ArticleStructure (London, England : 1993)2022
Structural insights into cooperative DNA recognition by the CCAAT-binding complex and its bZIP transcription factor HapX.
Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- Transcription factor NF-Y complex interacts with chromatin remodeling complexes SWI/SNF and RSC to coordinately regulate gene expression.Nucleic acids research · 2026Article
- Article
- Functional transitions of the Aspergillus fumigatus iron regulator HapX are governed by conserved domains cooperatively binding [2Fe-2S] clusters.Nucleic acids research · 2025Article
- Regulation of Ergosterol Biosynthesis in Pathogenic Fungi: Opportunities for Therapeutic Development.Microorganisms · 2025Review
- HapX-mediated H2B deub1 and SreA-mediated H2A.Z deposition coordinate in fungal iron resistance.Nucleic acids research · 2023Article
- Article
- Structure of the HapX:CCAAT-binding protein complex with DNA: A piece of the puzzle revealed.Structure (London, England : 1993) · 2022Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The heterotrimeric CCAAT-binding complex (CBC) is a fundamental eukaryotic transcription factor recognizing the CCAAT box. In certain fungi, like Aspergilli, the CBC cooperates with the basic leucine zipper HapX to control iron metabolism. HapX functionally depends on the CBC, and the stable interaction of both requires DNA. To study this cooperative effect, X-ray structures of the CBC-HapX-DNA complex were determined. Downstream of the CCAAT box, occupied by the CBC, a HapX dimer binds to the major groove. The leash-like N terminus of the distal HapX subunit contacts the CBC, and via a flexible polyproline type II helix mediates minor groove interactions that stimulate sequence promiscuity. In vitro and in vivo mutagenesis suggest that the structural and functional plasticity of HapX results from local asymmetry and its ability to target major and minor grooves simultaneously. The latter feature may also apply to related transcription factors such as yeast Hap4 and distinct Yap family members.
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