ArticleNucleic acids research2017
Amino acid substrates impose polyamine, eIF5A, or hypusine requirement for peptide synthesis.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.
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Who cites it
34 citing papers in PubMed, 1 synthesis or guideline pooled it, 54 citations in OpenAlex.
- Gut microbiota bridges dietary nutrients and host immunity.Science China. Life sciences · 2023Pooled it
- Ribosome dynamics at the conserved PGP motif governs 2A peptide-bond-skipping efficiency.Nucleic acids research · 2026Article
- ARID1A deficiency-driven reprogramming of polyamine metabolism promotes endometrial cancer malignancy and immune escape.Cell death & disease · 2026Article
- Prognostic, oncogenic roles, and pharmacogenomic features of AMD1 in hepatocellular carcinoma.Cancer cell international · 2024Article
- AMD1 promotes breast cancer aggressiveness via a spermidine-eIF5A hypusination-TCF4 axis.Breast cancer research : BCR · 2024Article
- CLPP-Null Eukaryotes with Excess Heme Biosynthesis Show Reduced L-arginine Levels, Probably via CLPX-Mediated OAT Activation.Biomolecules · 2024Article
- Manipulation of DHPS activity affects dendritic morphology and expression of synaptic proteins in primary rat cortical neurons.Frontiers in cellular neuroscience · 2024Article
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- eEF2 diphthamide modification restrains spurious frameshifting to maintain translational fidelity.Nucleic acids research · 2023Article
- Post-translational formation of hypusine in eIF5A: implications in human neurodevelopment.Amino acids · 2022Review
- Genome-wide RNAi screen identifies novel players in human 60S subunit biogenesis including key enzymes of polyamine metabolism.Nucleic acids research · 2022Article
- Polyamine import and accumulation causes immunomodulation in macrophages engulfing apoptotic cells.Cell reports · 2022Article
- Bracovirus Sneaks Into Apoptotic Bodies Transmitting Immunosuppressive Signaling Driven by Integration-Mediated eIF5A Hypusination.Frontiers in immunology · 2022Article
- The progress of protein synthesis factors eIFs, eEFs and eRFs in inflammatory bowel disease and colorectal cancer pathogenesis.Frontiers in oncology · 2022Review
- The eukaryotic initiation factor 5A (eIF5A1), the molecule, mechanisms and recent insights into the pathophysiological roles.Cell & bioscience · 2021Review
- Translational autoregulation of the S. cerevisiae high-affinity polyamine transporter Hol1.Molecular cell · 2021Article
- Article
- Spermidine supplementation in rare translation-associated disorders.Cell stress · 2021Article
- Eukaryotic translation factor eIF5A contributes to acetic acid tolerance in Saccharomyces cerevisiae via transcriptional factor Ume6p.Biotechnology for biofuels · 2021Article
- Impaired eIF5A function causes a Mendelian disorder that is partially rescued in model systems by spermidine.Nature communications · 2021Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Whereas ribosomes efficiently catalyze peptide bond synthesis by most amino acids, the imino acid proline is a poor substrate for protein synthesis. Previous studies have shown that the translation factor eIF5A and its bacterial ortholog EF-P bind in the E site of the ribosome where they contact the peptidyl-tRNA in the P site and play a critical role in promoting the synthesis of polyproline peptides. Using misacylated Pro-tRNAPhe and Phe-tRNAPro, we show that the imino acid proline and not tRNAPro imposes the primary eIF5A requirement for polyproline synthesis. Though most proline analogs require eIF5A for efficient peptide synthesis, azetidine-2-caboxylic acid, a more flexible four-membered ring derivative of proline, shows relaxed eIF5A dependency, indicating that the structural rigidity of proline might contribute to the requirement for eIF5A. Finally, we examine the interplay between eIF5A and polyamines in promoting translation elongation. We show that eIF5A can obviate the polyamine requirement for general translation elongation, and that this activity is independent of the conserved hypusine modification on eIF5A. Thus, we propose that the body of eIF5A functionally substitutes for polyamines to promote general protein synthesis and that the hypusine modification on eIF5A is critically important for poor substrates like proline.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.