2RSN: Solution structure of the chromodomain of Chp1 in complex with H3K9me3 peptide

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.
PDB ID: 2RSNDownload
MMDB ID: 102332
PDB Deposition Date: 2012/4/18
Updated in MMDB: 2012/08
Experimental Method:
solution nmr
Source Organism:
Schizosaccharomyces pombe 972h-
Similar Structures:
Biological Unit for 2RSN: dimeric; determined by author
Molecular Components in 2RSN
Label Count Molecule
Proteins (2 molecules)
Chromo Domain-containing Protein 1(Gene symbol: chp1)
Molecule annotation
Peptide From Histone H3
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB