2RSO
Solution structure of the chromodomain of Swi6
Summary for 2RSO
Entry DOI | 10.2210/pdb2rso/pdb |
Related | 2RSN |
NMR Information | BMRB: 11497 |
Descriptor | Chromatin-associated protein swi6 (1 entity in total) |
Functional Keywords | chromodomain, chromatin, silencing, chromosomal protein, methylation, transcription |
Biological source | Schizosaccharomyces pombe (Fission yeast) |
Cellular location | Nucleus (Probable): P40381 |
Total number of polymer chains | 1 |
Total formula weight | 10503.33 |
Authors | Shimojo, H.,Nishimura, Y. (deposition date: 2012-04-18, release date: 2012-08-29, Last modification date: 2024-05-15) |
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 Cited by 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: 22727667DOI: 10.1016/j.molcel.2012.05.017 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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