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| - | {{STRUCTURE_3uai| PDB=3uai | SCENE= }} | |
| - | ===Structure of the Shq1-Cbf5-Nop10-Gar1 complex from Saccharomyces cerevisiae=== | |
| - | {{ABSTRACT_PUBMED_22117216}} | |
| | | | |
| - | ==Function== | + | ==Structure of the Shq1-Cbf5-Nop10-Gar1 complex from Saccharomyces cerevisiae== |
| - | [[http://www.uniprot.org/uniprot/SHQ1_YEAST SHQ1_YEAST]] Involved in the early biogenesis steps of box H/ACA snoRNP assembly.<ref>PMID:12228251</ref> [[http://www.uniprot.org/uniprot/CBF5_YEAST CBF5_YEAST]] Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. May function as a pseudouridine synthase. Binds in vitro to centromeres and microtubules. It is a centromeric DNA-CBF3-binding factor which is involved in mitotic chromosome segregation. Essential for cell growth.<ref>PMID:8336724</ref> <ref>PMID:9315678</ref> <ref>PMID:9472021</ref> <ref>PMID:9848653</ref> <ref>PMID:10523634</ref> [[http://www.uniprot.org/uniprot/GAR1_YEAST GAR1_YEAST]] Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs. Essential for growth.<ref>PMID:9303321</ref> [[http://www.uniprot.org/uniprot/NOP10_YEAST NOP10_YEAST]] Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs. Essential for growth.<ref>PMID:9843512</ref> | + | <StructureSection load='3uai' size='340' side='right'caption='[[3uai]], [[Resolution|resolution]] 3.06Å' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[3uai]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UAI FirstGlance]. <br> |
| | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.06Å</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=3uai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uai OCA], [https://pdbe.org/3uai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uai RCSB], [https://www.ebi.ac.uk/pdbsum/3uai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uai ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CBF5_YEAST CBF5_YEAST] Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. May function as a pseudouridine synthase. Binds in vitro to centromeres and microtubules. It is a centromeric DNA-CBF3-binding factor which is involved in mitotic chromosome segregation. Essential for cell growth.<ref>PMID:8336724</ref> <ref>PMID:9315678</ref> <ref>PMID:9472021</ref> <ref>PMID:9848653</ref> <ref>PMID:10523634</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Shq1 is a conserved protein required for the biogenesis of eukaryotic H/ACA ribonucleoproteins (RNPs), including human telomerase. We report the structure of the Shq1-specific domain alone and in complex with H/ACA RNP proteins Cbf5, Nop10 and Gar1. The Shq1-specific domain adopts a novel helical fold and primarily contacts the PUA domain and the otherwise disordered C-terminal extension (CTE) of Cbf5. The structure shows that dyskeratosis congenita mutations found in the CTE of human Cbf5 likely interfere with Shq1 binding. However, most mutations in the PUA domain are not located at the Shq1-binding surface and also have little effect on the yeast Cbf5-Shq1 interaction. Shq1 binds Cbf5 independently of the H/ACA RNP proteins Nop10, Gar1 and Nhp2 and the assembly factor Naf1, but shares an overlapping binding surface with H/ACA RNA. Shq1 point mutations that disrupt Cbf5 interaction suppress yeast growth particularly at elevated temperatures. Our results suggest that Shq1 functions as an assembly chaperone that protects the Cbf5 protein complexes from non-specific RNA binding and aggregation before assembly of H/ACA RNA. |
| | | | |
| - | ==About this Structure==
| + | Structure of the Shq1-Cbf5-Nop10-Gar1 complex and implications for H/ACA RNP biogenesis and dyskeratosis congenita.,Li S, Duan J, Li D, Ma S, Ye K EMBO J. 2011 Nov 25. doi: 10.1038/emboj.2011.427. PMID:22117216<ref>PMID:22117216</ref> |
| - | [[3uai]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UAI OCA].
| + | |
| | | | |
| - | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <ref group="xtra">PMID:022117216</ref><references group="xtra"/><references/> | + | </div> |
| - | [[Category: Saccharomyces cerevisiae s288c]]
| + | <div class="pdbe-citations 3uai" style="background-color:#fffaf0;"></div> |
| - | [[Category: Ye, K.]]
| + | == References == |
| - | [[Category: H/aca rna]]
| + | <references/> |
| - | [[Category: H/aca rnp assembly intermediate]] | + | __TOC__ |
| - | [[Category: Isomerase-chaperone complex]] | + | </StructureSection> |
| - | [[Category: Nuclear]] | + | [[Category: Large Structures]] |
| | + | [[Category: Saccharomyces cerevisiae S288C]] |
| | + | [[Category: Ye K]] |
| Structural highlights
Function
CBF5_YEAST Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. May function as a pseudouridine synthase. Binds in vitro to centromeres and microtubules. It is a centromeric DNA-CBF3-binding factor which is involved in mitotic chromosome segregation. Essential for cell growth.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
Shq1 is a conserved protein required for the biogenesis of eukaryotic H/ACA ribonucleoproteins (RNPs), including human telomerase. We report the structure of the Shq1-specific domain alone and in complex with H/ACA RNP proteins Cbf5, Nop10 and Gar1. The Shq1-specific domain adopts a novel helical fold and primarily contacts the PUA domain and the otherwise disordered C-terminal extension (CTE) of Cbf5. The structure shows that dyskeratosis congenita mutations found in the CTE of human Cbf5 likely interfere with Shq1 binding. However, most mutations in the PUA domain are not located at the Shq1-binding surface and also have little effect on the yeast Cbf5-Shq1 interaction. Shq1 binds Cbf5 independently of the H/ACA RNP proteins Nop10, Gar1 and Nhp2 and the assembly factor Naf1, but shares an overlapping binding surface with H/ACA RNA. Shq1 point mutations that disrupt Cbf5 interaction suppress yeast growth particularly at elevated temperatures. Our results suggest that Shq1 functions as an assembly chaperone that protects the Cbf5 protein complexes from non-specific RNA binding and aggregation before assembly of H/ACA RNA.
Structure of the Shq1-Cbf5-Nop10-Gar1 complex and implications for H/ACA RNP biogenesis and dyskeratosis congenita.,Li S, Duan J, Li D, Ma S, Ye K EMBO J. 2011 Nov 25. doi: 10.1038/emboj.2011.427. PMID:22117216[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jiang W, Middleton K, Yoon HJ, Fouquet C, Carbon J. An essential yeast protein, CBF5p, binds in vitro to centromeres and microtubules. Mol Cell Biol. 1993 Aug;13(8):4884-93. PMID:8336724
- ↑ Cadwell C, Yoon HJ, Zebarjadian Y, Carbon J. The yeast nucleolar protein Cbf5p is involved in rRNA biosynthesis and interacts genetically with the RNA polymerase I transcription factor RRN3. Mol Cell Biol. 1997 Oct;17(10):6175-83. PMID:9315678
- ↑ Lafontaine DL, Bousquet-Antonelli C, Henry Y, Caizergues-Ferrer M, Tollervey D. The box H + ACA snoRNAs carry Cbf5p, the putative rRNA pseudouridine synthase. Genes Dev. 1998 Feb 15;12(4):527-37. PMID:9472021
- ↑ Watkins NJ, Gottschalk A, Neubauer G, Kastner B, Fabrizio P, Mann M, Luhrmann R. Cbf5p, a potential pseudouridine synthase, and Nhp2p, a putative RNA-binding protein, are present together with Gar1p in all H BOX/ACA-motif snoRNPs and constitute a common bipartite structure. RNA. 1998 Dec;4(12):1549-68. PMID:9848653
- ↑ Zebarjadian Y, King T, Fournier MJ, Clarke L, Carbon J. Point mutations in yeast CBF5 can abolish in vivo pseudouridylation of rRNA. Mol Cell Biol. 1999 Nov;19(11):7461-72. PMID:10523634
- ↑ Li S, Duan J, Li D, Ma S, Ye K. Structure of the Shq1-Cbf5-Nop10-Gar1 complex and implications for H/ACA RNP biogenesis and dyskeratosis congenita. EMBO J. 2011 Nov 25. doi: 10.1038/emboj.2011.427. PMID:22117216 doi:10.1038/emboj.2011.427
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