The allosuppressor gene SAL4 encodes a protein important for maintaining translational fidelity in Saccharomyces cerevisiae

Crouzet, Marc; İzgü, Fatih; Grant, Chris M.; Tuite, Mick F.

doi:10.1007/bf00434078

Cited by 27 publications

(15 citation statements)

References 36 publications

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“…Their identity to SUP1 and SUP2, respectively, was established by localization on linkage groups: SUP1 (SUP45)-in the right arm of the II chromosome (Ter Avanesyan and Inge-Vechtomov, 1974) and SUP2 (SUP35)-in the right arm of the IV chromosome (Ter Avanesyan, 1981). Later, the identity of these genes was confirmed by their cloning and sequencing (Surguchov et al, 1983;Himmelfarb et al, 1985;Breining and Piepersberg, 1986;Telkov et al, 1986;Crouzet et al, 1988;Kushnirov et al, 1988;Wilson and Culbertson, 1988).…”

Section: Identification Of Sup45 and Sup35 Genes In Saccharomyces Cermentioning

confidence: 96%

“…The genes with comparable characteristics when mutated had been described repeatedly and given different names by several groups-SUP1: SUP45 (Hawthorne and Leupold, 1974), SUPQ (Gerlach, 1975), SUP47 (Ono et al, 1984), SAL4 (Crouzet et al, 1988); SUP2: SUP35 (Hawthorne and Leupold, 1974), SUP36 (Ono et al, 1984), SUPP (Gerlach, 1975), SAL3 (Crouzet and Tuite, 1987); GST1 (Kikuchi et al, 1988). Finally in accordance with the internationally accepted nomenclature these two genes were named SUP45 and SUP35.…”

Section: Identification Of Sup45 and Sup35 Genes In Saccharomyces Cermentioning

confidence: 99%

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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: Identification Of Sup45 and Sup35 Genes In Saccharomyces Cermentioning

confidence: 96%

Section: Identification Of Sup45 and Sup35 Genes In Saccharomyces Cermentioning

confidence: 99%

Eukaryotic release factors (eRFs) history

Инге-Вечтомов

Zhouravleva

Maury

2003

Biology of the Cell

114

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“…The SUP45 and SUP35 gene products belong to the highly conserved eRF1 and eRF3 protein families, respectively (15,52). Both sup45 and sup35 mutants exhibit, among pleiotropic effects, either an omnipotent suppressor phenotype, i.e., suppression of all three nonsense codons (22,25), or an allosuppressor phenotype, i.e., an ability to enhance nonsense suppression by a weak suppressor tRNA (8,9). The effect of overexpression of the SUP45 and SUP35 genes of S. cerevisiae in a nonsense suppressor tRNA background has been studied recently.…”

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confidence: 99%

Overexpression of Human Release Factor 1 Alone Has an Antisuppressor Effect in Human Cells

Goff

Maury

Jean-Jean

1997

Molecular and Cellular Biology

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Two eukaryotic proteins involved in translation termination have recently been characterized in in vitro experiments. Eukaryotic release factor 1 (eRF1) catalyzes the release of the polypeptide chain without any stop codon specificity. The GTP-binding protein eRF3 confers GTP dependence to the termination process and stimulates eRF1 activity. We used tRNA-mediated nonsense suppression at different stop codons in a cat reporter gene to analyze the polypeptide chain release factor activities of the human eRF1 and eRF3 proteins overexpressed in human cells. In a chloramphenicol acetyltransferase assay, we measured the competition between the suppressor tRNA and the human release factors when a stop codon was present in the ribosomal A site. Whatever the stop codon (UAA, UAG, or UGA) present in the cat open reading frame, the overexpression of human eRF1 alone markedly decreased translational readthrough by suppressor tRNA. Thus, like the procaryotic release factors RF1 and RF2 in Escherichia coli, eRF1 seems to have an intrinsic antisuppressor activity in human cells. Levels of antisuppression of overexpression of both eRF3 and eRF1 were almost the same as those of overexpression of eRF1 alone, suggesting that eRF1-eRF3 complex-mediated termination may be controlled by the expression level of eRF1. Surprisingly, when overexpressed alone, eRF3 had an inhibitory effect on cat gene expression. The results of cat mRNA stability studies suggest that eRF3 inhibits gene expression at the transcriptional level. This indicates that in vivo, eRF3 may perform other functions, including the stimulation of eRF1 activity.Translation is usually completed when a stop codon enters the A site of the ribosome. Recognition of the stop codon by the release factor liberates the nascent polypeptide (4, 7). The first eukaryotic release factor, named eukaryotic release factor 1 (eRF1), was recently identified, and the in vitro release factor activity of human and Xenopus laevis eRF1 was characterized (15). eRF1 recognizes all three nonsense codons (UAA, UGA, and UAG) and catalyzes peptidyl-tRNA hydrolysis in a GTPindependent reaction. Because translation termination was shown to be a GTP-dependent process (28), it was suggested that another release factor which confers the GTP requirement to translation termination exists in eukaryotes (15,44). This second factor, named eRF3, which was first isolated from X. laevis (52), exhibits GTP binding motifs and stimulates eRF1 release factor activity in vitro but only in the presence of GTP. Although eRF3 does not recognize stop codons by itself, it binds to eRF1 to form an active termination complex. It was proposed that a quaternary complex composed of eRF1, eRF3, GTP, and the ribosome can govern eukaryotic translation termination at a stop codon of the mRNA (52). eRF3 is an eRF1-and ribosome-dependent GTPase (16) and is most likely the functional homolog of the recently sequenced prokaryotic release factor 3 (RF-3), a GTP-binding protein which stimulates RF-2 activity upon translation terminatio...

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“…From these phenotypic characteristics, SUP35 and SUP45 are believed to be involved in translational fidelity. Allosuppressor allele mutations of SUP35 and SUP45 have also been isolated and named sal3 and sal4, respectively (4,5 (15).…”

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confidence: 99%