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Updated: Jul 31, 2025
10:14
Biochemical Assays for Analyzing Activities of ATP-dependent Chromatin Remodeling Enzymes
Published on: October 25, 2014
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Structural analysis of ING3 protein and histone H3 binding
Mariola Ferreras-Gutiérrez1, Belén Chaves-Arquero1, Amaia González-Magaña2
1Centro de Investigaciones Biológicas Margarita Salas (CIB), CSIC, Madrid 28040, Spain.
Summary
The ING3 protein
Area of Science:
- Structural biology
- Epigenetics
- Cancer research
Background:
- ING proteins regulate chromatin transcription by binding to histone H3 trimethylated at Lysine 4 (H3K4me3).
- ING3, a member of the ING family, is implicated in histone acetylation and proposed as an oncoprotein.
Purpose of the Study:
- To elucidate the structural basis of ING3's function in chromatin regulation.
- To understand the structural mechanisms underlying ING3's interaction with histone modifications.
Main Methods:
- X-ray crystallography was used to determine the structures of the N-terminal domain and the Plant HomeoDomain (PHD) of ING3.
- Site-directed mutagenesis experiments were performed to assess the impact on histone recognition.
Main Results:
- The N-terminal domain of ING3 forms antiparallel coiled-coil homodimers.
- The ING3 PHD structure is similar to its homologs and binds H3K4me3 with low-micromolar affinity.
- Mutagenesis studies confirmed the structural basis for histone H3K4me3 recognition.
Conclusions:
- ING3 likely functions as a homodimer and a bivalent reader of H3K4me3 marks.
- The determined structures provide insights into the deleterious effects of ING3 mutations in tumors.
- ING proteins share conserved structural features for histone binding and chromatin regulation.
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