Mutational analysis of human prothymosin α reveals a bipartite nuclear localization signal

Yuri P. Rubtsov, Andrei S. Zolotukhin, Ivan A. Vorobjev, Nina V. Chichkova, Nickolay A. Pavlov, Elena M. Karger, Alexandra G. Evstafieva, Barbara K. Felber, Andrey B. Vartapetian

Research output: Contribution to journalArticlepeer-review

38 Citations (Scopus)


Mutants of human prothymosin a with impaired ability to inhibit yeast Saccharomyces cerevisiae. cerevisiae cell growth were characterized. Two types of prothymosin α-inactivating mutations were observed. Mutations that belong to the first type compromised the nuclear entry of prothymosin α by affecting its nuclear localization signal. Analysis of subcellular distribution of GFP-prothymosin α 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 α through an unknown mechanism, without influencing the nuclear import of the protein.

Original languageEnglish
Pages (from-to)135-141
Number of pages7
JournalFEBS Letters
Issue number1
Publication statusPublished - Aug 11 1997


  • Cell growth inhibition
  • Nuclear localization signal
  • PCR-based mutagenesis
  • Prothymosin α
  • Saccharomyces cerevisiae

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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