Characterization of yeast EF-1α: Non-conservation of post-translational modifications

Cavallius, Jens; Zoll, Wendy L.; Chakraburtty, Kalpana; Merrick, William C.

doi:10.1016/0167-4838(93)90281-u

Cited by 64 publications

(80 citation statements)

References 39 publications

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“…In this screen, ribosomal proteins L12 and L23, as well as eukaryotic translation elongation factors EF1␣ and EF2, were identified as lysine-methylated proteins, implying that protein-lysine methylation is deeply involved in translation, whereas protein acetylation seemed to have relatively wider involvement in cellular metabolic activity. Ribosomal proteins are methylated in some organisms (32)(33)(34)(35), and lysine methylation of EF1␣ has been widely observed among eukaryotes (36). Although methylation of the fission yeast EF1␣ had not been known, our results demonstrated that this is the case also in fission yeast.…”

Section: Identification Of Target Proteins Using the Mobilitome Data mentioning

confidence: 47%

Global Analysis of Gel Mobility of Proteins and Its Use in Target Identification

Shirai

Matsuyama

Yashiroda

et al. 2008

Journal of Biological Chemistry

118

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SDS-PAGE is a basic method that has long been used for separation of proteins according to their molecular sizes. Despite its simplicity, it provides information on characteristics of proteins beyond their molecular masses because gel mobility of proteins often reflects their physicochemical properties and posttranslational modifications. Here we report on a global analysis of gel mobility of the proteome, which we term the "mobilitome," covering 93.4% of the fission yeast proteome. To our surprise, more than 40% of proteins did not migrate to their calculated positions. Statistical analyses revealed that the discrepancy was largely dependent on the hydrophobicity of proteins. This experimental data set, with a high coverage rate of real mobility, made it feasible to identify proteins detected on the gel without using any specialized techniques. This approach enabled us to detect previously unknown post-translational modifications of a protein; for example, we revealed that eIF5A is novel substrate of a Sir2-related deacetylase Hst2. Furthermore, we concomitantly identified twelve acetylated and eight methylated proteins using specific anti-acetylated and antimethylated lysine antibodies, most of which had not been known to be subject to the modifications. Thus, we propose the general usefulness of the mobilitome and electrophoresis-based methodology for the identification and characterization of proteins detected on the gel.

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Section: Identification Of Target Proteins Using the Mobilitome Data mentioning

confidence: 47%

Global Analysis of Gel Mobility of Proteins and Its Use in Target Identification

Shirai

Matsuyama

Yashiroda

et al. 2008

Journal of Biological Chemistry

118

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“…In yeast, these include di-and trimethyl lysine, but do not include phosphoglycerol ethanolamine as observed in the mammalian factor (Cavallius et al 1993). The functional role of these modifications, however, remains unclear as mutation of the methylation sites does not affect cell growth or general protein synthesis (Cavallius et al 1997).…”

Section: Aa-trna Delivery By Eef1mentioning

confidence: 99%

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

2016

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In this review, we provide an overview of protein synthesis in the yeast Saccharomyces cerevisiae. The mechanism of protein synthesis is well conserved between yeast and other eukaryotes, and molecular genetic studies in budding yeast have provided critical insights into the fundamental process of translation as well as its regulation. The review focuses on the initiation and elongation phases of protein synthesis with descriptions of the roles of translation initiation and elongation factors that assist the ribosome in binding the messenger RNA (mRNA), selecting the start codon, and synthesizing the polypeptide. We also examine mechanisms of translational control highlighting the mRNA cap-binding proteins and the regulation of GCN4 and CPA1 mRNAs.

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“…1). Subsequently, the same modification was found in plant (11), but not yeast (12), eEF1A. The discovery of the EPG modification was prompted by the observation that a 49-kDa cytosolic protein was labeled after incubation of mammalian cells in culture with tritiated ethanolamine (Etn) (9,10), an approach that was originally aimed at identifying glycosylphosphatidylinositol (GPI)-anchored proteins.…”

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confidence: 99%

Phosphatidylethanolamine Is the Precursor of the Ethanolamine Phosphoglycerol Moiety Bound to Eukaryotic Elongation Factor 1A

Signorell

Jelk

Rauch

et al. 2008

Journal of Biological Chemistry

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In addition to its conventional role during protein synthesis, eukaryotic elongation factor 1A is involved in other cellular processes. Several regions of interaction between eukaryotic elongation factor 1A and the translational apparatus or the cytoskeleton have been identified, yet the roles of the different post-translational modifications of eukaryotic elongation factor 1A are completely unknown. One amino acid modification, which so far has only been found in eukaryotic elongation factor 1A, consists of ethanolamine-phosphoglycerol attached to two glutamate residues that are conserved between mammals and plants. We now report that ethanolamine-phosphoglycerol is also present in eukaryotic elongation factor 1A of the protozoan parasite Trypanosoma brucei, indicating that this unique protein modification is of ancient origin. In addition, using RNA-mediated gene silencing against enzymes of the Kennedy pathway, we demonstrate that phosphatidylethanolamine is a direct precursor of the ethanolamine-phosphoglycerol moiety. Down-regulation of the expression of ethanolamine kinase and ethanolamine-phosphate cytidylyltransferase results in inhibition of phosphatidylethanolamine synthesis in T. brucei procyclic forms and, concomitantly, in a block in glycosylphosphatidylinositol attachment to procyclins and ethanolamine-phosphoglycerol modification of eukaryotic elongation factor 1A.

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Characterization of yeast EF-1α: Non-conservation of post-translational modifications

Cited by 64 publications

References 39 publications

Global Analysis of Gel Mobility of Proteins and Its Use in Target Identification

Global Analysis of Gel Mobility of Proteins and Its Use in Target Identification

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

Phosphatidylethanolamine Is the Precursor of the Ethanolamine Phosphoglycerol Moiety Bound to Eukaryotic Elongation Factor 1A

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