2. Author's Information
    Seung Bum Lee
    Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, U.S.A.

    Jong Hwan Park
    Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, U.S.A.

    John E. Folk
    Chemical Biology Research Branch, National Institute of Drug Abuse and National Institute on Alcohol Abuse and Alcoholism, National Institutes of Health, Bethesda, MD 20892, U.S.A.

    Jason A. Deck
    Chemical Biology Research Branch, National Institute of Drug Abuse and National Institute on Alcohol Abuse and Alcoholism, National Institutes of Health, Bethesda, MD 20892, U.S.A.

    Anthony E. Pegg
    Department of Cellular and Molecular Physiology, Milton S. Hershey Medical Center, Pennsylvania State University, Hershey, PA 17033, U.S.A.

    Masaaki Sokabe
    Department of Biochemistry and Molecular Medicine, University of California, Davis, CA 95616, U.S.A.

    Christopher S. Fraser
    Department of Molecular and Cellular Biology, University of California, Davis, CA 95616, U.S.A.

    Myung Hee Park
    Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, U.S.A.
  3. Abstract
    eIF5A (eukaryotic translation initiation factor 5A) is the only cellular protein containing hypusine [Nϵ-(4-amino-2-hydroxybutyl)lysine]. eIF5A is activated by the post-translational synthesis of hypusine and the hypusine modification is essential for cell proliferation. In the present study, we report selective acetylation of the hypusine and/or deoxyhypusine residue of eIF5A by a key polyamine catabolic enzyme SSAT1 (spermidine/spermine-N1-acetyltransferase 1). This enzyme normally catalyses the N1-acetylation of spermine and spermidine to form acetyl-derivatives, which in turn are degraded to lower polyamines. Although SSAT1 has been reported to exert other effects in cells by its interaction with other cellular proteins, eIF5A is the first target protein specifically acetylated by SSAT1. Hypusine or deoxyhypusine, as the free amino acid, does not act as a substrate for SSAT1, suggesting a macromolecular interaction between eIF5A and SSAT1. Indeed, the binding of eIF5A and SSAT1 was confirmed by pull-down assays. The effect of the acetylation of hypusine on eIF5A activity was assessed by comparison of acetylated with non-acetylated bovine testis eIF5A in the methionyl-puromycin synthesis assay. The loss of eIF5A activity by this SSAT1-mediated acetylation confirms the strict structural requirement for the hypusine side chain and suggests a possible regulation of eIF5A by hypusine acetylation/deacetylation.
    Keywords
    acetylation, eukaryotic translation initiation factor 5A (eIF5A), hypusine, polyamine metabolism, post-translational modification, spermidine/spermine-N1-acetyltransferase 1 (SSAT1)
    DOI: 10.1042/BJ20101322
    ADLID: 27272-v4
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  1. Keywords
    acetylation eukaryotic translation initiation factor 5A (eIF5A) hypusine polyamine metabolism post-translational modification spermidine/spermine-N1-acetyltransferase 1 (SSAT1)
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