HP1 alpha binds Histone H3K9(me)3

Stable Identifier
Reaction [binding]
Homo sapiens
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Chromobox (CBX) genes encode members of the Heterochromatin Protein (HP) family. HP1 was discovered in Drosophila as a dominant suppressor of position-effect variegation and a major component of heterochromatin. The HP1 family is evolutionarily conserved, with members in fungi, plants and animals. Most animal species have several HP1 isoforms; humans have HP alpha, beta and gamme encoded by the genes CBX5, CBX1 and CBX3 respectively.
The HP1 amino-terminal chromodomain binds methylated lysine-9 of histone H3, causing transcriptional repression (Lachner et al. 2001). A crystal structure of human HP1 alpha in complex with H3K9(me)3 peptide is available (Amaya et al. 2008). The highly-conserved carboxy-terminal chromoshadow domain enables dimerization and also serves as a docking site for proteins involved in a wide variety of nuclear functions, from transcription to nuclear architecture.
Literature References
PubMed ID Title Journal Year
11242053 Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins

Rea, S, O'Carroll, D, Mechtler, K, Lachner, M, Jenuwein, T

Nature 2001
  Human chromobox homolog 5 (CBX5) in complex with H3K9(me)3 peptide

Bountra, C, Ouyang, H, Weigelt, J, Kozieradzki, I, Bochkarev, A, Arrowsmith, CH, Min, J, Edwards, AM, Amaya, MF, Ravichandran, M, Loppnau, P

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