ArticleThe Journal of biological chemistry2008
The solution structure of DNA-free Pax-8 paired box domain accounts for redox regulation of transcriptional activity in the pax protein family.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- PAX gene expression in autosomal dominant polycystic kidney disease contributes to cyst expansion and regulates a gene network associated with cyst growth.Human molecular genetics · 2026Article
- Review
- MITF Is Regulated by Redox Signals Controlled by the Selenoprotein Thioredoxin Reductase 1.Cancers · 2022Article
- PAX8 in the Junction between Development and Tumorigenesis.International journal of molecular sciences · 2022Review
- Impaired GSH biosynthesis disrupts eye development, lens morphogenesis and PAX6 function.The ocular surface · 2021Article
- Overview of PAX gene family: analysis of human tissue-specific variant expression and involvement in human disease.Human genetics · 2021Review
- Unraveling molecular targets of bisphenol A and S in the thyroid gland.Environmental science and pollution research international · 2018Article
- NMR solution structure of the RED subdomain of the Sleeping Beauty transposase.Protein science : a publication of the Protein Society · 2017Article
- Resonance assignment of disordered protein with repetitive and overlapping sequence using combinatorial approach reveals initial structural propensities and local restrictions in the denatured state.Journal of biomolecular NMR · 2016Article
- Identification of a novel pax8 gene sequence variant in four members of the same family: from congenital hypothyroidism with thyroid hypoplasia to mild subclinical hypothyroidism.BMC endocrine disorders · 2014Article
- Reversible and irreversible protein glutathionylation: biological and clinical aspects.Expert opinion on drug metabolism & toxicology · 2011Review
- Pathogenic mechanisms of tooth agenesis linked to paired domain mutations in human PAX9.Human molecular genetics · 2009Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pax-8 is a transcription factor belonging to the PAX genes superfamily and its crucial role has been proven both in embryo and in the adult organism. Pax-8 activity is regulated via a redox-based mechanism centered on the glutathionylation of specific cysteines in the N-terminal region (Cys45 and Cys57). These residues belong to a highly evolutionary conserved DNA binding site: the Paired Box (Prd) domain. Crystallographic protein-DNA complexes of the homologues Pax-6 and Pax-5 showed a bipartite Prd domain consisting of two helix-turn-helix (HTH) motifs separated by an extended linker region. Here, by means of nuclear magnetic resonance, we show for the first time that the HTH motifs are largely defined in the unbound Pax-8 Prd domain. Our findings contrast with previous induced fit models, in which Pax-8 is supposed to largely fold upon DNA binding. Importantly, our data provide the structural basis for the enhanced chemical reactivity of residues Cys45 and Cys57 and explain clinical missense mutations that are not obviously related to the DNA binding interface of the paired box domain. Finally, sequence conservation suggests that our findings could be a general feature of the Pax family transcription factors.
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