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Mol. Cell. Biol., 01 1998, 233-239, Vol 18, No. 1
J Kaufmann, K Ahrens, R Koop, ST Smale and R Muller
The transcription factor IID (TFIID) complex is highly conserved between
the Drosophila and mammalian systems. A mammalian homolog has been
described for all the Drosophila TATA box-binding protein- associated
factors (TAFs), with the exception of dTAF(II)150. We previously reported
the identification of CIF, an essential cofactor for TFIID-dependent
transcription from promoters containing initiator (Inr) elements. Here we
describe the molecular cloning of CIF150, the human homolog of dTAF(II)150,
and present biochemical evidence that this factor is involved in Inr
activity. CIF150 is capable of mediating TFIID-dependent Inr activity in a
complementation assay, and a protein fraction lacking Inr activity lacks
detectable amounts of CIF150. Despite the striking similarity to
dTAF(II)150, CIF150 does not appear to be associated with human TFIID.
However, in vitro binding assays revealed a specific and direct interaction
between CIF150 and hTAF(II)135. This interaction might be structurally
important for the functional interaction between CIF150 and human TFIID,
since CIF150 stabilizes TFIID binding to a core promoter.
Copyright © 1998, American Society for Microbiology
CIF150, a human cofactor for transcription factor IID-dependent initiator function
Institute for Molecular Biology and Tumor Research, Philipps University, Marburg, Germany. Joerg_Kaufmann@chiron.com
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