ArticleRNA biology2015
The extended AT-hook is a novel RNA binding motif.
Article in RNA biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 54 citations in OpenAlex.
- MeCP2 MBD-ID module: a unified DNA/RNA binding interface disrupted in Rett syndrome.Nucleic acids research · 2026Article
- Mapping the architecture of protein complexes inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- MeCP2 NID interaction with RNA: implications for Rett syndrome-relevant protein regulation.Human molecular genetics · 2026Article
- Dissecting the Binding Interactions of the Chromatin Remodeler SMARCA4 with G-Quadruplex DNA.Biochemistry · 2026Article
- A roll of the dice: pathogen-host interaction and the evolution of disease susceptibility.Parasitology · 2026Review
- MeCP2 functions as a DNA methylation reader in immune homeostasis and cancer.Frontiers in epigenetics and epigenomics · 2026Review
- Genome-Wide Analysis of the AT-Hook Gene Family inPlants (Basel, Switzerland) · 2025Article
- Binding to the Other Side: The AT-Hook DNA-Binding Domain Allows Nuclear Factors to Exploit the DNA Minor Groove.International journal of molecular sciences · 2024Review
- ISWI chromatin remodeling complexes recruit NSD2 and H3K36me2 in pericentromeric heterochromatin.The Journal of cell biology · 2024Article
- Enhancer switching in cell lineage priming is linked to eRNA, Brg1's AT-hook, and SWI/SNF recruitment.Molecular cell · 2024Article
- The SWI/SNF ATP-dependent chromatin remodeling complex in cell lineage priming and early development.Biochemical Society transactions · 2024Review
- Chromatin attachment to the nuclear matrix represses hypocotyl elongation in Arabidopsis thaliana.Nature communications · 2024Article
- The AT-hook is an evolutionarily conserved auto-regulatory domain of SWI/SNF required for cell lineage priming.Nature communications · 2023Article
- Article
- SGK2, 14-3-3, and HUWE1 Cooperate to Control the Localization, Stability, and Function of the Oncoprotein PTOV1.Molecular cancer research : MCR · 2022Article
- rigrag: high-resolution mapping of genic targeting preferences during HIV-1 integration in vitro and in vivo.Nucleic acids research · 2021Article
- SALL4 controls cell fate in response to DNA base composition.Molecular cell · 2021Article
- Insights Into the Molecular Evolution of AT-Hook Motif Nuclear Localization Genes inFrontiers in plant science · 2021Article
- MeCP2: The Genetic Driver of Rett Syndrome Epigenetics.Frontiers in genetics · 2021Review
- The molecular basis of selective DNA binding by the BRG1 AT-hook and bromodomain.Biochimica et biophysica acta. Gene regulatory mechanisms · 2020Article
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Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The AT-hook has been defined as a DNA binding peptide motif that contains a glycine-arginine-proline (G-R-P) tripeptide core flanked by basic amino acids. Recent reports documented variations in the sequence of AT-hooks and revealed RNA binding activity of some canonical AT-hooks, suggesting a higher structural and functional variability of this protein domain than previously anticipated. Here we describe the discovery and characterization of the extended AT-hook peptide motif (eAT-hook), in which basic amino acids appear symmetrical mainly at a distance of 12-15 amino acids from the G-R-P core. We identified 80 human and 60 mouse eAT-hook proteins and biochemically characterized the eAT-hooks of Tip5/BAZ2A, PTOV1 and GPBP1. Microscale thermophoresis and electrophoretic mobility shift assays reveal the nucleic acid binding features of this peptide motif, and show that eAT-hooks bind RNA with one order of magnitude higher affinity than DNA. In addition, cellular localization studies suggest a role for the N-terminal eAT-hook of PTOV1 in nucleocytoplasmic shuttling. In summary, our findings classify the eAT-hook as a novel nucleic acid binding motif, which potentially mediates various RNA-dependent cellular processes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.