eIF5A and EF‐P: two unique translation factors are now traveling the same road

@article{Rossi2014eIF5AAE,  title={eIF5A and EF‐P: two unique translation factors are now traveling the same road},  author={Danuza Rossi and Reginaldo Massanobu Kuroshu and Cleslei Fernando Zanelli and Sandro Roberto Valentini},  journal={Wiley Interdisciplinary Reviews: RNA},  year={2014},  volume={5},  url={https://api.semanticscholar.org/CorpusID:25447826}}
The findings that eIF5A and EF‐P are important for specific cellular processes and play a role in the relief of ribosome stalling caused by specific amino acid sequences, such as those containing prolines reinforce the hypothesis that these factors are involved in specialized translation.

61 Citations

Elongation Factor P: New Mechanisms of Function and an Evolutionary Diversity of Translation Regulation

The general evolutionary variety of theEF-P in different organisms, the problems of the regulation provided by the EF-P, and its role in the sustainability of the protein balance in the cell in different physiological states are inspected.

EF-P Dependent Pauses Integrate Proximal and Distal Signals during Translation

The findings indicate that the ability of a given PPX motif to initiate an EF-P-alleviated stall is strongly influenced by its local context, and that other indirect post-transcriptional effects determine the influence of such stalls on protein levels within the cell.

Modification of translation factor aIF5A from Sulfolobus solfataricus

It is shown that aIF5A of the crenarchaeum Sulfolobus solfataricus is hypusinated and forms a stable complex with deoxyhypusine synthase, the first enzyme of the hypusination pathway.

Stall no more at polyproline stretches with the translation elongation factors EF‐P and IF‐5A

The function of EF‐P and IF‐5A is reviewed and their unusual posttranslational protein modifications are reviewed, which reduces not only bacterial fitness, but also impairs virulence.

Estudo das interações de eIF5A com a maquinaria de tradução e com o complexo Ribosome Quality Control, utilizando modelo de Saccharomyces cerevisiae

It was observed that eIF5A is important for the formation of cellular aggregates caused by polylysines, and a correlation between normal levels of eif5A in the cell and the presence of Sis1 e Cdc42 in the aggregates was shown, suggesting a possible functional interaction between e IF5A and the RQC complex.

Mapping surface residues of eIF5A that are important for binding to the ribosome using alanine scanning mutagenesis

Interactions of eIF5A with ribosomal protein L1 are more important to stabilize the interaction with the ribosome as a whole than the contacts with P-tRNA.

Evidence for a Negative Cooperativity between eIF5A and eEF2 on Binding to the Ribosome

Results suggest that binding of eEF2 to the ribosome alters its conformation, resulting in a weakened affinity of eIF5A and impairment of this interplay compromises cell growth due to translation elongation defects.

Genome-Wide Analyses and Functional Classification of Proline Repeat-Rich Proteins: Potential Role of eIF5A in Eukaryotic Evolution

The importance of proline repeat-rich proteins and a potential role for eIF5A and its hypusine modification pathway in the course of eukaryotic evolution are suggested.
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99 References

Predicting the pathway involved in post-translational modification of Elongation factor P in a subset of bacterial species

Two protein families of unknown function, encoded by yjeA and yjeK genes in E. coli, are identified as candidates for this missing pathway, based on the analysis of the structural and biochemical properties of both protein families, and proposed two potential mechanisms for the modification of EF-P.

Is there a role for eIF5A in translation?

The putative translation factor eIF5A is essential for cell viability and is highly conserved from archaebacteria to mammals and has also been implicated in nuclear export of HIV-1 Rev and mRNA decay, but these findings are controversial in the literature and may reflect secondary effects of eIF-5A function.

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Molecular genetic and biochemical studies are used to show that eIF5A promotes translation elongation, and suggest that it might function together with eEF2 to promote ribosomal translocation.

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Bacterial, archaeal, and eukaryotic cells have hundreds to thousands of polyproline-containing proteins of diverse function, suggesting that EF-P and a/eIF-5A are critical for copy-number adjustment of multiple pathways across all kingdoms of life.

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It is indicated that hypusine very likely is required for the vital in vivo function of eIF-5A and suggests a precise, essential role for the polyamine spermidine in cell metabolism.

eIF5A interacts functionally with eEF2

Results demonstrate that eIF5A is closely related to eEF2 function during translation elongation, and the polysome profile defect of the eif5AK56A mutant is largely corrected by high-copy eEF1.

(R)-β-Lysine-modified Elongation Factor P Functions in Translation Elongation*

Findings indicate that EF-P functions in translation elongation, a role critically dependent on post-translational β-lysylation but not hydroxylation.
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