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J Biol Chem, Vol. 274, Issue 7, 3937-3940, February 12, 1999
From the Laboratory of Biochemistry and Molecular Biology, The
Rockefeller University, New York, New York 10021
Mammalian RNA polymerase II holoenzymes are large
complexes that have been reported to contain, in addition to RNA
polymerase II, homologues of several yeast SRBs, various general
transcription factors, and other polypeptides. On the basis of its
copurification with an SRB-containing RNA polymerase II complex by
conventional chromatography procedures, we have identified a human
homologue of Drosophila TRF-proximal protein, designated
hTRFP, and isolated its cognate cDNA. Antibody specific for SRB7
can immunoprecipitate hTRFP and RNA polymerase II and, reciprocally,
antibody specific for hTRFP can immunoprecipitate RNA polymerase II and
SRB7. These data indicate that hTRFP is an integral component of an RNA
polymerase II-SRB complex. Whereas the precise function of hTRFP
remains to be determined, the hTRFP-containing RNA polymerase II-SRB
complex supports basal level transcription and, relative to RNA
polymerase II alone, enhances transcriptional activation by Gal4-VP16
in the presence of cofactor PC4. Thus, hTRFP may regulate transcription of class II genes through association with the RNA polymerase II-SRB complex.
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