Polypeptide chain elongation factor 1 alpha (EF-1 alpha) from yeast: nucleotide sequence of one of the two genes for EF-1 alpha from Saccharomyces cerevisiae.

Nagata, Shinji; Nagashima, Koji; Tsunetsugu-Yokota, Yasuko; Fujimura, Katsuya; Miyazaki, Motoichi; Kaziro, Yoshito

doi:10.1002/j.1460-2075.1984.tb02053.x

Cited by 148 publications

(34 citation statements)

References 33 publications

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“…Many of the genes coding for components of the translational apparatus are duplicated in S. cerevisiae, including TEFI and TEF2, the genes encoding elongation factor lot (EF-lat) (36,49), and EFTI and EFT2, the genes encoding EF-2 (40). The TEF3 gene was localized to the left arm of chromosome XVI, centromere distal to the RADJ gene, by hybridization of TEF3 DNA to yeast chromosomes separated by gel electrophoresis and to the library of overlapping yeast genomic DNA fragments.…”

Section: S S S L L L a I A S G A N D V S H I Q A A H V C V G I S G M mentioning

confidence: 99%

DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae.

Ripmaster¹,

Vaughn²,

Woolford³

1993

Mol. Cell. Biol.

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To identify Saccharomyces cerevisiae mutants defective in assembly or function of ribosomes, a collection of cold-sensitive strains generated by treatment with ethyl methanesulfonate was screened by sucrose gradient analysis for altered ratios of free 40S to 60S ribosomal subunits or qualitative changes in polyribosome profiles. Mutations The eukaryotic ribosome is a complex organelle which in most species contains more than 75 different proteins and four different RNA molecules. The primary sequences of eukaryotic rRNAs and many eukaryotic ribosomal proteins (r-proteins) (reviewed in references 65 and 66) have been determined or inferred from sequences of the respective genes. Regulation of expression of these genes has been studied in some detail (65,66). Despite the large volume of data concerning the structure and expression of individual components of eukaryotic ribosomes, the pathway of assembly of ribosomal subunits and the functional roles that r-proteins and rRNAs play during the translation process are not well understood.Ribosome biogenesis occurs in the nucleolus of eukaryotic cells, where rRNA is transcribed and processed, and associates with r-proteins imported from the cytoplasm (reviewed in references 19, 65, and 66). Preribosomal particles containing rRNA precursors, r-proteins, and non-r-proteins have been detected within the nucleolus (59, 63). Most of the r-proteins assemble into subunits while in the nucleolus, although some final steps of maturation occur after transport of subunits to the cytoplasm (61). The ribosomal subunits are then competent to catalyze protein synthesis.Reconstitution and genetic studies have been applied successfully to study the ribosome assembly pathway in prokaryotic cells. Functional 30S and 50S ribosomal subunits of Escherichia coli can be reconstituted from purified rRNA and r-proteins in vitro (38,60

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Section: S S S L L L a I A S G A N D V S H I Q A A H V C V G I S G M mentioning

confidence: 99%

DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae.

Ripmaster¹,

Vaughn²,

Woolford³

1993

Mol. Cell. Biol.

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“…It promotes the GTP-dependent binding of aminoacyl-tRNA to the ribosome and participates in the proofreading of the codon-anticodon match (16,23,38). Yeast EF-la is encoded by two unlinked genes, TEF1 and TEF2 (5,25,26,31). The two genes are efficiently transcribed at about the same level, and the presence of either gene is sufficient for cell viability and normal growth rates (4).…”

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“…The ura3-52 allele is not suppressible and does not revert (27). (26); (B) map of the TEF2-L YS2 region (31). The extent of the deletion in the tef2-A (or lys2-201) allele is also shown (31,34 confirmed that pJS7 contains one of the two genes encoding EF-la, since the 0.87-kilobase EcoRI-HindIII fragment from the pJS7 insert hybridized with the p3L6 TEF2 probe (kindly provided by C. Falco; data not shown).…”

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Elongation factor EF-1 alpha gene dosage alters translational fidelity in Saccharomyces cerevisiae.

et al. 1989

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Changes in the dosage of genes encoding elongation factor EF-la were shown to cause parallel changes in the misreading of nonsense codons. Higher amounts of EF-la were correlated with increased nonsense suppression, suggesting that the level of EF-la is critically involved in translational fidelity.To understand how translational accuracy is controlled, it is important to identify which genes are involved and to determine how they exert their effects. The best-studied mutations that alter translational fidelity in yeast cells are the codon-specific suppressors caused by altered tRNA anticodons (for reviews, see references 32 and 40). Among other genes that affect translational accuracy are the omnipotent suppressors, e.g., sup35 and sup45, which cause non-codonspecific misreading (3,9,11,17, 42), and the recessive antisuppressor, asu9, which increases translational fidelity in sup35 and sup45 strains (19,20). While attempting to clone asu9, we found that an extra copy of one of two redundant genes coding for the translation elongation factor EF-la increased suppression efficiency in a sup45-2 asu9 strain.EF-la is an important component of the translational apparatus. It promotes the GTP-dependent binding of aminoacyl-tRNA to the ribosome and participates in the proofreading of the codon-anticodon match (16,23,38). Yeast EF-la is encoded by two unlinked genes, TEF1 and TEF2 (5,25,26,31). The two genes are efficiently transcribed at about the same level, and the presence of either gene is sufficient for cell viability and normal growth rates (4). Mutations in the yeast EF-la and its Escherichia coli analog EF-Tu have been found to affect translational fidelity (13,14,30,37,41). In yeast cells, single mutational changes in TEF2 were shown to cause dominant suppression of both nonsense and frameshift mutations (30). In this paper, we show that the level of EF-la also affects translational fidelity.(Preliminary accounts of some of these results have been reported elsewhere [J. M. Song and S. W. Liebman, Yeast 2:S364, 1986; S. W. Liebman, J. M. Song, J. All-Robyn, E. Griffin, and D. Kelley-Geraghty, NATO ASI Ser. H14: [403][404][405][406][407][408][409][410][411][412][413][414] 1988].)A DNA clone containing the TEF1 gene complements asu9. Saccharomyces cerevisiae strain SL680-4B (a asu9-1 sup45-2 leu2-1 met8-1 trpl-1 ade3-26 hisS-2 lys2-1 canl-132 ura3-52) was chosen as the host for selection of asu9 complementing clones. In this strain, the asu9-1 mutation prevented growth on medium containing trichodermin (0.5 ,ug/ml; kindly provided by Leo Pharmaceutical Products), and the asu9-1 and sup45-2 mutations together permitted only a low * Corresponding author. and replated on medium with uracil, leucine, and methionine omitted and containing 0.5 jxg of trichodermin per ml to select for asu9 complementing clones. Plasmid pJS7, isolated from one of the fastest-growing transformants on this medium, caused both a slight reduction in the trichodermin sensitivity and enhanced suppression of leu2-1 and met8-1 upon retransformat...

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“…Subsequent hydrolysis of GTP and release of the factor as eEF-Tu-GDP allows its reuse throughout the elongation process (reviewed reference in 13). The functional importance of eEF-Tu in 'roteii1 synthesis has stimulated research on the structure and functional domains of the protein itself (12,29,30,33) as well as on the identification and expression of the genes for etF-Tu (2,4,14,15,19,25,31,32).…”

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“…Genomic and/or cDNA clones exist for eEF-Tu from Saccharomyces cerevisiae (4,19,25), Artemia sp. (14,31), and humans (2).…”

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Expression of a gene for mouse eucaryotic elongation factor Tu during murine erythroleukemic cell differentiation.

Roth¹,

Bragg²,

Corrias³

et al. 1987

Mol. Cell. Biol.

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The eucaryotic elongation factor Tu (eEF-Tu) is a single polypeptide with an approximate M, of 53,000.During protein synthesis eEF-Tu promotes the binding of aminoacyl-tRNA to the ribosome. To study the expression of the gene(s) for this factor, a genomic clone was isolated that contains a mouse eEF-Tu gene. We screened a phage genomic library with a synthetic oligonucleotide probe complementary to a region of the Saccharomyces cerevisiae and Artemia sp. eEF-Tu genes which codes for an area that is highly conserved between both yeast and Artemui sp. eEF-Tu. From approximately 75,000 phage plaques we obtained five isolates with apparently identical inserts. All five clones contained a 3.8-kilobase EcoRI fragment that hybridized to additional oligonucleotide probes corresponding to different conserved regions of eEF-Tu. We sequenced the 5' end of one genomic clone and determined the length of the cloned fragment that was protected by eEF-Tu mRNA in Si nuclease protection assays. A quantitative SI nuclease protection assay was used to compare the relative steady-state levels of eEF-Tu mRNA in total RNA isolated from hexamethylenebisacetamide-induced muriniP erythroleukemia cells. The results show a dramatic reduction in the steady-state level of eEF-Tu mRNA as differentiation proceeds. A similar reduction in transcription of eEF-Tu mRNA was observed in isolated nuciei. Finally, we examined the in vivo synthesis of eEF-Tu during differentiation and found that it declined in a manner parallel to the decline in the steady-state level of eEF-Tu mRNA. In addition, we have isolated and sequenced a cDNA clone for mouse eEF-Tu. The derived amino acid sequence is compared with sequences from other eucaryotes.

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Polypeptide chain elongation factor 1 alpha (EF-1 alpha) from yeast: nucleotide sequence of one of the two genes for EF-1 alpha from Saccharomyces cerevisiae.

Cited by 148 publications

References 33 publications

DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae.

DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae.

Elongation factor EF-1 alpha gene dosage alters translational fidelity in Saccharomyces cerevisiae.

Expression of a gene for mouse eucaryotic elongation factor Tu during murine erythroleukemic cell differentiation.

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