). hSL1 binds to the
core region of the rRNA promoter, but does so inefficiently in the absence
of human UBF (hUBF). hUBF interacts with the upstream control element of
the rRNA promoter and facilitates binding of hSL1. The molecular basis by
which hUBF increases binding of hSL1 remains to be elucidated. In this
report, we use an immobilized protein binding assay to identify and purify
a 95-kDa TBP-binding polypeptide. Microsequence analysis reveals that the
95-kDa TBP-binding protein is hUBF. We show that hUBF is stably associated
with TBP and is present in large TBP-containing complexes. Our results
indicate that the cooperative binding of hUBF and hSL1 on the rRNA promoter
is mediated by direct interaction between hUBF and TBP. We also provide
evidence that hUBF associates with TFIID, a TBP-containing RNA polymerase
II transcription factor.
The RNA polymerase I transcription factor, upstream binding factor, interacts directly with the TATA box-binding protein
Howard Hughes Medical Institute, University of Massachusetts Medical Center, Worcester 01605.
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