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Papers In Press, published online ahead of print October 30, 2000
Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724
Corresponding Author: Hernande{at}cshl.org
The nucleation of RNA polymerase I, II, and III transcription complexes is usually directed by distinct multisubunit factors. In the case of the human RNA polymerase II and III snRNA genes, whose core promoters consist of a proximal sequence element (PSE) and a PSE combined with a TATA box, respectively, the same multisubunit complex is involved in the establishment of RNA polymerase II and III initiation complexes. This factor, the snRNA activating protein complex or SNAPc, binds to the PSE of both types of promoters and contains five types of subunits, SNAP190, SNAP50, SNAP45, SNAP43, and SNAP19. SNAPc binds cooperatively with both Oct-1, an activator of snRNA promoters, and in the RNA polymerase III snRNA promoters, with TBP, which binds to the TATA box located downstream of the PSE. Here we have defined subunit domains required for SNAPc subunit-subunit association and we show that complexes containing little more than the domains mapped here as required for subunit-subunit contacts bind specifically to the PSE. These data provide a detailed map of the subunit-subunit interactions within a multifunctional basal transcription complex.
J. Biol. Chem, 10.1074/jbc.M009301200
Submitted on October 11, 2000
Revised on October 30, 2000
Accepted on October 27, 2000
A map of protein-protein contacts within the snRNA activating protein complex SNAPc
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