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Mutational Analysis of Human Prothymosin Alpha Reveals a Bipartite Nuclear Localization Signal

  1. Author:
    Rubtsov, Y. P.
    Zolotukhin, A. S.
    Vorobjev, I. A.
    Chichkova, N. V.
    Pavlov, N. A.
    Karger, E. M.
    Evstafieva, A. G.
    Felber, B. K.
    Vartapetian, A. B.
  2. Author Address

    Vartapetian AB MOSCOW MV LOMONOSOV STATE UNIV BELOZERSKY INST PHYSICOCHEM BIOL MOSCOW 119899 RUSSIA MOSCOW MV LOMONOSOV STATE UNIV BELOZERSKY INST PHYSICOCHEM BIOL MOSCOW 119899 RUSSIA NCI FREDERICK CANC RES & DEV CTR ABL BASIC RES PROGRAM FREDERICK, MD 21701 USA
    1. Year: 1997
  1. Journal: Febs Letters
    1. 413
    2. 1
    3. Pages: 135-141
  2. Type of Article: Article
  1. Abstract:

    Mutants of human prothymosin alpha with impaired ability to inhibit yeast Saccharomyces cerevisiae. cerevisiae cell growth were characterized, Two types of prothymosin alpha-inactivating mutations were observed, Mutations that belong to the first type compromised the nuclear entry of prothymosin alpha by affecting its nuclear localization signal. Analysis of subcellular distribution of GFP-prothymosin alpha fusions revealed a bipartite nuclear localization signal that is both necessary and sufficient for nuclear import of the protein in human cells, Mutations of the second type abrogated the inhibitory action of prothymosin alpha through an unknown mechanism, without influencing the nuclear import of the protein. (C) 1997 Federation of European Biochemical Societies. [References: 34]

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