ArticleProceedings of the National Academy of Sciences of the United States of America2012
HCF-1 self-association via an interdigitated Fn3 structure facilitates transcriptional regulatory complex formation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Identification of a Polypeptide Inhibitor ofJournal of the American Chemical Society · 2024Article
- HCF-2 inhibits cell proliferation and activates differentiation-gene expression programs.Nucleic acids research · 2019Article
- O-linked N-acetylglucosamine transferase promotes cervical cancer tumorigenesis through human papillomaviruses E6 and E7 oncogenes.Oncotarget · 2016Article
- Connecting the regulatory genome.Nature genetics · 2016Article
- Proteolysis of HCF-1 by Ser/Thr glycosylation-incompetent O-GlcNAc transferase:UDP-GlcNAc complexes.Genes & development · 2016Article
- Genomic Determinants of THAP11/ZNF143/HCFC1 Complex Recruitment to Chromatin.Molecular and cellular biology · 2015Article
- Distinct OGT-Binding Sites Promote HCF-1 Cleavage.PloS one · 2015Article
- The making of a sweet modification: structure and function of O-GlcNAc transferase.The Journal of biological chemistry · 2014Review
- HCFC1 is a common component of active human CpG-island promoters and coincides with ZNF143, THAP11, YY1, and GABP transcription factor occupancy.Genome research · 2013Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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