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Stm1通过休眠核糖体对真核起始因子5A、真核延伸因子2和转运RNA的保护作用。

Implication of Stm1 in the protection of eIF5A, eEF2 and tRNA through dormant ribosomes.

作者信息

Du Mengtan, Li Xin, Dong Wanlin, Zeng Fuxing

机构信息

Department of Systems Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, China.

Institute for Biological Electron Microscopy, Southern University of Science and Technology, Shenzhen, China.

出版信息

Front Mol Biosci. 2024 Apr 18;11:1395220. doi: 10.3389/fmolb.2024.1395220. eCollection 2024.

DOI:10.3389/fmolb.2024.1395220
PMID:38698775
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11063288/
Abstract

Dormant ribosomes are typically associated with preservation factors to protect themselves from degradation under stress conditions. Stm1/SERBP1 is one such protein that anchors the 40S and 60S subunits together. Several proteins and tRNAs bind to this complex as well, yet the molecular mechanisms remain unclear. Here, we reported the cryo-EM structures of five newly identified Stm1/SERBP1-bound ribosomes. These structures highlighted that eIF5A, eEF2, and tRNA might bind to dormant ribosomes under stress to avoid their own degradation, thus facilitating protein synthesis upon the restoration of growth conditions. In addition, Ribo-seq data analysis reflected the upregulation of nutrient, metabolism, and external-stimulus-related pathways in the strain, suggesting possible regulatory roles of Stm1. The knowledge generated from the present work will facilitate in better understanding the molecular mechanism of dormant ribosomes.

摘要

休眠核糖体通常与保护因子相关联,以在应激条件下保护自身免受降解。Stm1/SERBP1就是这样一种将40S和60S亚基锚定在一起的蛋白质。还有几种蛋白质和tRNA也结合到这个复合物上,但其分子机制仍不清楚。在此,我们报道了五个新鉴定的与Stm1/SERBP1结合的核糖体的冷冻电镜结构。这些结构突出表明,eIF5A、eEF2和tRNA可能在应激条件下与休眠核糖体结合,以避免自身降解,从而在生长条件恢复时促进蛋白质合成。此外,核糖体测序数据分析反映了该菌株中营养、代谢和外部刺激相关途径的上调,表明Stm1可能具有调控作用。本研究产生的知识将有助于更好地理解休眠核糖体的分子机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fadd/11063288/20b04eba6ff8/fmolb-11-1395220-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fadd/11063288/b2b88f47a079/fmolb-11-1395220-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fadd/11063288/eecbfd04d26c/fmolb-11-1395220-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fadd/11063288/4e68f9b0a2d7/fmolb-11-1395220-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fadd/11063288/232223676e30/fmolb-11-1395220-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fadd/11063288/20b04eba6ff8/fmolb-11-1395220-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fadd/11063288/b2b88f47a079/fmolb-11-1395220-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fadd/11063288/eecbfd04d26c/fmolb-11-1395220-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fadd/11063288/4e68f9b0a2d7/fmolb-11-1395220-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fadd/11063288/232223676e30/fmolb-11-1395220-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fadd/11063288/20b04eba6ff8/fmolb-11-1395220-g005.jpg

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