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7ohx

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Nog1-TAP associated immature ribosomal particles from S. cerevisiae after rpL34 expression shut down, population A

Structural highlights

7ohx is a 10 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.
Method:	Electron Microscopy, Resolution 3.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAK16_YEAST Its role might be as part of the apparatus concerned with the nuclear events of the cell cycle.^[1]

Publication Abstract from PubMed

In yeast and human cells many of the ribosomal proteins (r-proteins) are required for the stabilisation and productive processing of rRNA precursors. Functional coupling of r-protein assembly with the stabilisation and maturation of subunit precursors potentially promotes the production of ribosomes with defined composition. To further decipher mechanisms of such an intrinsic quality control pathway we analysed here the contribution of three yeast large ribosomal subunit r-proteins rpL2 (uL2), rpL25 (uL23) and rpL34 (eL34) for intermediate nuclear subunit folding steps. Structure models obtained from single particle cryo-electron microscopy analyses provided evidence for specific and hierarchic effects on the stable positioning and remodelling of large ribosomal subunit domains. Based on these structural and previous biochemical data we discuss possible mechanisms of r-protein dependent hierarchic domain arrangement and the resulting impact on the stability of misassembled subunits.

Analysis of subunit folding contribution of three yeast large ribosomal subunit proteins required for stabilisation and processing of intermediate nuclear rRNA precursors.,Poll G, Pilsl M, Griesenbeck J, Tschochner H, Milkereit P PLoS One. 2021 Nov 23;16(11):e0252497. doi: 10.1371/journal.pone.0252497. , eCollection 2021. PMID:34813592^[2]

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

References

↑ Wickner RB. Host function of MAK16: G1 arrest by a mak16 mutant of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1988 Aug;85(16):6007-11. PMID:3045810
↑ Pöll G, Pilsl M, Griesenbeck J, Tschochner H, Milkereit P. Analysis of subunit folding contribution of three yeast large ribosomal subunit proteins required for stabilisation and processing of intermediate nuclear rRNA precursors. PLoS One. 2021 Nov 23;16(11):e0252497. PMID:34813592 doi:10.1371/journal.pone.0252497