2rso: Difference between revisions
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New page: '''Unreleased structure''' The entry 2rso is ON HOLD Authors: Shimojo, H., Nishimura, Y. Description: Solution structure of the chromodomain of Swi6 |
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==Solution structure of the chromodomain of Swi6== | |||
<StructureSection load='2rso' size='340' side='right'caption='[[2rso]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2rso]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RSO FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rso OCA], [https://pdbe.org/2rso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rso RCSB], [https://www.ebi.ac.uk/pdbsum/2rso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rso ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SWI6_SCHPO SWI6_SCHPO] Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Involved in the repression of the silent mating-type loci MAT2 and MAT3. May compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Intrinsic nucleic Acid-binding activity of chp1 chromodomain is required for heterochromatic gene silencing.,Ishida M, Shimojo H, Hayashi A, Kawaguchi R, Ohtani Y, Uegaki K, Nishimura Y, Nakayama J Mol Cell. 2012 Jul 27;47(2):228-41. Epub 2012 Jun 21. PMID:22727667<ref>PMID:22727667</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2rso" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Schizosaccharomyces pombe 972h-]] | |||
[[Category: Nishimura Y]] | |||
[[Category: Shimojo H]] | |||
Latest revision as of 20:52, 12 April 2023
Solution structure of the chromodomain of Swi6
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