Author
Listed:
- Elzbieta Wieczorek
(Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP
Virginia Commonwealth University)
- Marjorie Brand
(Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP)
- Xavier Jacq
(Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP
Columbia University)
- László Tora
(Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP)
Abstract
Initiation of transcription of a gene from a core promoter region by RNA polymerase II requires the assembly of several initiation factors to form a preinitiation complex. Assembly of this complex1,2 is thought to be nucleated exclusively by the sequence-specific binding of the TFIID transcription factor complex, which is composed of the TATA-binding protein (TBP) and TBP-associated factors (TAFIIs) (refs 3, 4), to the different promoters. Here we isolate and characterize a new multiprotein complex that does not contain either TBP or a TBP-like factor but is composed of several TAFIIs and other proteins. This complex can replace TFIID on both TATA-containing and TATA-lacking promoters in in vitro transcription assays. Moreover, an anti-TBP antibody that inhibits TBP- and TFIID-dependent transcription does not inhibit activity of this new complex. These results indicate that TBP-free RNA polymerase II mediated transcription may be able to occur in mammalian cells and that multiple preinitiation complexes may play an important role in regulating gene expression.
Suggested Citation
Elzbieta Wieczorek & Marjorie Brand & Xavier Jacq & László Tora, 1998.
"Function of TAFII-containing complex without TBP in transcription by RNA polymerase II,"
Nature, Nature, vol. 393(6681), pages 187-191, May.
Handle:
RePEc:nat:nature:v:393:y:1998:i:6681:d:10.1038_30283
DOI: 10.1038/30283
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