Nuclear and nucleolar targeting of human ribosomal protein S25: Common features shared with HIV-1 regulatory proteins

Satoshi Kubota, Terry D. Copeland, Roger J. Pomerantz

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

The nuclear and nucleolar targeting properties of human ribosomal protein S25 (RPS25) were analysed by the expression of epitope-tagged RPS25 cDNAs in Cos-1 cells. The tagged RPS25 was localized to the cell nucleus with a strong predominance in the nucleolus. At the amino terminus of RPS25, two stretches of highly basic residues juxtapose. This configuration shares common features with the nucleolar targeting signals (NOS) of lentiviral RNA-binding transactivators, including human immunodeficiencg viruses' (HIV) Rev proteins. Deletion and site-directed mutational analyses demonstrated that the first NOS-like stretch is dispensable for both nuclear and nucleolar localization of RPS25, and that the nuclear targeting signal is located within the second NOS-like stretch. It has also been suggested that a set of continuous basic residues and the total number of basic residues should be required for nucleolar targeting. Signal-mediated nuclear/nucleolar targeting was further characterized by the construction and expression of a variety of chimeric constructs, utilizing three different backbones with RPS25 cDNA fragments. Immunofluorescence analyses demonstrated a 17 residue peptide of RPS25 as a potential nuclear/nucleolar targeting signal. The identified peptide signal may belong to a putative subclass of NOS, characterized by compact structure, together with lentiviral RNA-binding transactivators.

Original languageEnglish
Pages (from-to)1503-1514
Number of pages12
JournalOncogene
Volume18
Issue number7
DOIs
Publication statusPublished - Feb 18 1999
Externally publishedYes

Keywords

  • HIV-1
  • Nuclear targeting
  • Protein
  • Rev
  • Ribosome

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cancer Research

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