Activator Recruitment by the General Transcription Machinery: X-ray Structural Analysis of the Oct-1 POU Domain/human U1 Octamer/SNAP190 Peptide Ternary Complex

Overview

Journal Genes Dev

Specialty Molecular Biology

Date 2002 Nov 5

PMID 12414730

Citations 6

Authors

Stacy Hovde

Craig S Hinkley

Katie Strong

Aimee Brooks

Liping Gu

R William Henry

James Geiger

Affiliations

Soon will be listed here.

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.

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