The Arabidopsis LHP1 protein colocalizes with histone H3 Lys27 trimethylation

Xiaoyu Zhang (1) , Sophie Germann (2) , Bartlomiej J. Blus (3) , Sepideh Khorasanizadeh (3) , Valérie Gaudin (2) , Steven E. Jacobsen (1)

1 Department of Molecular, Cell, and Developmental Biology
2 Laboratoire de biologie cellulaire et moléculaire
3 Department of Biochemistry and Molecular Genetics [Charlottesville]

Polycomb proteins are required for maintenance of silent chromatin states via histone H3 Lys27 trimethylation ( H3K27me3) in animals, but homologs are not found in plant genomes. Using a DamID- chip method, we found that the Arabidopsis thaliana chromodomain- containing protein LHP1 colocalizes with H3K27me3 genome- wide. The LHP1 chromodomain also binds H3K27me3 with high affinity, suggesting that LHP1 has functions similar to those of Polycomb.

Mots clés: HISTONE H3 LYS27; PROTEIN LHP1; ARABIDOPSIS THALIANA

Domaines: Sciences du Vivant [q-bio]

Xiaoyu Zhang, Sophie Germann, Bartlomiej J. Blus, Sepideh Khorasanizadeh, Valérie Gaudin, et al.. The Arabidopsis LHP1 protein colocalizes with histone H3 Lys27 trimethylation. Nature Structural and Molecular Biology, 2007, 14 (9), pp.869-871. ⟨10.1038/nsmb1283⟩. ⟨hal-02665086⟩