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J. Biol. Chem., Vol. 276, Issue 7, 5027-5035, February 16, 2001
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and§
From the Howard Hughes Medical Institute, Cold Spring Harbor
Laboratory, Cold Spring Harbor, New York 11724
The nucleation of RNA polymerases I-III
transcription complexes is usually directed by distinct multisubunit
factors. In the case of the human RNA polymerase II and III small
nuclear RNA (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 TATA-binding protein, 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.
Supported by the Howard Hughes Medical Institute.
§
To whom correspondence should be addressed: Cold Spring Harbor
Laboratory, 1 Bungtown Rd., Cold Spring Harbor, NY 11724. Tel.: 516-367-8362; Fax: 516-367-6801; E-mail: Hernande@cshl.org.
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