ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structure of a new DNA-binding domain which regulates pathogenesis in a wide variety of fungi.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- The Gti1/Pac2 family protein CFG1 controls fungal chlamydospore formation through orchestrating cell wall remodeling, lipid metabolism, and ribosome biogenesis.Applied and environmental microbiology · 2026Article
- Role of theToxins · 2025Article
- MaPac2, a Transcriptional Regulator, Is Involved in Conidiation, Stress Tolerances and Pathogenicity inJournal of fungi (Basel, Switzerland) · 2025Article
- Role of theJournal of fungi (Basel, Switzerland) · 2024Article
- Dissection of integrated readout reveals the structural thermodynamics of DNA selection by transcription factors.Structure (London, England : 1993) · 2024Article
- Decoding Transcription Regulatory Mechanisms Associated withmSystems · 2022Article
- A genome-scale yeast library with inducible expression of individual genes.Molecular systems biology · 2021Article
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- Wor1 establishes opaque cell fate through inhibition of the general co-repressor Tup1 in Candida albicans.PLoS genetics · 2018Article
- Transcription Factors Encoded on Core and Accessory Chromosomes of Fusarium oxysporum Induce Expression of Effector Genes.PLoS genetics · 2016Article
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- The WOR1 5' untranslated region regulates white-opaque switching in Candida albicans by reducing translational efficiency.Molecular microbiology · 2015Article
- High-Copy Overexpression Screening Reveals PDR5 as the Main Doxorubicin Resistance Gene in Yeast.PloS one · 2015Article
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- Profile of Alexander D. Johnson.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
6 authors.
Funding
Abstract
WOPR-domain proteins are found throughout the fungal kingdom where they function as master regulators of cell morphology and pathogenesis. Genetic and biochemical experiments previously demonstrated that these proteins bind to specific DNA sequences and thereby regulate transcription. However, their primary sequence showed no relationship to any known DNA-binding domain, and the basis for their ability to recognize DNA sequences remained unknown. Here, we describe the 2.6-Å crystal structure of a WOPR domain in complex with its preferred DNA sequence. The structure reveals that two highly conserved regions, separated by an unconserved linker, form an interdigitated β-sheet that is tilted into the major groove of DNA. Although the main interaction surface is in the major groove, the highest-affinity interactions occur in the minor groove, primarily through a deeply penetrating arginine residue. The structure reveals a new, unanticipated mechanism by which proteins can recognize specific sequences of DNA.
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