3G7L

Chromodomain of Chp1 in complex with Histone H3K9me3 peptide

Summary for 3G7L

• Entry DOI: 10.2210/pdb3g7l/pdb
• Descriptor: Chromo domain-containing protein 1, Histone H3.1/H3.2, ACETIC ACID, ... (5 entities in total)
• Functional Keywords: chromodomain, protein-peptide complex, silencing, cell cycle, chromosome partition, dna-binding, nucleus, rna-mediated gene silencing, acetylation, chromosomal protein, dna damage, dna repair, methylation, nucleosome core, phosphoprotein, nuclear protein
• Biological source: Schizosaccharomyces pombe (Fission yeast); More
• Cellular location: Nucleus: Q10103; Nucleus (By similarity): P09988
• Total number of polymer chains: 2
• Total formula weight: 9475.92

Authors

Schalch, T.,Joshua-Tor, L. (deposition date: 2009-02-10, release date: 2009-04-21, Last modification date: 2023-09-06)

Primary citation

Schalch, T.,Job, G.,Noffsinger, V.J.,Shanker, S.,Kuscu, C.,Joshua-Tor, L.,Partridge, J.F.
High-affinity binding of Chp1 chromodomain to K9 methylated histone H3 is required to establish centromeric heterochromatin
Mol.Cell, 34:36-46, 2009

PubMed Abstract: In fission yeast, assembly of centromeric heterochromatin requires the RITS complex, which consists of Ago1, Tas3, Chp1, and siRNAs derived from centromeric repeats. Recruitment of RITS to centromeres has been proposed to depend on siRNA-dependent targeting of Ago1 to centromeric sequences. Previously, we demonstrated that methylated lysine 9 of histone H3 (H3K9me) acts upstream of siRNAs during heterochromatin establishment. Our crystal structure of Chp1's chromodomain in complex with a trimethylated lysine 9 H3 peptide reveals extensive sites of contact that contribute to Chp1's high-affinity binding. We found that this high-affinity binding is critical for the efficient establishment of centromeric heterochromatin, but preassembled heterochromatin can be maintained when Chp1's affinity for H3K9me is greatly reduced.

PubMed: 19362535
DOI: 10.1016/j.molcel.2009.02.024

Experimental method

X-RAY DIFFRACTION (2.2 Å)