Molecular cloning of bovine eIF5A and deoxyhypusine synthase cDNA

DNA Seq. 2004 Feb;15(1):26-32. doi: 10.1080/10425170310001652174.

Abstract

Deoxyhypusine synthase is the first of the two enzymes that catalyzes the maturation of eukaryotic initiation factor 5A (eIF5A). The mature eIF5A is the only known protein in eukaryotic cells that contains the unusual amino acid hypusine (N(epsilon)-(4-amino-2(R)-hydroxybutyl)-lysine). Synthesis of hypusine is essential for the function of eIF5A in eukaryotic cell proliferation and survival. Here we describe the cloning and characterization of bovine eIF5A and bovine deoxyhypusine synthase. The deduced bovine eIF5A protein is 100% identical to human eIF5A-1, and the deduced bovine deoxyhypusine synthase protein showed a 93% identity to the human protein.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cattle
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Eukaryotic Translation Initiation Factor 5A
  • Humans
  • Male
  • Molecular Sequence Data
  • Oxidoreductases Acting on CH-NH Group Donors / genetics*
  • Peptide Initiation Factors / genetics*
  • RNA-Binding Proteins / genetics*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Testis / enzymology

Substances

  • DNA, Complementary
  • Peptide Initiation Factors
  • RNA-Binding Proteins
  • Oxidoreductases Acting on CH-NH Group Donors
  • deoxyhypusine synthase