Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 43, Pages 17430-17435Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1208378109
Keywords
crystallography; chromatin; nuclear localization sequence
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Funding
- World Class University [R31-2008-000-10071-0]
- National Research Foundation [2011-0020334, 2011-0004520, 2011-0031955, 2011-0031416]
- MEST
- Swiss National Science Foundation
- University of Lausanne
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Host-cell factor 1 (HCF-1) is an unusual transcriptional regulator that undergoes a process of proteolytic maturation to generate N-(HCF-1(N)) and C-(HCF-1(C)) terminal subunits noncovalently associated via self-association sequence elements. Here, we present the crystal structure of the self-association sequence 1 (SAS1) including the adjacent C-terminal HCF-1 nuclear localization signal (NLS). SAS1 elements from each of the HCF-1(N) and HCF-1(C) subunits form an interdigitated fibronectin type 3 (Fn3) tandem repeat structure. We show that the C-terminal NLS recruited by the interdigitated SAS1 structure is required for effective formation of a transcriptional regulatory complex: the herpes simplex virus VP16-induced complex. Thus, HCF-1(N)-HCF-1(C) association via an integrated Fn3 structure permits an NLS to facilitate formation of a transcriptional regulatory complex.
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