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Nucleolin interacts with telomerase.

Telomerase is a specialized reverse transcriptase composed of core RNA and protein subunits which plays essential roles in maintaining telomeres in actively dividing cells. Recent work indicates that telomerase shuttles between subcellular compartments during assembly and in response to specific stimuli. In particular, telomerase colocalizes with nucleoli in normal human fibroblasts. Here, we show that nucleolin, a major nucleolar phosphoprotein, interacts with telomerase and alters its subcellular localization. Nucleolin binds the human telomerase reverse transcriptase subunit (hTERT) through interactions with its RNA binding domain 4 and carboxyl-terminal RGG domain, and this binding also involves the telomerase RNA subunit hTERC. The protein-protein interaction between nucleolin and hTERT is critical for the nucleolar localization of hTERT. These findings indicate that interaction of hTERT and nucleolin participates in the dynamic intracellular localization of telomerase complex.

Pubmed ID: 15371412


  • Khurts S
  • Masutomi K
  • Delgermaa L
  • Arai K
  • Oishi N
  • Mizuno H
  • Hayashi N
  • Hahn WC
  • Murakami S


The Journal of biological chemistry

Publication Data

December 3, 2004

Associated Grants

  • Agency: NCI NIH HHS, Id: K01 CA94223

Mesh Terms

  • Catalytic Domain
  • Cell Line
  • Cell Line, Tumor
  • Cell Nucleolus
  • Cell Nucleus
  • DNA-Binding Proteins
  • Fibroblasts
  • Glutathione Transferase
  • Green Fluorescent Proteins
  • Humans
  • Immunoprecipitation
  • Microscopy, Confocal
  • Microscopy, Fluorescence
  • Phosphoproteins
  • Plasmids
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA
  • RNA-Binding Proteins
  • Recombinant Fusion Proteins
  • Recombinant Proteins
  • Telomerase
  • Transfection