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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/G0SFC3_CHATD G0SFC3_CHATD] | [https://www.uniprot.org/uniprot/G0SFC3_CHATD G0SFC3_CHATD] | ||
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== Publication Abstract from PubMed == | |||
Eukaryotic ribosome biogenesis requires the nuclear import of approximately 80 nascent ribosomal proteins and the elimination of excess amounts by the cellular degradation machinery. Assembly chaperones recognize nascent unassembled ribosomal proteins and transport them together with karyopherins to their nuclear destination. We report the crystal structure of ribosomal protein L4 (RpL4) bound to its dedicated assembly chaperone of L4 (Acl4), revealing extensive interactions sequestering 70 exposed residues of the extended RpL4 loop. The observed molecular recognition fundamentally differs from canonical promiscuous chaperone-substrate interactions. We demonstrate that the eukaryote-specific RpL4 extension harbours overlapping binding sites for Acl4 and the nuclear transport factor Kap104, facilitating its continuous protection from the cellular degradation machinery. Thus, Acl4 serves a dual function to facilitate nuclear import and simultaneously protect unassembled RpL4 from the cellular degradation machinery. | |||
Molecular basis for protection of ribosomal protein L4 from cellular degradation.,Huber FM, Hoelz A Nat Commun. 2017 Feb 2;8:14354. doi: 10.1038/ncomms14354. PMID:28148929<ref>PMID:28148929</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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==See Also== | ==See Also== | ||
*[[Ribosomal protein L4|Ribosomal protein L4]] | *[[Ribosomal protein L4|Ribosomal protein L4]] | ||
== References == | |||
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</StructureSection> | </StructureSection> | ||
Latest revision as of 13:52, 30 October 2024
Crystal structure of assembly chaperone of ribosomal protein L4 (Acl4) in complex with ribosomal protein L4 (RpL4)Crystal structure of assembly chaperone of ribosomal protein L4 (Acl4) in complex with ribosomal protein L4 (RpL4)
Structural highlights
FunctionPublication Abstract from PubMedEukaryotic ribosome biogenesis requires the nuclear import of approximately 80 nascent ribosomal proteins and the elimination of excess amounts by the cellular degradation machinery. Assembly chaperones recognize nascent unassembled ribosomal proteins and transport them together with karyopherins to their nuclear destination. We report the crystal structure of ribosomal protein L4 (RpL4) bound to its dedicated assembly chaperone of L4 (Acl4), revealing extensive interactions sequestering 70 exposed residues of the extended RpL4 loop. The observed molecular recognition fundamentally differs from canonical promiscuous chaperone-substrate interactions. We demonstrate that the eukaryote-specific RpL4 extension harbours overlapping binding sites for Acl4 and the nuclear transport factor Kap104, facilitating its continuous protection from the cellular degradation machinery. Thus, Acl4 serves a dual function to facilitate nuclear import and simultaneously protect unassembled RpL4 from the cellular degradation machinery. Molecular basis for protection of ribosomal protein L4 from cellular degradation.,Huber FM, Hoelz A Nat Commun. 2017 Feb 2;8:14354. doi: 10.1038/ncomms14354. PMID:28148929[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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