2RSN

Solution structure of the chromodomain of Chp1 in complex with H3K9me3 peptide

Summary for 2RSN

• Entry DOI: 10.2210/pdb2rsn/pdb
• Related: 2RSO
• NMR Information: BMRB: 11496
• Descriptor: Chromo domain-containing protein 1, peptide from Histone H3 (2 entities in total)
• Functional Keywords: chromodomain, protein-peptide complex, rna-mediated gene silencing, chromosomal protein, methylation, nuclear protein
• Biological source: Schizosaccharomyces pombe (Fission yeast); More
• Cellular location: Nucleus: Q10103
• Total number of polymer chains: 2
• Total formula weight: 10935.27

Authors

Shimojo, H.,Nishimura, Y. (deposition date: 2012-04-18, release date: 2012-08-29, Last modification date: 2025-03-26)

Primary citation

Ishida, M.,Shimojo, H.,Hayashi, A.,Kawaguchi, R.,Ohtani, Y.,Uegaki, K.,Nishimura, Y.,Nakayama, J.
Intrinsic nucleic Acid-binding activity of chp1 chromodomain is required for heterochromatic gene silencing
Mol.Cell, 47:228-241, 2012

PubMed Abstract: Centromeric heterochromatin assembly in fission yeast requires the RNAi pathway. Chp1, a chromodomain (CD) protein, forms the Ago1-containing RNA-induced transcriptional silencing (RITS) complex and recruits siRNA-bound RITS to methylated histone H3 lysine 9 (H3K9me) via its CD. Here, we show that the CD of Chp1 (Chp1-CD) possesses unique nucleic acid-binding activities that are essential for heterochromatic gene silencing. Detailed electrophoretic-mobility shift analyses demonstrated that Chp1 binds to RNA via the CD in addition to its central RNA-recognition motif. Interestingly, robust RNA- and DNA-binding activity of Chp1-CD was strongly enhanced when it was bound to H3K9me, which was revealed to involve a positively charged domain within the Chp1-CD by structural analyses. These results demonstrate a role for the CD that provides a link between RNA, DNA, and methylated histone tails to ensure heterochromatic gene silencing.

PubMed: 22727667
DOI: 10.1016/j.molcel.2012.05.017

Experimental method

SOLUTION NMR