Activator recruitment by the general transcription machinery: X-ray structural analysis of the Oct-1 POU domain/human U1 octamer/SNAP190 peptide ternary complex

  1. Stacy Hovde1,
  2. Craig S. Hinkley2,
  3. Katie Strong1,
  4. Aimee Brooks1,
  5. Liping Gu2,
  6. R. William Henry2, and
  7. James Geiger1,3
  1. 1Department of Chemistry, 2Department of Biochemistry & Molecular Biology, Michigan State University, East Lansing, Michigan 48823, USA

Abstract

Transcriptional activation of the human U1 snRNA genes is dependent on a noncanonical octamer element contained within an upstream enhancer. The U1 octamer only weakly recruits the Oct-1 POU domain, although recruitment is stimulated by a peptide containing the Oct-1-binding domain of SNAP190. Structural analysis of the Oct-1 POU domain/U1 octamer/SNAP190 peptide complex revealed that SNAP190 makes extensive protein contacts with the Oct-1 POU-specific domain and with the DNA phosphate backbone within the enhancer. Although SNAP190 and OCA-B both interact with the Oct-1 POU domain through the same Oct-1 interface, a single nucleotide within the U1 octamer ablates OCA-B recruitment without compromising activator recruitment by SNAP190.

Supplemental material is available athttp://www.genesdev.org.

Keywords

Footnotes

  • 3 Corresponding author.

  • E-MAIL geiger{at}cem.msu.edu; FAX (517) 353-1793.

  • Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1021002.

    • Received July 3, 2002.
    • Accepted September 13, 2002.
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