3uai

From Proteopedia

(Difference between revisions)

Revision as of 13:19, 25 December 2014

Structure of the Shq1-Cbf5-Nop10-Gar1 complex from Saccharomyces cerevisiae

Structural highlights

3uai is a 4 chain structure with sequence from Saccharomyces cerevisiae s288c. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3uah
Gene:	CBF5 (Saccharomyces cerevisiae S288c), NOP10 (Saccharomyces cerevisiae S288c), GAR1 (Saccharomyces cerevisiae S288c), SHQ1 (Saccharomyces cerevisiae S288c)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[SHQ1_YEAST] Involved in the early biogenesis steps of box H/ACA snoRNP assembly.^[1] [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.^[2] ^[3] ^[4] ^[5] ^[6] [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.^[7] [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.^[8]

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^[9]

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

References

↑ Yang PK, Rotondo G, Porras T, Legrain P, Chanfreau G. The Shq1p.Naf1p complex is required for box H/ACA small nucleolar ribonucleoprotein particle biogenesis. J Biol Chem. 2002 Nov 22;277(47):45235-42. Epub 2002 Sep 11. PMID:12228251 doi:10.1074/jbc.M207669200
↑ 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
↑ Bousquet-Antonelli C, Henry Y, G'elugne JP, Caizergues-Ferrer M, Kiss T. A small nucleolar RNP protein is required for pseudouridylation of eukaryotic ribosomal RNAs. EMBO J. 1997 Aug 1;16(15):4770-6. PMID:9303321 doi:10.1093/emboj/16.15.4770
↑ Henras A, Henry Y, Bousquet-Antonelli C, Noaillac-Depeyre J, Gelugne JP, Caizergues-Ferrer M. Nhp2p and Nop10p are essential for the function of H/ACA snoRNPs. EMBO J. 1998 Dec 1;17(23):7078-90. PMID:9843512 doi:10.1093/emboj/17.23.7078
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3uai"

@@ Line 7: / Line 7: @@
 <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=3uai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uai OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uai RCSB], [http://www.ebi.ac.uk/pdbsum/3uai PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3uai

From Proteopedia

Revision as of 13:19, 25 December 2014

Structure of the Shq1-Cbf5-Nop10-Gar1 complex from Saccharomyces cerevisiae

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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