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Otu2 识别和去泛素化 40S 核糖体的分子基础。

Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2.

机构信息

Department of Biochemistry, Gene Center, Feodor-Lynen-Str. 25, University of Munich, 81377, Munich, Germany.

Division of Physical Chemistry, Rudjer Boskovic Institute, Bijenicka cesta 54, 10000, Zagreb, Croatia.

出版信息

Nat Commun. 2023 May 12;14(1):2730. doi: 10.1038/s41467-023-38161-w.

DOI:10.1038/s41467-023-38161-w
PMID:37169754
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10175282/
Abstract

In actively translating 80S ribosomes the ribosomal protein eS7 of the 40S subunit is monoubiquitinated by the E3 ligase Not4 and deubiquitinated by Otu2 upon ribosomal subunit recycling. Despite its importance for translation efficiency the exact role and structural basis for this translational reset is poorly understood. Here, structural analysis by cryo-electron microscopy of native and reconstituted Otu2-bound ribosomal complexes reveals that Otu2 engages 40S subunits mainly between ribosome recycling and initiation stages. Otu2 binds to several sites on the intersubunit surface of the 40S that are not occupied by any other 40S-binding factors. This binding mode explains the discrimination against 80S ribosomes via the largely helical N-terminal domain of Otu2 as well as the specificity for mono-ubiquitinated eS7 on 40S. Collectively, this study reveals mechanistic insights into the Otu2-driven deubiquitination steps for translational reset during ribosome recycling/(re)initiation.

摘要

在活跃地翻译 80S 核糖体的过程中，40S 亚基中的核糖体蛋白 eS7 被 E3 连接酶 Not4 单泛素化，在核糖体亚基循环后被 Otu2 去泛素化。尽管它对翻译效率很重要，但对于这种翻译重置的确切作用和结构基础仍了解甚少。在这里，通过冷冻电镜对天然和重建的 Otu2 结合核糖体复合物的结构分析表明，Otu2 主要在核糖体循环和起始阶段之间与 40S 亚基结合。Otu2 结合到 40S 亚基的亚基间表面上的几个位点，这些位点不被任何其他 40S 结合因子占据。这种结合模式解释了 Otu2 通过其 N 端结构域的大部分螺旋结构来区分 80S 核糖体，以及对 40S 上单泛素化的 eS7 的特异性。总的来说，这项研究揭示了 Otu2 驱动的核糖体循环/（再）起始过程中翻译重置的去泛素化步骤的机制见解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d414/10175282/b717e3b5a447/41467_2023_38161_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d414/10175282/f5abeadb1c77/41467_2023_38161_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d414/10175282/d64954d912d9/41467_2023_38161_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d414/10175282/f4e1f6b87eb8/41467_2023_38161_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d414/10175282/08265ec31102/41467_2023_38161_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d414/10175282/b717e3b5a447/41467_2023_38161_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d414/10175282/f5abeadb1c77/41467_2023_38161_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d414/10175282/d64954d912d9/41467_2023_38161_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d414/10175282/f4e1f6b87eb8/41467_2023_38161_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d414/10175282/08265ec31102/41467_2023_38161_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d414/10175282/b717e3b5a447/41467_2023_38161_Fig5_HTML.jpg

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