The Elongation factor-1δ (EF-1δ) originates from gene duplication of an EF-1β ancestor and fusion with a protein-binding domain

Guerrucci, Marie-Anne; Monnier, Annabelle; Delalande, Christelle; Bellé, Robert

doi:10.1016/s0378-1119(99)00153-5

Cited by 11 publications

(11 citation statements)

References 24 publications

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“…The eEF1d protein, a subunit of elongation factor 1, was discovered in Xenopus [6] and is specific to higher animals [9]. The protein eEF1d, although sharing an activity redundant with eEF1b, is original both at the structural level by the presence of a leucine zipper motif and at the functional guanine nucleotide exchange domain which cannot substitute for the eEF1b counterpart (see Introduction).…”

Section: Discussionmentioning

confidence: 99%

“…Although less investigated, a regulatory role for the elongation step has also been suggested [4], mainly since the discovery of the highly organized macromolecular structerminal of eEF1d was not able to complement yeast mutants conditional for EF1b [8]. Furthermore, the eEF1d protein contains a specific N-terminal domain, characterized by the presence of a leucine zipper motif, a feature related to a protein-binding function [9]. Thus, the specific function of eEF1d requires determination.…”

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confidence: 99%

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Sea urchin elongation factor 1? (EF1?) and evidence for cell cycle-directed localization changes of a sub-fraction of the protein at M phase

Boulben

Monnier

Breton

et al. 2003

Cellular and Molecular Life Sciences (CMLS)

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Eukaryotic elongation factor 1 (eEF1) is a translational multimolecular complex reported in higher eukaryotes to be a target of CDK1/cyclin B, the universal regulator of M phase, but whose role in the cell cycle remains to be determined. A specific polyclonal antibody was produced and used to characterize the delta subunit of sea urchin elongation factor 1 (SgEF1delta) in early embryos, a powerful model for investigating cell cycle regulation. The SgEF1delta protein was present in unfertilized eggs as two isoforms of 35 and 37 kDa, issued from two different mRNAs. The two canonical eEF1delta partners, eEF1gamma and eEF1beta, were shown to co-immunoprecipitate with the SgEF1delta isoforms. Both isoforms were associated in a macromolecular complex, which resolved upon gel filtration chromatography at a molecular weight > 400 kDa, suggesting association with other yet unidentified partners. After fertilization, the amount as well as the ratio of both SgEF1delta isoforms remained constant during the first cell division as judged by Western blotting. Immunofluorescence analysis showed that a pool of the protein concentrated as a ring at the embryo nuclear location around the period of nuclear envelope breakdown and was visualized later as two large spheres around the mitotic spindle poles. Thus, the eEF1delta protein shows cell cycle-specific localization changes in sea urchin embryos.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Sea urchin elongation factor 1? (EF1?) and evidence for cell cycle-directed localization changes of a sub-fraction of the protein at M phase

Boulben

Monnier

Breton

et al. 2003

Cellular and Molecular Life Sciences (CMLS)

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“…Published phylogenetic analyses of plant eEF1Ba and eEF1Bb proteins suggest that eEF1Bb subunits from dicots and monocots are more closely related to each other than are eEF1Bb and eEF1Ba subunits within their own respective monocot or dicot classes (Fig. 7) (Guerrucci et al 1999). Rice eEF1Bb was strongly phosphorylated by CDK, and its recognition sequence (TPDV) is also found in eEF1Bb subunits from corn, sorghum, and wheat (Fig.…”

Section: Cdk Physically and Catalytically Associates With Eef1bbmentioning

confidence: 97%

“…A difference in phosphorylatability by human CDK between wild-type and T91A mutant eEF1Bb proteins A portion of the phylogenetic tree based on the predicted amino acid sequences of eEF1Bb and eEF1Ba from several plant species (Guerrucci et al 1999) is shown. Predicted amino acid sequences of consensus CDK phosphorylation sites located within the N-terminal 100 residues are given in parentheses.…”

Section: Cdk Physically and Catalytically Associates With Eef1bbmentioning

confidence: 99%

Mutation of a conserved CDK site converts a metazoan Elongation Factor 1Bβ subunit into a replacement for yeast eEF1Bα

et al. 2003

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Elongation factor subunit eEF1Bbeta (formerly EF-1beta in plants and EF-1delta in animals) was identified and cloned in a screen for proteins from pea that interact with a cyclin-dependent kinase (CDK). CDKs are enzymes that regulate progression through meiotic and mitotic cell cycles in eukaryotes. eEF1Bbeta and the related protein eEF1Balpha (formerly EF-1beta' in plants and EF-1beta in animals and fungi) can catalyze GTP/GDP exchange on the G-protein eEF1A (formerly EF-1alpha in plants, animals and fungi) during the elongation phase of protein synthesis in eukaryotes. Recombinant Cdc2 and its native homologues from pea extracts associated both in vitro and in vivo with eEF1Bbeta. A Cdc2-cyclin B complex phosphorylated recombinant plant eEF1Bbetas, but not eEF1Balpha. These interactions between CDK and eEF1Bbeta prompted investigations into the in vivo consequences of this relationship. Expression of cDNAs encoding rice or pea eEF1Bbeta subunits failed to complement a Saccharomyces cerevisiae mutant deleted for the eEF1Balpha gene, as was previously observed for the human eEF1Bbeta. However, replacement of Thr91, the sole consensus CDK phosphorylation site in pea eEF1Bbeta, with alanine allowed the pea protein to substitute for eEF1Balpha function in vivo. In addition, this rescued strain was severely cold sensitive, and more sensitive to translational inhibitors than wild-type yeast. Taken together, these results suggest a physiological connection between the cyclin-dependent class of kinases and a translational elongation factor in mitotic cells, and provide the first in vivo evidence that an altered form of eEF1Bbeta can serve as the guanine nucleotide exchange factor for eEF1A.

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“…However, yeast deficient in its catalytic subunit can be rescued from lethality by eEF1A overexpression (11). eEF1D, which originated from gene duplication of an eEF1B2 ancestor and fusion with a leucine zipper domain (12), is unique to higher eukaryotes, whereas a divergent catalytic subunit, termed eEF1B␤, has developed in plants (13). Although eEF1B2 and eEF1D share a common function and highly homologous catalytic domains, they have been suggested to bind their substrate eEF1A through different sites, on the basis of the observation that binding of eEF1A to eEF1B2 results in masking of a CK2 phosphorylation site, whereas a similarly located site on eEF1D is not masked by binding to eEF1A (14).…”

mentioning

confidence: 99%

Mitotic Modulation of Translation Elongation Factor 1 Leads to Hindered tRNA Delivery to Ribosomes

Sivan¹,

Aviner²,

Elroy‐Stein

2011

Journal of Biological Chemistry

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Translation elongation in eukaryotes is mediated by the concerted actions of elongation factor 1A (eEF1A), which delivers aminoacylated tRNA to the ribosome; elongation factor 1B (eEF1B) complex, which catalyzes the exchange of GDP to GTP on eEF1A; and eEF2, which facilitates ribosomal translocation. Here we present evidence in support of a novel mode of translation regulation by hindered tRNA delivery during mitosis. A conserved consensus phosphorylation site for the mitotic cyclin-dependent kinase 1 on the catalytic delta subunit of eEF1B (termed eEF1D) is required for its posttranslational modification during mitosis, resulting in lower affinity to its substrate eEF1A. This modification is correlated with reduced availability of eEF1A⅐tRNA complexes, as well as reduced delivery of tRNA to and association of eEF1A with elongating ribosomes. This mode of regulation by hindered tRNA delivery, although first discovered in mitosis, may represent a more globally applicable mechanism employed under other physiological conditions that involve down-regulation of protein synthesis at the elongation level.

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The Elongation factor-1δ (EF-1δ) originates from gene duplication of an EF-1β ancestor and fusion with a protein-binding domain

Cited by 11 publications

References 24 publications

Sea urchin elongation factor 1? (EF1?) and evidence for cell cycle-directed localization changes of a sub-fraction of the protein at M phase

Sea urchin elongation factor 1? (EF1?) and evidence for cell cycle-directed localization changes of a sub-fraction of the protein at M phase

Mutation of a conserved CDK site converts a metazoan Elongation Factor 1Bβ subunit into a replacement for yeast eEF1Bα

Mitotic Modulation of Translation Elongation Factor 1 Leads to Hindered tRNA Delivery to Ribosomes

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