Cloning and genetic characterization of a calcium‐ and phospholipid‐binding protein from <i>Saccharomyces cerevisiae</i> that is homologous to translation elongation factor‐1γ

Kambouris, Nicholas G.; Burke, Daniel J.; Creutz, Carl E.

doi:10.1002/yea.320090206

Cited by 17 publications

(15 citation statements)

References 47 publications

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“…EF-13 alone has nucleotide exchange activity, although in A. salina, this activity is stimulated by EF-l1y (22). The TEF3 gene is identical to the CAMI gene, recently cloned by Kambouris et al (23). Tef3p (Camlp) was found to be tightly associated with a polypeptide of 34 kDa, which is identical to the published molecular mass for S. cerevisiae elongation factor EF-13 (11).…”

Section: Discussionsupporting

confidence: 56%

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: Discussionsupporting

confidence: 56%

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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“…In S. cerevisiae, CPBP is encoded by the TEF3 gene and has a 64% sequence homology with EF-1␥, which is encoded by the TEF4 gene (14). We failed to detect EF-1␥ during CPBP purification, which is in line with a previous report (15). Although the EF-1 complex plays an important role in protein translation (16), disruption of the TEF3 and TEF4 genes failed to be lethal (14), leading to the conclusion that CPBP and its homologue, EF-1␥, may be redundant in translational regulation but may have other, not-yet-described functions (14).…”

Section: Discussionsupporting

confidence: 92%

A homologue of elongation factor 1γ regulates methionine sulfoxide reductase A gene expression in Saccharomyces cerevisiae

Hanbauer

Boja

Moskovitz

2003

Proc. Natl. Acad. Sci. U.S.A.

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Methionine sulfoxide reductase A (MsrA) maintains the function of many proteins by reversing oxidation of methionine residues. Lack of this repair mechanism very likely increases aging-related disease susceptibility. In Saccharomyces cerevisiae, disruption of the msrA gene increases free and protein-bound methionine sulfoxide and decreases cell viability. Although the underlying mechanisms in the induction of the msrA gene are still unknown, a transcriptional regulation may be involved. Hence, a search of nuclear proteins regulating the msrA gene is a major target of the experiments reported in this article. Using protein purification combined with MS, we discovered that calcium phospholipid-binding protein (CPBP), a homologue of elongation factor-1␥, is a component of a complex that binds to the msrA promoter. By measuring CPBP cooperative binding to the msrA promoter, we have mapped the CPBP binding site to a 39-bp sequence at the 3 end of the promoter. In a mutant yeast strain lacking the CPBP-encoding gene, the ability to overexpress msrA mRNA and MsrA protein was impaired and MsrA catalytic activity was greatly reduced, suggesting that CPBP may enhance msrA gene expression.

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“…3 The TEF3 gene was isolated as encoding a calcium-dependent membrane binding protein and as a gene dosage suppressor of a 40S ribosomal subunit assembly mutant. 4,5 The later effect was not seen for TEF4. 3 TEF4 was isolated as a high copy antisuppressor of tRNA mediated nonsense suppression.…”

Section: Introductionmentioning

confidence: 88%

The Translation Elongation Factor eEF1B Plays a Role in the Oxidative Stress Response Pathway

Olarewaju

Ortiz²,

Chowdhury³

et al. 2004

RNA Biology

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The multi-subunit guanine nucleotide exchange factor eEF1B for Saccharomyces cerevisiae Translation Elongation Factor 1A (eEF1A) has catalytic (eEF1Bα) and noncatalytic (eEF1Bγ) subunits. Deletion of the two nonessential genes encoding eEF1Bγ has no dramatic effects on total protein synthesis or translational fidelity. Instead, loss of each gene gives resistance to oxidative stress, and loss of both is additive. The level of stress resistance is similar to overexpression of the Yap1p stress transcription factor and is dependent on the presence of the YAP1gene. Cells lacking the catalytic eEF1Bα subunit show even greater resistance to CdSO 4 , with or without eEF1Bγ present. Thus, the loss of guanine nucleotide exchange activity promotes the resistance. As nucleotide exchange is a critical regulator of most G-proteins, these results indicate a new mechanism in the growing list of examples of post-transcriptional responses to cellular stress.

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Cloning and genetic characterization of a calcium‐ and phospholipid‐binding protein from Saccharomyces cerevisiae that is homologous to translation elongation factor‐1γ

Cited by 17 publications

References 47 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.

A homologue of elongation factor 1γ regulates methionine sulfoxide reductase A gene expression in Saccharomyces cerevisiae

The Translation Elongation Factor eEF1B Plays a Role in the Oxidative Stress Response Pathway

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