Literature Review

DHPS



eIF5A

eIF5A interacts in a hypusine-dependent manner with a molecular complex and plays an important role in translation of mRNA to protein.

  • Mutational analyses of human eIF5A-1: identification of amino acid residues critical for eIF5A activity and hypusine modification. (PMID: 18067580,(ncbi.nlm.nih.gov)) Cano V.S.P. … Park M.H. FEBS J. 2008 22 64
    • K47D and G49A were effective substrates for deoxyhypusine synthase, yet failed to support growth, suggesting critical roles of Lys47 and Gly49 in eIF5A activity. This research supports that eIF5A plays a central role in translation.
  • The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A). (PMID: 16452303,(ncbi.nlm.nih.gov)) Park M.H. J. Biochem. 2006 3 2264
    • Deoxyhypusine hydroxylase is a HEAT-repeat protein with a symmetrical superhelical structure consisting of 8 helical hairpins. It contains tightly bound iron coordination sites of four His-Glu pairs at the active sites. The structural fold of deoxyhypusine hydroxylase is entirely different from those of the other known protein hydroxylases.
  • Tandem affinity purification revealed the hypusine-dependent binding of eukaryotic initiation factor 5A to the translating 80S ribosomal complex. (PMID: 16215987,(ncbi.nlm.nih.gov)) Jao D.L. … Chen K.Y.J. Cell. Biochem. 2006 22 64
    • The physiological function of eIF5A was determined via tandem affinity purification. Researchers discovered that eIF5A interacts in a hypusine-dependent manner with a molecular complex rather than a single protein.
  • Identification and characterization of eukaryotic initiation factor 5A-2. (PMID: 14622290,(ncbi.nlm.nih.gov)) Clement P.M.J. … Johansson H.E. Eur. J. Biochem. 2003 3 22 64
    • eIF5A is the only known cellular protein to contain hypusine, which is necessary for sustained cell proliferation. This paper describes eIF5A-2 protein in human cell lines. Since there are differences in gene expression in different cell lines, there are tissue-specific functions of the eIF5A-2 isoform.
  • Subcellular localization of the hypusine-containing eukaryotic initiation factor 5A by immunofluorescent staining and green fluorescent protein tagging. (PMID: 12210765,(ncbi.nlm.nih.gov)) Jao D.L. … Yu Chen K. J. Cell. Biochem. 2002 22 64
    • This study shows that eIF-5A enters the nucleus via passive diffusion.
  • Hypusine is required for a sequence-specific interaction of eukaryotic initiation factor 5A with postsystematic evolution of ligands by exponential enrichment RNA. (PMID: 11060315,(ncbi.nlm.nih.gov)) Xu A. … Chen K.Y. J. Biol. Chem. 2001 22 64
    • The eIF-5A-RNA interaction depends physiologically on hypusine and the core motif of the target RNA.
  • Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 A resolution. (PMID: 9753699,(ncbi.nlm.nih.gov)) Peat T.S. … Terwilliger T.C. Structure 1998 22 64
    • This study shows that the lysine that is post-translationally modified by deoxyhypusine synthase is freely solvent accessible and suggests that IF-5A is involved in RNA binding.
  • Structural features of the eIF-5A precursor required for posttranslational synthesis of deoxyhypusine. (PMID: 7929297,(ncbi.nlm.nih.gov)) Joe Y.A. … Park M.H. J. Biol. Chem. 1994 3 22 64
    • This study defines the minimum domain of the eIF-5A precursor protein required for enzymatic deoxyhypusine synthesis as Phe30-Asp80.
  • PCR-based cloning of the full-length Neurospora eukaryotic initiation factor 5A cDNA: polyhistidine-tagging and overexpression for protein affinity binding. (PMID: 8093005,(ncbi.nlm.nih.gov)) Tao Y. … Chen K.Y. Biochem. J. 1994 22 64
    • A simple PCR-based strategy was developed to obtain a full-length cDNA of Neurospora crassa eIF-5A using a one-step affinity-column chromatography.
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