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Literature DB >> 18988853

Insights into translational termination from the structure of RF2 bound to the ribosome.

Albert Weixlbaumer¹, Hong Jin, Cajetan Neubauer, Rebecca M Voorhees, Sabine Petry, Ann C Kelley, Venki Ramakrishnan.

Abstract

The termination of protein synthesis occurs through the specific recognition of a stop codon in the A site of the ribosome by a release factor (RF), which then catalyzes the hydrolysis of the nascent protein chain from the P-site transfer RNA. Here we present, at a resolution of 3.5 angstroms, the crystal structure of RF2 in complex with its cognate UGA stop codon in the 70S ribosome. The structure provides insight into how RF2 specifically recognizes the stop codon; it also suggests a model for the role of a universally conserved GGQ motif in the catalysis of peptide release.

Entities: Chemical

Mesh：

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Year: 2008 PMID： 18988853 PMCID： PMC2642913 DOI： 10.1126/science.1164840

Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728

31 in total

1. Recognition of cognate transfer RNA by the 30S ribosomal subunit.

Authors: J M Ogle; D E Brodersen; W M Clemons ; M J Tarry; A P Carter; V Ramakrishnan
Journal: Science Date: 2001-05-04 Impact factor: 47.728

2. Functional sites of interaction between release factor RF1 and the ribosome.

Authors: K S Wilson; K Ito; H F Noller; Y Nakamura
Journal: Nat Struct Biol Date: 2000-10

3. Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3.

Authors: Andrei V Zavialov; Liliana Mora; Richard H Buckingham; Måns Ehrenberg
Journal: Mol Cell Date: 2002-10 Impact factor: 17.970

4. Selection of tRNA by the ribosome requires a transition from an open to a closed form.

Authors: James M Ogle; Frank V Murphy; Michael J Tarry; V Ramakrishnan
Journal: Cell Date: 2002-11-27 Impact factor: 41.582

5. Structure of the Escherichia coli ribosomal termination complex with release factor 2.

Authors: Bruno P Klaholz; Tillmann Pape; Andrey V Zavialov; Alexander G Myasnikov; Elena V Orlova; Bente Vestergaard; Måns Ehrenberg; Marin van Heel
Journal: Nature Date: 2003-01-02 Impact factor: 49.962

6. The essential role of the invariant GGQ motif in the function and stability in vivo of bacterial release factors RF1 and RF2.

Authors: Liliana Mora; Valérie Heurgué-Hamard; Stéphanie Champ; Måns Ehrenberg; Lev L Kisselev; Richard H Buckingham
Journal: Mol Microbiol Date: 2003-01 Impact factor: 3.501

7. The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release.

Authors: Elaine M Youngman; Julie L Brunelle; Anna B Kochaniak; Rachel Green
Journal: Cell Date: 2004-05-28 Impact factor: 41.582

8. A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation.

Authors: V Dinçbas-Renqvist; A Engström; L Mora; V Heurgué-Hamard; R Buckingham; M Ehrenberg
Journal: EMBO J Date: 2000-12-15 Impact factor: 11.598

9. Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1.

Authors: B Vestergaard; L B Van; G R Andersen; J Nyborg; R H Buckingham; M Kjeldgaard
Journal: Mol Cell Date: 2001-12 Impact factor: 17.970

10. A cryo-electron microscopic study of ribosome-bound termination factor RF2.

Authors: Urmila B S Rawat; Andrey V Zavialov; Jayati Sengupta; Mikel Valle; Robert A Grassucci; Jamie Linde; Bente Vestergaard; Måns Ehrenberg; Joachim Frank
Journal: Nature Date: 2003-01-02 Impact factor: 49.962

146 in total

1. Crystal structure of release factor RF3 trapped in the GTP state on a rotated conformation of the ribosome.

Authors: Jie Zhou; Laura Lancaster; Sergei Trakhanov; Harry F Noller
Journal: RNA Date: 2011-12-20 Impact factor: 4.942

2. Hypothesis: emergence of translation as a result of RNA helicase evolution.

Authors: Nikolay Zenkin
Journal: J Mol Evol Date: 2012-04-28 Impact factor: 2.395

3. Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1.

Authors: Vladimir I Polshakov; Boris D Eliseev; Berry Birdsall; Ludmila Yu Frolova
Journal: Protein Sci Date: 2012-04-19 Impact factor: 6.725

Insights into translational termination from the structure of RF2 bound to the ribosome.

1. Recognition of cognate transfer RNA by the 30S ribosomal subunit.

2. Functional sites of interaction between release factor RF1 and the ribosome.

3. Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3.

4. Selection of tRNA by the ribosome requires a transition from an open to a closed form.

5. Structure of the Escherichia coli ribosomal termination complex with release factor 2.

6. The essential role of the invariant GGQ motif in the function and stability in vivo of bacterial release factors RF1 and RF2.

7. The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release.

8. A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation.

9. Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1.

10. A cryo-electron microscopic study of ribosome-bound termination factor RF2.

1. Crystal structure of release factor RF3 trapped in the GTP state on a rotated conformation of the ribosome.

2. Hypothesis: emergence of translation as a result of RNA helicase evolution.

3. Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1.

4. Another burst of smoke: atomic resolution structures of RF3 bound to the ribosome.

5. Kinetic basis for global loss of fidelity arising from mismatches in the P-site codon:anticodon helix.

6. Mutations at the accommodation gate of the ribosome impair RF2-dependent translation termination.

7. Protein synthesis: Translocation in slow motion.

8. Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.

9. Missense suppressor mutations in 16S rRNA reveal the importance of helices h8 and h14 in aminoacyl-tRNA selection.

Review 10. Fidelity at the molecular level: lessons from protein synthesis.