核糖体终止复合体重塑释放因子 RF3 并排出 GDP。

IF 16.8 1区 生物学 Nature Structural &Molecular Biology Pub Date : 2024-07-19 DOI:10.1038/s41594-024-01360-0
Li Li, Mariia Yu Rybak, Jinzhong Lin, Matthieu G Gagnon
{"title":"核糖体终止复合体重塑释放因子 RF3 并排出 GDP。","authors":"Li Li, Mariia Yu Rybak, Jinzhong Lin, Matthieu G Gagnon","doi":"10.1038/s41594-024-01360-0","DOIUrl":null,"url":null,"abstract":"<p><p>Translation termination involves release factors RF1, RF2 and the GTPase RF3 that recycles RF1 and RF2 from the ribosome. RF3 dissociates from the ribosome in the GDP-bound form and must then exchange GDP for GTP. The 70S ribosome termination complex (70S-TC) accelerates GDP exchange in RF3, suggesting that the 70S-TC can function as the guanine nucleotide exchange factor for RF3. Here, we use cryogenic-electron microscopy to elucidate the mechanism of GDP dissociation from RF3 catalyzed by the Escherichia coli 70S-TC. The non-rotated ribosome bound to RF1 remodels RF3 and induces a peptide flip in the phosphate-binding loop, efficiently ejecting GDP. Binding of GTP allows RF3 to dock at the GTPase center, promoting the dissociation of RF1 from the ribosome. The structures recapitulate the functional cycle of RF3 on the ribosome and uncover the mechanism by which the 70S-TC allosterically dismantles the phosphate-binding groove in RF3, a previously overlooked function of the ribosome.</p>","PeriodicalId":18836,"journal":{"name":"Nature Structural &Molecular Biology","volume":" ","pages":""},"PeriodicalIF":16.8000,"publicationDate":"2024-07-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The ribosome termination complex remodels release factor RF3 and ejects GDP.\",\"authors\":\"Li Li, Mariia Yu Rybak, Jinzhong Lin, Matthieu G Gagnon\",\"doi\":\"10.1038/s41594-024-01360-0\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Translation termination involves release factors RF1, RF2 and the GTPase RF3 that recycles RF1 and RF2 from the ribosome. RF3 dissociates from the ribosome in the GDP-bound form and must then exchange GDP for GTP. The 70S ribosome termination complex (70S-TC) accelerates GDP exchange in RF3, suggesting that the 70S-TC can function as the guanine nucleotide exchange factor for RF3. Here, we use cryogenic-electron microscopy to elucidate the mechanism of GDP dissociation from RF3 catalyzed by the Escherichia coli 70S-TC. The non-rotated ribosome bound to RF1 remodels RF3 and induces a peptide flip in the phosphate-binding loop, efficiently ejecting GDP. Binding of GTP allows RF3 to dock at the GTPase center, promoting the dissociation of RF1 from the ribosome. The structures recapitulate the functional cycle of RF3 on the ribosome and uncover the mechanism by which the 70S-TC allosterically dismantles the phosphate-binding groove in RF3, a previously overlooked function of the ribosome.</p>\",\"PeriodicalId\":18836,\"journal\":{\"name\":\"Nature Structural &Molecular Biology\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":16.8000,\"publicationDate\":\"2024-07-19\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature Structural &Molecular Biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1038/s41594-024-01360-0\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature Structural &Molecular Biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1038/s41594-024-01360-0","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

摘要

翻译终止涉及释放因子 RF1、RF2 和 GTP 酶 RF3,后者从核糖体中回收 RF1 和 RF2。RF3 以 GDP 结合的形式从核糖体中解离,然后必须将 GDP 交换为 GTP。70S 核糖体终止复合体(70S-TC)可加速 RF3 的 GDP 交换,这表明 70S-TC 可充当 RF3 的鸟嘌呤核苷酸交换因子。在这里,我们利用低温电子显微镜阐明了大肠杆菌 70S-TC 催化 RF3 中 GDP 解离的机制。与 RF1 结合的非旋转核糖体重塑了 RF3,并诱导磷酸盐结合环中的肽翻转,从而有效地排出 GDP。GTP 的结合使 RF3 与 GTPase 中心对接,促进 RF1 与核糖体分离。这些结构再现了 RF3 在核糖体上的功能周期,并揭示了 70S-TC 异构拆除 RF3 磷酸盐结合槽的机制,这是以前被忽视的核糖体功能。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

摘要图片

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
The ribosome termination complex remodels release factor RF3 and ejects GDP.

Translation termination involves release factors RF1, RF2 and the GTPase RF3 that recycles RF1 and RF2 from the ribosome. RF3 dissociates from the ribosome in the GDP-bound form and must then exchange GDP for GTP. The 70S ribosome termination complex (70S-TC) accelerates GDP exchange in RF3, suggesting that the 70S-TC can function as the guanine nucleotide exchange factor for RF3. Here, we use cryogenic-electron microscopy to elucidate the mechanism of GDP dissociation from RF3 catalyzed by the Escherichia coli 70S-TC. The non-rotated ribosome bound to RF1 remodels RF3 and induces a peptide flip in the phosphate-binding loop, efficiently ejecting GDP. Binding of GTP allows RF3 to dock at the GTPase center, promoting the dissociation of RF1 from the ribosome. The structures recapitulate the functional cycle of RF3 on the ribosome and uncover the mechanism by which the 70S-TC allosterically dismantles the phosphate-binding groove in RF3, a previously overlooked function of the ribosome.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Nature Structural &Molecular Biology
Nature Structural &Molecular Biology 生物-生化与分子生物学
自引率
1.80%
发文量
160
期刊介绍: Nature Structural & Molecular Biology is a monthly journal that focuses on the functional and mechanistic understanding of how molecular components in a biological process work together. It serves as an integrated forum for structural and molecular studies. The journal places a strong emphasis on the functional and mechanistic understanding of how molecular components in a biological process work together. Some specific areas of interest include the structure and function of proteins, nucleic acids, and other macromolecules, DNA replication, repair and recombination, transcription, regulation of transcription and translation, protein folding, processing and degradation, signal transduction, and intracellular signaling.
期刊最新文献
The ribosome termination complex remodels release factor RF3 and ejects GDP. Structural basis for Parkinson’s disease-linked LRRK2’s binding to microtubules Structural basis for context-specific inhibition of translation by oxazolidinone antibiotics Higher-order phosphatase–substrate contacts terminate the integrated stress response Structural basis of nucleosome transcription mediated by Chd1 and FACT
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1