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| | ==Crystal structure of the Chp1-Tas3 complex core== | | ==Crystal structure of the Chp1-Tas3 complex core== |
| - | <StructureSection load='3tix' size='340' side='right' caption='[[3tix]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='3tix' size='340' side='right'caption='[[3tix]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3tix]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TIX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TIX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3tix]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TIX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tas3, SPBC83.03c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), chp1, SPAC18G6.02c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tas3, SPBC83.03c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), chp1, SPAC18G6.02c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tix OCA], [http://pdbe.org/3tix PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tix RCSB], [http://www.ebi.ac.uk/pdbsum/3tix PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tix ProSAT]</span></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=3tix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tix OCA], [https://pdbe.org/3tix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tix RCSB], [https://www.ebi.ac.uk/pdbsum/3tix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tix ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations. [[http://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> | + | [[https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations. [[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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Fission yeast]] | | [[Category: Fission yeast]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Joshua-Tor, L]] | | [[Category: Joshua-Tor, L]] |
| | [[Category: Schalch, T]] | | [[Category: Schalch, T]] |
| Structural highlights
Function
[SMT3_YEAST] Not known; suppressor of MIF2 mutations. [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
RNA interference (RNAi) is critical for the assembly of heterochromatin at Schizosaccharomyces pombe centromeres. Central to this process is the RNA-induced initiation of transcriptional gene silencing (RITS) complex, which physically anchors small noncoding RNAs to chromatin. RITS includes Ago1, the chromodomain protein Chp1, and Tas3, which forms a bridge between Chp1 and Ago1. Chp1 is a large protein with no recognizable domains, apart from its chromodomain. Here we describe how the structured C-terminal half of Chp1 binds the Tas3 N-terminal domain, revealing the tight association of Chp1 and Tas3. The structure also shows a PIN domain at the C-terminal tip of Chp1 that controls subtelomeric transcripts through a post-transcriptional mechanism. We suggest that the Chp1-Tas3 complex provides a solid and versatile platform to recruit both RNAi-dependent and RNAi-independent gene-silencing pathways for locus-specific regulation of heterochromatin.
The Chp1-Tas3 core is a multifunctional platform critical for gene silencing by RITS.,Schalch T, Job G, Shanker S, Partridge JF, Joshua-Tor L Nat Struct Mol Biol. 2011 Nov 13;18(12):1351-7. doi: 10.1038/nsmb.2151. PMID:22081013[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
- ↑ Schalch T, Job G, Shanker S, Partridge JF, Joshua-Tor L. The Chp1-Tas3 core is a multifunctional platform critical for gene silencing by RITS. Nat Struct Mol Biol. 2011 Nov 13;18(12):1351-7. doi: 10.1038/nsmb.2151. PMID:22081013 doi:10.1038/nsmb.2151
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