ArticleThe Journal of biological chemistry2007
Specificity of the deoxyhypusine hydroxylase-eukaryotic translation initiation factor (eIF5A) interaction: identification of amino acid residues of the enzyme required for binding of its substrate, deoxyhypusine-containing eIF5A.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- Brazilin attenuates methylglyoxal‑induced endothelial injury by enhancing eIF5A hypusination and inhibiting the AMPK/mTOR‑mediated autophagy/apoptosis axisInternational journal of molecular medicine · 2026Article
- PtoeIF5A1: A Pleiotropic Regulator of Development, PCD, and Salt Tolerance inPlants (Basel, Switzerland) · 2026Article
- Post-translational formation of hypusine in eIF5A: implications in human neurodevelopment.Amino acids · 2022Review
- The Molecular and Physiological Effects of Protein-Derived Polyamines in the Intestine.Nutrients · 2020Review
- Recent insights into eukaryotic translation initiation factors 5A1 and 5A2 and their roles in human health and disease.Cancer cell international · 2020Review
- PhDHS Is Involved in Chloroplast Development in Petunia.Frontiers in plant science · 2019Article
- Hypusine, a polyamine-derived amino acid critical for eukaryotic translation.The Journal of biological chemistry · 2018Review
- Posttranslational hypusination of the eukaryotic translation initiation factor-5A regulates Fusarium graminearum virulence.Scientific reports · 2016Article
- A novel mouse model for inhibition of DOHH-mediated hypusine modification reveals a crucial function in embryonic development, proliferation and oncogenic transformation.Disease models & mechanisms · 2014Article
- Article
- Assay of deoxyhypusine hydroxylase activity.Methods in molecular biology (Clifton, N.J.) · 2011Article
- Evidence for conformational changes in the yeast deoxyhypusine hydroxylase Lia1 upon iron displacement from its active site.Amino acids · 2010Article
- Inhibition of HIV-1 gene expression by Ciclopirox and Deferiprone, drugs that prevent hypusination of eukaryotic initiation factor 5A.Retrovirology · 2009Article
- The Drosophila deoxyhypusine hydroxylase homologue nero and its target eIF5A are required for cell growth and the regulation of autophagy.The Journal of cell biology · 2009Article
- Mutational analyses of human eIF5A-1--identification of amino acid residues critical for eIF5A activity and hypusine modification.The FEBS journal · 2008Article
- Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modification.Amino acids · 2007Review
- The hypusine-containing translation factor eIF5A.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Deoxyhypusine hydroxylase (DOHH) is a novel metalloenzyme that catalyzes the final step of the post-translational synthesis of hypusine (Nepsilon-(4-amino-2-hydroxybutyl)lysine) in the eukaryotic translation initiation factor 5A (eIF5A). Hypusine synthesis is unique in that it occurs in only one protein, denoting the strict specificity of the modification enzymes toward the substrate protein. The specificity of the interaction between eIF5A and DOHH was investigated using human eIF5A (eIF5A-1 isoform) and human recombinant DOHH. DOHH displayed a strong preference for binding the deoxyhypusine-containing form of eIF5A, over the eIF5A precursor or the hypusine-containing eIF5A, indicating a role for the deoxyhypusine residue in binding. In addition to the deoxyhypusine residue, a large portion of the eIF5A polypeptide (>20-90 amino acids) is required for effective modification by DOHH. We have identified the amino acid residues of DOHH that are critical for substrate binding by alanine substitution of 36 conserved amino acid residues. Of these, alanine substitution at Glu57, Glu90, Glu208, Glu241, Gly63, or Gly214 caused a severe impairment in eIF5A(Dhp) binding, with a complete loss of binding and activity in the E57A and E208A mutant enzymes. Only aspartate substitution mutants, E57D or E208D, retained partial activity and substrate binding, whereas alanine, glutamine, or asparagine mutants did not. These findings support a proposed model of DOHH-eIF5A binding in which the amino group(s) of the deoxyhypusine side chain of the substrate is primarily anchored by gamma-carboxyl groups of Glu57 and Glu208 at the DOHH active site.
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