ArticleLife science alliance2023
Structure of SALL4 zinc finger domain reveals link between AT-rich DNA binding and Okihiro syndrome.
Article in Life science alliance, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Experience with patients presenting with the clinical features of Holt-Oram syndrome: a single center retrospective study.Journal of cardiothoracic surgery · 2026Article
- Article
- Thalidomide-induced limb malformations: an update and reevaluation.Archives of toxicology · 2025Review
- Molecular mechanism, diagnosis, and treatment of VACTERL association.Frontiers in pediatrics · 2025Review
- Identification of a novel SALL4 variant associated with unilateral renal agenesis and right renal pelvis duplication by prenatal exome sequencing: a case report.Frontiers in pediatrics · 2025Article
- Updated understanding of the protein-DNA recognition code used by C2H2 zinc finger proteins.Current opinion in structural biology · 2024Review
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Spalt-like 4 (SALL4) maintains vertebrate embryonic stem cell identity and is required for the development of multiple organs, including limbs. Mutations in SALL4 are associated with Okihiro syndrome, and SALL4 is also a known target of thalidomide. SALL4 protein has a distinct preference for AT-rich sequences, recognised by a pair of zinc fingers at the C-terminus. However, unlike many characterised zinc finger proteins, SALL4 shows flexible recognition with many different combinations of AT-rich sequences being targeted. SALL4 interacts with the NuRD corepressor complex which potentially mediates repression of AT-rich genes. We present a crystal structure of SALL4 C-terminal zinc fingers with an AT-rich DNA sequence, which shows that SALL4 uses small hydrophobic and polar side chains to provide flexible recognition in the major groove. Missense mutations reported in patients that lie within the C-terminal zinc fingers reduced overall binding to DNA but not the preference for AT-rich sequences. Furthermore, these mutations altered association of SALL4 with AT-rich genomic sites, providing evidence that these mutations are likely pathogenic.
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Registered trials
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