HCF-1 self-association via an interdigitated Fn3 structure facilitates transcriptional regulatory complex formation
| Autor: | Fabienne Lammers, Winship Herr, Jihye Park, Ji-Joon Song |
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| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Host cell factor C1 Regulation of gene expression Multidisciplinary Transcription Genetic Molecular Sequence Data Nuclear Localization Signals Plasma protein binding Biological Sciences Biology Crystallography X-Ray Molecular biology Cell biology Amino Acid Sequence Gene Expression Regulation Host Cell Factor C1/chemistry Host Cell Factor C1/physiology Humans Tandem Repeat Sequences Tandem repeat Transcriptional regulation NLS Host Cell Factor C1 Peptide sequence Nuclear localization sequence |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 43, pp. 17430-17435 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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