B. Ma et N. Hernandez, A map of protein-protein contacts within the small nuclear RNA-activating protein complex SNAP(c), J BIOL CHEM, 276(7), 2001, pp. 5027-5035
The nucleation of RNA polymerases I-III transcription complexes is usually
directed by distinct multisubunit factors. In the case of the human RNA pol
ymerase II and III small nuclear RNA (snRNA) genes, whose core promoters co
nsist of a proximal sequence element (PSE) and a PSE combined with a TATA b
ox, respectively, the same multisubunit complex is involved in the establis
hment of RNA polymerase II and III initiation complexes. This factor, the s
nRNA-activating protein complex or SNAP(c), binds to the PSE of both types
of promoters and contains five types of subunits, SNAP190, SNAP50, SNAP45,
SNAP43, and SNAP19, SNAP(c) binds cooperatively with both Oct-1, an activat
or 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 SNAP, subunit-subun
it association, and we show that complexes containing little more than the
domains mapped here as required for subunit-subunit contacts bind specifica
lly to the PSE, These data provide a detailed map of the subunit-subunit in
teractions within a multifunctional basal transcription complex.