The transcription factor IIF (TFIIF) is composed of 58 kDa (RAP74) and 26 kDa (RAP30) subunits that form a heterodimer, and was first identified through the ability to interact with immobilized RNA polymerase II. In addition to its role in transcription initiation, TFIIF can increase the specificity and efficiency of RNA polymerase II transcription, and can especially increase the rate of transcription elongation.
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The Journal of biological chemistry, 264(15), 8913-8921 (1989-05-25)
The purification and characterization of transcription factor IIF (TFIIF), a factor required for transcription by the RNA polymerase II machinery, is described. TFIIF was isolated from the previously described IIE protein fraction. TFIIF enters into the transcription cycle via a
The Journal of biological chemistry, 260(18), 10353-10360 (1985-08-25)
We have used affinity chromatography on columns containing immobilized calf thymus RNA polymerase II to isolate three phosphoproteins (RAP72, RAP38, and RAP30) that bind directly to RNA polymerase II. All could be isolated from cell nuclei, and all three could
RAP30/74 is a heteromeric general transcription initiation factor which binds to RNA polymerase II. Here we report that preparations of RAP30/74 contain an ATP-dependent DNA helicase whose probable function is to melt the DNA at transcriptional start sites. The sequence
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