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HCF-1 self-association via an interdigitated Fn3 structure facilitates transcriptional regulatory complex formation.
Proceedings of the National Academy of Sciences of the United States of America
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.
Amino Acid Sequence, Crystallography, X-Ray, Gene Expression Regulation, Host Cell Factor C1/chemistry, Host Cell Factor C1/physiology, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Localization Signals, Tandem Repeat Sequences, Transcription, Genetic
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