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| | <StructureSection load='4zox' size='340' side='right'caption='[[4zox]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='4zox' size='340' side='right'caption='[[4zox]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zox]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZOX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZOX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zox]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZOX FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zov|4zov]]</td></tr> | + | </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=4zox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zox OCA], [https://pdbe.org/4zox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zox RCSB], [https://www.ebi.ac.uk/pdbsum/4zox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zox ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SQT1, YIR012W, YIB12W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), RPL10, GRC5, QSR1, YLR075W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=4zox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zox OCA], [http://pdbe.org/4zox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zox RCSB], [http://www.ebi.ac.uk/pdbsum/4zox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zox ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SQT1_YEAST SQT1_YEAST]] May be involved in the late step of 60S ribosomal subunit assembly or modification in the cytoplasm. | + | [https://www.uniprot.org/uniprot/SQT1_YEAST SQT1_YEAST] May be involved in the late step of 60S ribosomal subunit assembly or modification in the cytoplasm. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Altegoer, F]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Bange, G]] | + | [[Category: Altegoer F]] |
| - | [[Category: Pausch, P]] | + | [[Category: Bange G]] |
| - | [[Category: Chaperone]] | + | [[Category: Pausch P]] |
| - | [[Category: Ribosomal biogenesis]]
| + | |
| - | [[Category: Wd40 - repeat]]
| + | |
| Structural highlights
Function
SQT1_YEAST May be involved in the late step of 60S ribosomal subunit assembly or modification in the cytoplasm.
Publication Abstract from PubMed
Exponentially growing yeast cells produce every minute >160,000 ribosomal proteins. Owing to their difficult physicochemical properties, the synthesis of assembly-competent ribosomal proteins represents a major challenge. Recent evidence highlights that dedicated chaperone proteins recognize the N-terminal regions of ribosomal proteins and promote their soluble expression and delivery to the assembly site. Here we explore the intuitive possibility that ribosomal proteins are captured by dedicated chaperones in a co-translational manner. Affinity purification of four chaperones (Rrb1, Syo1, Sqt1 and Yar1) selectively enriched the mRNAs encoding their specific ribosomal protein clients (Rpl3, Rpl5, Rpl10 and Rps3). X-ray crystallography reveals how the N-terminal, rRNA-binding residues of Rpl10 are shielded by Sqt1's WD-repeat beta-propeller, providing mechanistic insight into the incorporation of Rpl10 into pre-60S subunits. Co-translational capturing of nascent ribosomal proteins by dedicated chaperones constitutes an elegant mechanism to prevent unspecific interactions and aggregation of ribosomal proteins on their road to incorporation.
Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones.,Pausch P, Singh U, Ahmed YL, Pillet B, Murat G, Altegoer F, Stier G, Thoms M, Hurt E, Sinning I, Bange G, Kressler D Nat Commun. 2015 Jun 26;6:7494. doi: 10.1038/ncomms8494. PMID:26112308[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pausch P, Singh U, Ahmed YL, Pillet B, Murat G, Altegoer F, Stier G, Thoms M, Hurt E, Sinning I, Bange G, Kressler D. Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones. Nat Commun. 2015 Jun 26;6:7494. doi: 10.1038/ncomms8494. PMID:26112308 doi:http://dx.doi.org/10.1038/ncomms8494
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