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Structural basis for aminoglycoside inhibition of bacterial ribosome recycling
- M. A. Borovinskaya, R. Pai, J. Cate
- Biology, ChemistryNature Structural &Molecular Biology
- 29 July 2007
It is shown in X-ray crystal structures of the Escherichia coli 70S ribosome that RRF binding causes RNA helix H69 of the large ribosomal subunit, which is crucial for subunit association, to swing away from the subunit interface, providing a structural explanation for aminoglycoside inhibition of ribosomes recycling.
The role of ribosome recycling factor in dissociation of 70S ribosomes into subunits.
- G. Hirokawa, Romana M. Nijman, V. Raj, H. Kaji, K. Igarashi, A. Kaji
- Biology, Computer ScienceRNA
- 1 August 2005
It is shown that 70S ribosomes, as well as the model post-termination complexes, are dissociated into stable subunits by cooperative action of three translation factors: ribosome recycling factor, elongation factor G (EF-G), and initiation factor 3 (IF3).
Exploring the Stereochemistry of CXCR4-Peptide Recognition and Inhibiting HIV-1 Entry with d-Peptides Derived from Chemokines*
Acting as CXCR4 antagonists and with much higher biological stability than l-counterparts, the d-peptides showed significant activity in inhibiting the replication of CX CR4-dependent HIV-1 strains.
Release of Ribosome-bound Ribosome Recycling Factor by Elongation Factor G*
It is proposed that the release of ribosome-bound RRF by EF-G is required for post-termination complex disassembly, and thiostrepton traps an intermediate complex having RRF on a position that clashes with the P/E site bound tRNA.
The ribosome-recycling step: consensus or controversy?
HIV-1 reverse transcriptase inhibitor from Phyllanthus niruri.
An aqueous extract of Phyllanthus niruri (Euphorbiaceae) inhibited human immunodeficiency virus type-1 reverse transcriptase (HIV-1-RT), and repandusinic acid A monosodium salt (RA) was shown to be a competitive inhibitor with respect to the template-primer while it was a noncompetitive inhibitor withrespect to the substrate.
Post‐termination complex disassembly by ribosome recycling factor, a functional tRNA mimic
The data are consistent with the notion that RRF binds to the A‐site and is translocated to the P‐site, releasing deacylated tRNA from the P- and E‐sites, and the release of mRNA, is accompanied by therelease of RRF and EF‐G from the ribosome.
Progression of the ribosome recycling factor through the ribosome dissociates the two ribosomal subunits.
Structural insights into initial and intermediate steps of the ribosome‐recycling process
- T. Yokoyama, T. Shaikh, Nobuhiro Iwakura, H. Kaji, A. Kaji, R. Agrawal
- Biology, ChemistryThe EMBO journal
- 4 April 2012
The results suggest that the ribosomal intersubunit reorganizations upon RRF binding and subsequentEF‐G binding could be instrumental in destabilizing the PoTC and the modes of action of EF‐G during tRNA translocation and ribosome‐recycling steps are markedly different.