Nucleic Acids Research, 1992, Vol. 20, No. 22 5889-5898
© 1992
MOLECULAR BIOLOGY |
Cofractionation of the TATA-binding protein with the RNA polymerase III transcription factor TFIIIB
European Molecular Biology Laboratory Meyerhofstrasse 1, Postfach 102209, D6900 Heidelberg, Germany
* To whom correspondence should be addressed
Received September 24, 1992. Accepted October 16, 1992.
We have investigated the requirement for TBP (TATA-binding protein) in transcription mediated by RNA polymerase III (pol III) in fractionated HeLa cell extracts.Two activities, TFIIIB and TFIIIC, found in phosphocel-lulose fractions PC B and PC C respectively, have been defined as necessary and sufficient, with pol III, for in vitro transcription of tRNA genes. Depletion of TBP from PC B, using antibodies raised against human TBP, is shown to inhibit the pol III transcriptional activity of the fraction. Furthermore, TBP is present in fractions with human TFIIIB activity, and a proportion of TBP co-fractionates with TFIIIB over four chromatographic purification steps. TFIIIB fractions are capable of supplying TBP in the form necessary for pol III transcription, and cannot be substituted by fractions containing other TBP complexes or TBP alone. The use of a 5S RNA gene and two tRNA templates supports the general relevance of our findings for pol III gene transcription. Purified TFIIIB activity can also support pol ll-mediated transcription, and is found in a complex of 
230kD, suggesting that TFIIIB may be the same as the previously characterized B-TFIID complex (1,2). We suggest that transcription by the three RNA polymerases is mediated by distinct TBP - TAF complexes: SL1 and D-TFIID for pol I and pol II respectively, and TFIIIB for pol III.
+ Present address: Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands
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