9t3l: Difference between revisions
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==Crystal structure of the Acl1 ankyrin repeat domain in complex with the second Rpl1 domain== | |||
<StructureSection load='9t3l' size='340' side='right'caption='[[9t3l]], [[Resolution|resolution]] 2.55Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9t3l]] 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=9T3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9T3L 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]] 2.55Å</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=9t3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9t3l OCA], [https://pdbe.org/9t3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9t3l RCSB], [https://www.ebi.ac.uk/pdbsum/9t3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9t3l ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In eukaryotes, most newly synthesized ribosomal proteins (r-proteins) need to rapidly and safely get into the nucleus to reach their assembly site on pre-ribosomal particles. However, only for few r-proteins tailored support mechanisms involving so-called dedicated chaperones (DCs) could so far be revealed. Here, with the primary aim of identifying novel DCs, we performed TurboID-based proximity labelling with all 46 large subunit r-proteins of Saccharomyces cerevisiae, which unveiled the fungi-specific Acl1 and the conserved Bcl1 as candidate DCs of Rpl1. We show that the functionally cooperating Acl1 and Bcl1 both directly interact with Rpl1, form a trimeric Acl1-Rpl1-Bcl1 complex, and enable the nuclear import of Rpl1. Moreover, our crystal structure of the minimal Acl1-Rpl1 complex reveals how Acl1's ankyrin repeat domain shields a positively charged ribosomal RNA-binding surface of Rpl1. Our proximity labelling approach also permitted to establish novel interactions between four r-proteins and distinct importins and to illuminate r-protein neighbourhoods on successive pre-60S particles. Additionally, reciprocal proximity labelling with the known DCs indicates that almost all appear to be transiently associated with pre-ribosomal particles. Our study provides for the first time comprehensive insight into the physical proximities of large subunit r-proteins along their entire life cycle. | |||
Exploration of the proxiOME of large subunit ribosomal proteins reveals Acl1 and Bcl1 as cooperating dedicated chaperones of Rpl1.,Favre S, Pillet B, Burchert F, Siva Sankar D, Mendez-Godoy A, Kiontke S, Dengjel J, Bange G, Kressler D Nucleic Acids Res. 2026 Mar 19;54(6):gkag264. doi: 10.1093/nar/gkag264. PMID:41909949<ref>PMID:41909949</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Bange | <div class="pdbe-citations 9t3l" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | |||
[[Category: Bange G]] | |||
[[Category: Burchert F]] | |||
[[Category: Kiontke S]] | |||
