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Functional significance of eIF5A and its hypusine modification in eukaryotes Park MH; Nishimura K; Zanelli CF; Valentini SRAmino Acids 2010[Feb]; 38 (2): 491-500The unusual basic amino acid, hypusine [N(epsilon)-(4-amino-2-hydroxybutyl)-lysine], is a modified lysine with the addition of the 4-aminobutyl moiety from the polyamine spermidine. This naturally occurring amino acid is a product of a unique posttranslational modification that occurs in only one cellular protein, eukaryotic translation initiation factor 5A (eIF5A, eIF-5A). Hypusine is synthesized exclusively in this protein by two sequential enzymatic steps involving deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). The deoxyhypusine/hypusine synthetic pathway has evolved in archaea and eukaryotes, and eIF5A, DHS and DOHH are highly conserved suggesting a vital cellular function of eIF5A. Gene disruption and mutation studies in yeast and higher eukaryotes have provided valuable information on the essential nature of eIF5A and the deoxyhypusine/hypusine modification in cell growth and in protein synthesis. In view of the extraordinary specificity and functional significance of hypusine-containing eIF5A in mammalian cell proliferation, eIF5A and the hypusine biosynthetic enzymes are novel potential targets for intervention in aberrant cell proliferation.|Animals[MESH]|Bacteria/chemistry/genetics/metabolism[MESH]|Bacterial Proteins/chemistry/genetics/metabolism[MESH]|Eukaryota/chemistry/genetics/*metabolism[MESH]|Eukaryotic Translation Initiation Factor 5A[MESH]|Fungal Proteins/chemistry/genetics/metabolism[MESH]|Fungi/chemistry/genetics/metabolism[MESH]|Humans[MESH]|Lysine/*analogs & derivatives/metabolism[MESH]|Peptide Initiation Factors/chemistry/genetics/*metabolism[MESH]|Protein Structure, Secondary[MESH]|RNA-Binding Proteins/chemistry/genetics/*metabolism[MESH] |
