Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth.

Janosi, Laszlo; Shimizu, Ichiro; Kaji, Akira

doi:10.1073/pnas.91.10.4249

Cited by 111 publications

(105 citation statements)

References 39 publications

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“…It is known that RRF is essential for bacterial growth since E. coli became lethal upon depletion of RRF [5] or by temperature-sensitive (Ts) mutations in RRF [9]. A reporter gene expression analysis suggests that inactivation of Ts RRF at the non-permissive temperature triggers unscheduled reinitiation of protein synthesis downstream of the stop codon, consistent with the predicted role for ribosome recycling, though the reinitiation mechanism remains to be understood in vitro.…”

Section: Introductionmentioning

confidence: 62%

“…A ¢nal step for recycling may be a direct decomposition of this complex; alternatively, a translocase may be required to forward deacylated tRNA and RF to the E and P sites of the ribosome, respectively, prior to the complete decomposition. In bacteria, the decomposition is catalyzed by a ribosome recycling factor (RRF, originally called ribosome releasing factor [4,5]) probably in concert with the elongation factor EF-G or RF3 in vitro (review in [1]). However, the mechanism of the RRF function is still very poorly understood.…”

Section: Introductionmentioning

confidence: 99%

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Amber mutations in ribosome recycling factors of Escherichia coli and Thermus thermophilus: evidence for C‐terminal modulator element

et al. 1999

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Ribosome recycling factor, referred to as RRF, is essential for bacterial growth because of its activity of decomposition of the post-termination complex of the ribosome after release of polypeptides. In this study, we isolated a conditionally lethal amber mutation, named frr-3, in the Escherichia coli RRF gene at amino acid position 161, showing that the truncation of the C-terminal 25 amino acids of RRF is lethal to E. coli. An RRF gene cloned from Thermus thermophilus, whose protein is 44% identical and 68% similar to E. coli RRF, failed to complement the frr-3(Am) allele. However, truncation of the C-terminal five amino acids conferred intergeneric complementation activity on T. thermophilus RRF, demonstrating the modulator activity of the C-terminal tail. Rapid purification of T. thermophilus RRF was achieved by T7-RNA polymerase-driven overexpression for crystallography.z 1999 Federation of European Biochemical Societies.

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Section: Introductionmentioning

confidence: 62%

Section: Introductionmentioning

confidence: 99%

Amber mutations in ribosome recycling factors of Escherichia coli and Thermus thermophilus: evidence for C‐terminal modulator element

et al. 1999

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“…After translational termination by RF1 or RF2, the termination complex must be disassembled in order to recycle ribosomes, tRNA, mRNA, and release factors+ In vitro release of tRNA and mRNA from the ribosome is catalyzed by elongation factor EF-G and the ribosome recycling factor (RRF, formerly called ribosome releasing factor) in presence of GTP (Hirashima & Kaji, 1972;Ogawa & Kaji, 1975;Janosi et al+, 1996)+ RRF is essential for cell growth (Janosi et al+, 1994)+ We tested whether RF3 could replace EF-G GTPase activity to allow ribosome recycling by RRF+ In this paper, we report a GTPase activity with RF3, which is only dependent on ribosomes, much comparable to the GTPase activity of EF-G+ RF3 stimulates RF1-catalyzed termination dependent on GTP, whereas termination with RF2 is stimulated independently of the presence of GTP+ RF3 can replace EF-G in the in vitro mRNA release from the ribosome by RRF, dependent on GTP+ Excess of RF3 and RRF can result in decomposition of the translation complex, independent of previous termination by RF1 or RF2+…”

Section: Introductionmentioning

confidence: 99%

Release factor RF-3 GTPase activity acts in disassembly of the ribosome termination complex

Grentzmann

Kelly

Laalami

et al. 1998

RNA

187

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RF3 was initially characterized as a factor that stimulates translational termination in an in vitro assay. The factor has a GTP binding site and shows sequence similarity to elongation factors EF-Tu and EF-G. Paradoxically, addition of GTP abolishes RF3 stimulation in the classical termination assay, using stop triplets.We here show GTP hydrolysis, which is only dependent on the simultaneous presence of RF3 and ribosomes. Applying a new termination assay, which uses a minimessenger RNA instead of separate triplets, we show that GTP in the presence of RF3 stimulates termination at rate-limiting concentrations of RF1. We show that RF3 can substitute for EF-G in RRF-dependent ribosome recycling reactions in vitro. This activity is GTP-dependent. In addition, excess RF3 and RRF in the presence of GTP caused release of nonhydrolyzed fmet-tRNA. This supports previous genetic experiments, showing that RF3 might be involved in ribosomal drop off of peptidyl-tRNA. In contrast to GTP involvement of the above reactions, stimulation of termination with RF2 by RF3 was independent of the presence of GTP. This is consistent with previous studies, indicating that RF3 enhances the affinity of RF2 for the termination complex without GTP hydrolysis. Based on our results, we propose a model of how RF3 might function in translational termination and ribosome recycling.

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“…YHRO38w, a ribosome recycling factor homologue: Ribosome releasing factor is responsible for the dissociation of ribosomes from mRNA after translation termination (Ichikawa & Kaji, 1989) and is also called ribosome recycling factor (Janosi et al, 1994). RRF appears to be essential for growth in E. coli (Janosi et al, 1994).…”

Section: Yeast Chromosome Vi11mentioning

confidence: 99%

“…RRF appears to be essential for growth in E. coli (Janosi et al, 1994). Searching databases with YHR038w, the nuclear protein D2 from the plant Daucus carota (S. Schrader, R. Kaldenhoff, & G. Richter, 1993, unpubl.…”

Section: Yeast Chromosome Vi11mentioning

confidence: 99%

New protein functions in yeast chromosome VIII

et al. 1995

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(Johnston et al., 1994) reported the function of 46% of the probable 269 gene products, either as experimentally known or as predicted by exploiting evolutionary relationships to proteins of known function.As of the submission date of this paper, we have been able to add functional information to another 9% of the putative ORFs, by searching more recent versions of sequence databases and using improved similarity search tools (Bork et al., 1992;Koonin et al., 1994;Scharf et al., 1994). As a result, the level of tentative functional assignment for chromosome VI11 is now above 50% of all ORFs (Fig. 1). Results and discussion:The newly identified tentative functions range from enzymes (e.g., chelate synthase, glutaminase-asparaginase, gamma-butyrobetaine hydroxylase, 2-deoxyglucose-' Present address:

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Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth.

Cited by 111 publications

References 39 publications

Amber mutations in ribosome recycling factors of Escherichia coli and Thermus thermophilus: evidence for C‐terminal modulator element

Amber mutations in ribosome recycling factors of Escherichia coli and Thermus thermophilus: evidence for C‐terminal modulator element

Release factor RF-3 GTPase activity acts in disassembly of the ribosome termination complex

New protein functions in yeast chromosome VIII

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