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Recognition of Histone H3K4 Trimethylation by the Plant Homeodomain of PHF2 Modulates Histone Demethylation*
- Publication Year :
- 2010
- Publisher :
- American Society for Biochemistry and Molecular Biology, 2010.
-
Abstract
- Distinct lysine methylation marks on histones create dynamic signatures deciphered by the "effector" modules, although the underlying mechanisms remain unclear. We identified the plant homeodomain- and Jumonji C domain-containing protein PHF2 as a novel histone H3K9 demethylase. We show in biochemical and crystallographic analyses that PHF2 recognizes histone H3K4 trimethylation through its plant homeodomain finger and that this interaction is essential for PHF2 occupancy and H3K9 demethylation at rDNA promoters. Our study provides molecular insights into the mechanism by which distinct effector domains within a protein cooperatively modulate the "cross-talk" of histone modifications.
- Subjects :
- Protein Conformation
Green Fluorescent Proteins
Biology
SAP30
Crystallography, X-Ray
Biochemistry
DNA, Ribosomal
Methylation
Histones
Mice
Histone demethylation
Histone H1
Histone H2A
Histone methylation
Histone code
Animals
Humans
Molecular Biology
Plant Proteins
Genetics
Homeodomain Proteins
Histone deacetylase 2
Cell Biology
Protein Structure, Tertiary
Histone methyltransferase
Peptides
Reports
HeLa Cells
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....097ca038231c00b59d22c7b3382b57be