Recessive suppression in yeast <i>Saccharomyces cerevisiae</i> is mediated by a ribosomal mutation

Surguchov, Andrei; Berestetskaya, Y.; Fominykch, Elena S.; Pospelova, E. M.; Smirnov, V.N.; Ter‐Avanesyan, Michael D.; Инге-Вечтомов, С. Г.

doi:10.1016/0014-5793(80)80786-1

Cited by 48 publications

(11 citation statements)

References 14 publications

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“…The level of ambiguity was calculated as the ratio of Leu/Phe incorporation either at different Mg ++ concentrations (Surguchov et al, 1980) or in the presence of neomycin (Surguchov et al, 1981a) or paromomycin (Mironova et al, 1982). Using a ribosomal subunits mixing experiment it has been shown that the 40S subunit of the ribosome is responsible for the elevated ambiguity of in vitro translation (Eustice et al, 1986).…”

Section: Interaction With Dominant (Trna) Suppressorsmentioning

confidence: 99%

Eukaryotic release factors (eRFs) history

Инге-Вечтомов

Zhouravleva

Maury

2003

Biology of the Cell

114

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In the present review, we describe the history of the identification of the eukaryotic translation termination factors eRF1 and eRF3. As in the case of several proteins involved in general and essential processes in all cells (e.g., DNA replication, gene expression regulation...) the strategies and methodologies used to identify these release factors were first established in prokaryotes. The genetic investigations in Saccharomyces cerevisiae have made a major contribution in the field. A large amount of data have been produced, from which it was concluded that the SUP45 and SUP35 genes were controlling translation termination but were also involved in other functions important for the cell organization and the cell cycle accomplishment. This does not seem to be restricted to yeast but is also probably the case in eukaryotes in general. The biochemical studies of the proteins encoded by the higher eukaryote homologs of SUP45 and SUP35 were efficient and permitted the identification of eRF1 as being the key protein in the termination process, eRF3 having a stimulating role. Around 25 years were needed after the identification of sup45 and sup35 mutants for the characterization of their gene products as eRF1 and eRF3, respectively. It also has to be pointed out that if the results came first from bacteria, the identification of RF3 and eRF3 was made practically at the same time. Moreover, eRF1 was the first crystal structure obtained for a class-1 release factor, the bacterial RF2 structure came later. The goal is now to understand at the molecular level the roles of both eRF1 and eRF3 in addition to their translation termination functions.

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Section: Interaction With Dominant (Trna) Suppressorsmentioning

confidence: 99%

Eukaryotic release factors (eRFs) history

Инге-Вечтомов

Zhouravleva

Maury

2003

Biology of the Cell

114

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“…The yeast GST1 gene product is a GTP-binding protein structurally related to polypeptide elongation factor 1-␣ and reportedly functions as a polypeptide releasing factor 3 (eRF3) in yeast. Mutations in the GST1 gene were shown to increase the level of translational ambiguity (41)(42)(43). The human GSPT1 was shown to be capable of complementing the temperature-sensitive growth of the yeast gst1 mutant (44), suggesting that human GSPT1 is a functional homologue of the yeast GST1 gene product and could also function as an eRF3.…”

Section: Processed Gspt1 Can Potentiate Caspase Activation-previ-mentioning

confidence: 99%

The Polypeptide Chain-releasing Factor GSPT1/eRF3 Is Proteolytically Processed into an IAP-binding Protein

Hegde

Srinivasula

Datta

et al. 2003

Journal of Biological Chemistry

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“…Omnipotent suppressor is a class of nonsense suppressors that is recessive and effective toward three types of nonsense codons (3). Mutations in the GSPT/ SUP35 gene were shown to increase the level of translational ambiguity (4,5), suggesting that this gene product may also function as a positive regulator of translational accuracy in yeast.…”

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confidence: 99%

The Eukaryotic Polypeptide Chain Releasing Factor (eRF3/GSPT) Carrying the Translation Termination Signal to the 3′-Poly(A) Tail of mRNA

Hoshino

Imai

Kobayashi

et al. 1999

Journal of Biological Chemistry

239

227

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The mammalian GTP-binding protein GSPT, whose carboxyl-terminal sequence is homologous to the eukaryotic elongation factor EF1␣, binds to the polypeptide chain releasing factor eRF1 to function as eRF3 in the translation termination. The amino-terminal domain of GSPT was, however, not required for the binding. Search for other GSPT-binding proteins in yeast two-hybrid screening system resulted in the identification of a cDNA encoding polyadenylate-binding protein (PABP), whose amino terminus is associating with the poly(A) tail of mRNAs presumably for their stabilization. The interaction appeared to be mediated through the carboxyl-terminal domain of PABP and the aminoterminal region of GSPT. Interestingly, multimerization of PABP with poly(A), which is ascribed to the action of its carboxyl-terminal domain, was completely inhibited by the interaction with the amino-terminal domain of GSPT. These results indicate that GSPT/eRF3 may play important roles not only in the termination of protein synthesis but also in the regulation of mRNA stability. Thus, the present study is the first report showing that GSPT/eRF3 carries the translation termination signal to 3-poly(A) tail ubiquitously present in eukaryotic mRNAs.The yeast GSPT gene, whose product is a GTP-binding protein structurally related to the translation elongation factor EF1␣, was first isolated based on the ability to complement a temperature-sensitive gst1 mutation of Saccharomyces cerevisiae (1). Because DNA synthesis was substantially arrested at the nonpermissive temperature in this mutant, the GSPT gene product appears to play an essential role at the G 1 to S phase transition in the yeast cell cycle. On the other hand, SUP35 was cloned by another group investigating omnipotent suppressor mutant of S. cerevisiae, and the gene turned out to be identical to GSPT (2). Omnipotent suppressor is a class of nonsense suppressors that is recessive and effective toward three types of nonsense codons (3). Mutations in the GSPT/ SUP35 gene were shown to increase the level of translational ambiguity (4, 5), suggesting that this gene product may also function as a positive regulator of translational accuracy in yeast.In eukaryotic protein synthesis, all three types of termination codons are directly recognized by a polypeptide chain releasing factor, eRF1, to release synthesized polypeptide chain from ribosome, and another releasing factor, eRF3, appears to be essentially required for the ribosomal binding of eRF1. Recently, it was reported in S. cerevisiae (6) and Xenopus laevis (7) that the product of the GSPT/SUP35 gene forms a complex with eRF1 to function as eRF3. We previously cloned a human homologue of the yeast GSPT gene (8) and more recently isolated two mouse GSPT genes, the counterpart of human GSPT1 and a novel member of the GSPT gene family, GSPT2 (9). The mammalian GSPT1 and GSPT2 could also associate with eRF1 to function as eRF3, although the two GSPTs were clearly distinct from each other in terms of their amino-terminal sequences, the expression...

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Recessive suppression in yeast Saccharomyces cerevisiae is mediated by a ribosomal mutation

Cited by 48 publications

References 14 publications

Eukaryotic release factors (eRFs) history

Eukaryotic release factors (eRFs) history

The Polypeptide Chain-releasing Factor GSPT1/eRF3 Is Proteolytically Processed into an IAP-binding Protein

The Eukaryotic Polypeptide Chain Releasing Factor (eRF3/GSPT) Carrying the Translation Termination Signal to the 3′-Poly(A) Tail of mRNA

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