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DOI | 10.1016/j.ecolecon.2016.08.011 |
Structural basis of co-translational quality control by ArfA and RF2 bound to ribosome | |
Zeng, Fuxing1; Chen, Yanbo1; Remis, Jonathan2; Shekhar, Mrinal3,4; Phillips, James C.4; Tajkhorshid, Emad1,3,4; Jin, Hong1,3 | |
2017-01-26 | |
发表期刊 | NATURE
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ISSN | 0028-0836 |
EISSN | 1476-4687 |
出版年 | 2017 |
卷号 | 541期号:7638页码:554-557 |
文章类型 | Article |
语种 | 英语 |
国家 | USA |
英文摘要 | Quality control mechanisms intervene appropriately when defective translation events occur, in order to preserve the integrity of protein synthesis. Rescue of ribosomes translating on messenger RNAs that lack stop codons is one of the co-translational quality control pathways. In many bacteria, ArfA recognizes stalled ribosomes and recruits the release factor RF2, which catalyses the termination of protein synthesis(1-3). Although an induced-fit mechanism of nonstop mRNA surveillance mediated by ArfA and RF2 has been reported(4), the molecular interaction between ArfA and RF2 in the ribosome that is responsible for the mechanism is unknown. Here we report an electron cryo-microscopy structure of ArfA and RF2 in complex with the 70S ribosome bound to a nonstop mRNA. The structure, which is consistent with our kinetic and biochemical data, reveals the molecular interactions that enable ArfA to specifically recruit RF2, not RF1, into the ribosome and to enable RF2 to release the truncated protein product in this co-translational quality control pathway. The positively charged C-terminal domain of ArfA anchors in the mRNA entry channel of the ribosome. Furthermore, binding of ArfA and RF2 induces conformational changes in the ribosomal decoding centre that are similar to those seen in other protein-involved decoding processes. Specific interactions between residues in the N-terminal domain of ArfA and RF2 help RF2 to adopt a catalytically competent conformation for peptide release. Our findings provide a framework for understanding recognition of the translational state of the ribosome by new proteins, and expand our knowledge of the decoding potential of the ribosome. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000396116600056 |
WOS关键词 | CRYO-EM STRUCTURE ; PEPTIDE-BOND FORMATION ; TRANSFER-RNA HYDROLYSIS ; INDUCED-FIT MECHANISM ; ESCHERICHIA-COLI ; STALLED RIBOSOMES ; MESSENGER-RNA ; GGQ MOTIF ; TERMINATION COMPLEX ; RELEASE FACTOR-2 |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/15324 |
专题 | 资源环境科学 |
作者单位 | 1.Univ Illinois, Dept Biochem, Urbana, IL 61801 USA; 2.Northwestern Univ, Dept Mol Biosci, Evanston, IL 60208 USA; 3.Univ Illinois, Ctr Biophys & Quantitat Biol, Urbana, IL 61801 USA; 4.Univ Illinois, Beckman Inst Adv Sci & Technol, Urbana, IL 61801 USA |
推荐引用方式 GB/T 7714 | Zeng, Fuxing,Chen, Yanbo,Remis, Jonathan,et al. Structural basis of co-translational quality control by ArfA and RF2 bound to ribosome[J]. NATURE,2017,541(7638):554-557. |
APA | Zeng, Fuxing.,Chen, Yanbo.,Remis, Jonathan.,Shekhar, Mrinal.,Phillips, James C..,...&Jin, Hong.(2017).Structural basis of co-translational quality control by ArfA and RF2 bound to ribosome.NATURE,541(7638),554-557. |
MLA | Zeng, Fuxing,et al."Structural basis of co-translational quality control by ArfA and RF2 bound to ribosome".NATURE 541.7638(2017):554-557. |
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