- EMDB-8506: Structural Basis of Co-translational Quality Control by ArfA and ... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-8506
タイトル
Structural Basis of Co-translational Quality Control by ArfA and RF2 Binding to Ribosome
マップデータ
試料
複合体: Non-stop ribosomal complex with ArfA and RF2
複合体: 30S subunit
細胞器官・細胞要素: 16S rRNA
RNA: 16S rRNA
細胞器官・細胞要素: 30S ribosomal protein S3
タンパク質・ペプチド: 30S ribosomal protein S3
細胞器官・細胞要素: 30S ribosomal protein S4
タンパク質・ペプチド: 30S ribosomal protein S4
細胞器官・細胞要素: 30S ribosomal protein S5
細胞器官・細胞要素: 30S ribosomal protein S12
タンパク質・ペプチド: 30S ribosomal protein S5
タンパク質・ペプチド: 30S ribosomal protein S12
複合体: 50S subunit
細胞器官・細胞要素: 23S rRNA
RNA: 23S rRNA
細胞器官・細胞要素: Alternative ribosome-rescue factor A
タンパク質・ペプチド: Alternative ribosome-rescue factor A
細胞器官・細胞要素: Peptide chain release factor 2
タンパク質・ペプチド: Peptide chain release factor 2
細胞器官・細胞要素: P-site tRNA fMet
RNA: P-site tRNA fMet
細胞器官・細胞要素: mRNA
RNA: mRNA
キーワード
Ribosome / ArfA / RF2 / nonstop translation
機能・相同性
機能・相同性情報
translation release factor activity, codon specific / ribosomal large subunit binding / misfolded RNA binding / Group I intron splicing / RNA folding / translational termination / negative regulation of translational initiation / rescue of stalled ribosome / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing ...translation release factor activity, codon specific / ribosomal large subunit binding / misfolded RNA binding / Group I intron splicing / RNA folding / translational termination / negative regulation of translational initiation / rescue of stalled ribosome / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing / transcription antitermination / DNA-templated transcription termination / maintenance of translational fidelity / mRNA 5'-UTR binding / regulation of translation / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / tRNA binding / cytoplasmic translation / rRNA binding / ribosome / structural constituent of ribosome / translation / response to antibiotic / mRNA binding / cytoplasm / cytosol 類似検索 - 分子機能
Alternative ribosome-rescue factor A / Alternative ribosome-rescue factor A / Peptide chain release factor 2 / Peptide chain release factor / PCRF domain / PCRF / Peptide chain release factor class I superfamily / Prokaryotic-type class I peptide chain release factors signature. / Peptide chain release factor class I / RF-1 domain ...Alternative ribosome-rescue factor A / Alternative ribosome-rescue factor A / Peptide chain release factor 2 / Peptide chain release factor / PCRF domain / PCRF / Peptide chain release factor class I superfamily / Prokaryotic-type class I peptide chain release factors signature. / Peptide chain release factor class I / RF-1 domain / Ribosomal protein S3, bacterial-type / Ribosomal protein S4, bacterial-type / Ribosomal protein S5, bacterial-type / Ribosomal protein S12, bacterial-type / K Homology domain / K homology RNA-binding domain / Ribosomal protein S3, conserved site / Ribosomal protein S3 signature. / KH domain / Type-2 KH domain profile. / K Homology domain, type 2 / Ribosomal protein S3, C-terminal / Ribosomal protein S3, C-terminal domain / Ribosomal protein S3, C-terminal domain superfamily / Ribosomal protein S5, N-terminal, conserved site / Ribosomal protein S5 signature. / K homology domain superfamily, prokaryotic type / S5 double stranded RNA-binding domain profile. / Ribosomal protein S5 / Ribosomal protein S5, N-terminal / Ribosomal protein S5, N-terminal domain / Ribosomal protein S5, C-terminal / Ribosomal protein S4/S9 N-terminal domain / Ribosomal protein S5, C-terminal domain / Ribosomal protein S4/S9 N-terminal domain / Ribosomal protein S4/S9, N-terminal / Ribosomal protein S4, conserved site / Ribosomal protein S4 signature. / Ribosomal protein S4/S9 / K homology domain-like, alpha/beta / S4 RNA-binding domain profile. / S4 RNA-binding domain / S4 domain / RNA-binding S4 domain / RNA-binding S4 domain superfamily / Ribosomal protein S12 signature. / Ribosomal protein S12/S23 / Ribosomal protein S12/S23 / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold / Nucleic acid-binding, OB-fold 類似検索 - ドメイン・相同性
Peptide chain release factor RF2 / Small ribosomal subunit protein uS12 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein uS4 / Small ribosomal subunit protein uS5 / Alternative ribosome-rescue factor A 類似検索 - 構成要素
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM120552
米国
引用
ジャーナル: Nature / 年: 2017 タイトル: Structural basis of co-translational quality control by ArfA and RF2 bound to ribosome. 著者: Fuxing Zeng / Yanbo Chen / Jonathan Remis / Mrinal Shekhar / James C Phillips / Emad Tajkhorshid / Hong Jin / 要旨: 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 ...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. Although an induced-fit mechanism of nonstop mRNA surveillance mediated by ArfA and RF2 has been reported, 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.