Abstract
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.
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Acknowledgements
We apologize to authors of work uncited due to space constraints. We thank B. van Steensel (Netherlands Cancer Institute) for advice on DamID, N. Houba-Hérin for helpful discussions, I. Henderson for critical reading of the manuscript, and M. Pellegrini and S. Cokus for help with statistical analysis and data submission. X.Z. is supported by a post-doctoral fellowship from the Jonsson Cancer Center Foundation. S.G. is supported by graduate studentships from the French Ministry of Research (ACI no. 03-3-135) and from the French Cancer Research Association (ARC). Research in the Khorasanizadeh laboratory is supported by US National Institutes of Health (NIH) grant GM064786. Research in the Jacobsen laboratory is supported by NIH grant GM60398 and a grant from the NIH ENCODE Program, HG003523. S.E.J. is an investigator of the Howard Hughes Medical Institute.
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S.K., V.G. and S.E.J. designed the experiments; X.Z., S.G. and B.J.B. performed the experiments and analyzed the data; X.Z. wrote the paper.
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Zhang, X., Germann, S., Blus, B. et al. The Arabidopsis LHP1 protein colocalizes with histone H3 Lys27 trimethylation. Nat Struct Mol Biol 14, 869–871 (2007). https://doi.org/10.1038/nsmb1283
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DOI: https://doi.org/10.1038/nsmb1283
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