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- W1571567681 abstract "We have shown previously that under specific conditions, a TATA box will mediate efficient in vitro transcription by RNA polymerase (pol) III in the absence of a PSE or other promoter elements. The reaction requires a HeLa cell phosphocellulose protein fraction, fraction B, which must be preincubated with the template DNA. Fraction B does not contain any detectable pol II type transcription factor IID (TFIID) activity. In this report, the relationship between fraction B and TFIID was further examined. Purified human TATA-binding protein (TBP) can substitute for fraction B to mediate TATA-dependent pol III transcription. Both TBP and fraction B prefer a reverse TATA box for pol III transcription, yet TBP bound to a reverse TATA box functions poorly for pol II transcription. Like TFIID, fraction B forms a template-committed complex with TATA-containing promoters. TBP, however, will not template commit for pol III transcription unless premixed with phosphocellulose fraction C. TBP-mediated pol III transcription is also more sensitive to the detergent Sarkosyl (N-lauroylsarcosine, Sigma) than is the fraction B reaction unless it is premixed with fraction C. Together, the data suggest that TBP can complex with a component of fraction C, and this complex is then functionally equivalent to fraction B. We propose that fraction B contains TBP in a complex with some other component(s) of the pol III transcription machinery and that this B complex TBP may be specific for pol III transcription." @default.
- W1571567681 created "2016-06-24" @default.
- W1571567681 creator A5033470704 @default.
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- W1571567681 date "1993-01-01" @default.
- W1571567681 modified "2023-09-26" @default.
- W1571567681 title "TATA box-mediated in vitro transcription by RNA polymerase III. Evidence for TATA-binding protein in a polymerase III type complex." @default.
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- W1571567681 doi "https://doi.org/10.1016/s0021-9258(18)54052-7" @default.
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