2rsn: Difference between revisions

Latest revision as of 22:29, 26 March 2025

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

Structural highlights

2rsn is a 2 chain structure with sequence from Schizosaccharomyces pombe and Schizosaccharomyces pombe 972h-. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 20 models
Ligands:	M3L
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHP1_SCHPO Component of the kinetochore which plays a role in stabilizing microtubules and so allowing accurate chromosome segregation. Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-induced transcriptional silencing (RITS) complex which is involved in the biosynthesis of dsRNA from primer siRNAs provided by the RNA-directed RNA polymerase (RDRC) complex.^[1] ^[2] ^[3] ^[4]

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Doe CL, Wang G, Chow C, Fricker MD, Singh PB, Mellor EJ. The fission yeast chromo domain encoding gene chp1(+) is required for chromosome segregation and shows a genetic interaction with alpha-tubulin. Nucleic Acids Res. 1998 Sep 15;26(18):4222-9. PMID:9722643
↑ Thon G, Verhein-Hansen J. Four chromo-domain proteins of Schizosaccharomyces pombe differentially repress transcription at various chromosomal locations. Genetics. 2000 Jun;155(2):551-68. PMID:10835380
↑ Motamedi MR, Verdel A, Colmenares SU, Gerber SA, Gygi SP, Moazed D. Two RNAi complexes, RITS and RDRC, physically interact and localize to noncoding centromeric RNAs. Cell. 2004 Dec 17;119(6):789-802. PMID:15607976 doi:10.1016/j.cell.2004.11.034
↑ Verdel A, Jia S, Gerber S, Sugiyama T, Gygi S, Grewal SI, Moazed D. RNAi-mediated targeting of heterochromatin by the RITS complex. Science. 2004 Jan 30;303(5658):672-6. Epub 2004 Jan 2. PMID:14704433 doi:10.1126/science.1093686
↑ 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. 2012 Jul 27;47(2):228-41. Epub 2012 Jun 21. PMID:22727667 doi:10.1016/j.molcel.2012.05.017

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OCA

[1] Doe CL, Wang G, Chow C, Fricker MD, Singh PB, Mellor EJ. The fission yeast chromo domain encoding gene chp1(+) is required for chromosome segregation and shows a genetic interaction with alpha-tubulin. Nucleic Acids Res. 1998 Sep 15;26(18):4222-9. PMID:9722643

[2] Thon G, Verhein-Hansen J. Four chromo-domain proteins of Schizosaccharomyces pombe differentially repress transcription at various chromosomal locations. Genetics. 2000 Jun;155(2):551-68. PMID:10835380

[3] Motamedi MR, Verdel A, Colmenares SU, Gerber SA, Gygi SP, Moazed D. Two RNAi complexes, RITS and RDRC, physically interact and localize to noncoding centromeric RNAs. Cell. 2004 Dec 17;119(6):789-802. PMID:15607976 doi:10.1016/j.cell.2004.11.034

[4] Verdel A, Jia S, Gerber S, Sugiyama T, Gygi S, Grewal SI, Moazed D. RNAi-mediated targeting of heterochromatin by the RITS complex. Science. 2004 Jan 30;303(5658):672-6. Epub 2004 Jan 2. PMID:14704433 doi:10.1126/science.1093686

[5] 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. 2012 Jul 27;47(2):228-41. Epub 2012 Jun 21. PMID:22727667 doi:10.1016/j.molcel.2012.05.017

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[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2rsn is ON HOLD
+==Solution structure of the chromodomain of Chp1 in complex with H3K9me3 peptide==
+<StructureSection load='2rsn' size='340' side='right'caption='[[2rsn]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2rsn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe] and [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=2RSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RSN FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></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=2rsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsn OCA], [https://pdbe.org/2rsn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rsn RCSB], [https://www.ebi.ac.uk/pdbsum/2rsn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsn ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CHP1_SCHPO CHP1_SCHPO] Component of the kinetochore which plays a role in stabilizing microtubules and so allowing accurate chromosome segregation. Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-induced transcriptional silencing (RITS) complex which is involved in the biosynthesis of dsRNA from primer siRNAs provided by the RNA-directed RNA polymerase (RDRC) complex.<ref>PMID:9722643</ref> <ref>PMID:10835380</ref> <ref>PMID:15607976</ref> <ref>PMID:14704433</ref>
+<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.
-Authors: Shimojo, H., Nishimura, Y.
+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>
-Description: Solution structure of the chromodomain of Chp1 in complex with H3K9me3 peptide
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2rsn" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Schizosaccharomyces pombe]]
+[[Category: Schizosaccharomyces pombe 972h-]]
+[[Category: Nishimura Y]]
+[[Category: Shimojo H]]

2rsn: Difference between revisions

Latest revision as of 22:29, 26 March 2025

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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