Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome: functional implications (Q24562642)

1

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Manjuli R Sharma

2

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Michael C Kiel

3

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Go Hirokawa

4

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Timothy M Booth

5

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Christian M T Spahn

6

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Robert A Grassucci

7

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Akira Kaji

Proceedings of the National Academy of Sciences of the United States of America

8

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language of work or name

English

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publication date

15 June 2004

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published in

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volume

101

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issue

24

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page(s)

8900-5

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cites work

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

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

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Structure and binding mode of a ribosome recycling factor (RRF) from mesophilic bacterium

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The path of messenger RNA through the ribosome

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Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch

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Visualization of tRNA movements on the Escherichia coli 70S ribosome during the elongation cycle

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Crystal structure of the ribosome recycling factor from Escherichia coli

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Specific interaction between the ribosome recycling factor and the elongation factor G from Mycobacterium tuberculosis mediates peptidyl-tRNA release and ribosome recycling in Escherichia coli

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A ratchet-like inter-subunit reorganization of the ribosome during translocation

24 March 2017

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The fourth step of protein synthesis: disassembly of the posttermination complex is catalyzed by elongation factor G and ribosome recycling factor, a near-perfect mimic of tRNA.

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Location of translational initiation factor IF3 on the small ribosomal subunit

27 September 2017

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Visualization of elongation factor G on the Escherichia coli 70S ribosome: the mechanism of translocation

27 September 2017

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Visualization of release factor 3 on the ribosome during termination of protein synthesis

27 September 2017

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Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing.

30 May 2018

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Movement of the decoding region of the 16 S ribosomal RNA accompanies tRNA translocation

30 May 2018

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Fitting atomic models into electron-microscopy maps

30 May 2018

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EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=428444

Evidence for in vivo ribosome recycling, the fourth step in protein biosynthesis

30 May 2018

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Visualization of elongation factor Tu on the Escherichia coli ribosome.

30 May 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0401904101

Release of ribosome-bound ribosome recycling factor by elongation factor G.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0401904101

Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0401904101

Binding of ribosome recycling factor to ribosomes, comparison with tRNA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0401904101

Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution † 1 †This article is dedicated to the memory of Anneke van Heel. 1Edited by M.F. Moody

21 January 2018

1 reference

12 December 2020

Release factor RF3 abolishes competition between release factor RF1 and ribosome recycling factor (RRF) for a ribosome binding site

1 reference

12 December 2020

Effect of buffer conditions on the position of tRNA on the 70 S ribosome as visualized by cryoelectron microscopy

1 reference

12 December 2020

Novel roles for classical factors at the interface between translation termination and initiation

1 reference

12 December 2020

Characterization of Mycobacterium tuberculosis ribosome recycling factor (RRF) and a mutant lacking six amino acids from the C-terminal end reveals that the C-terminal residues are important for its occupancy on the ribosome

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.0401904101

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ADS bibcode

2004PNAS..101.8900A

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1 reference

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PubMed publication ID

15178758

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