Nucleolin interacts with telomerase

Shilagardi Khurts, Kenkichi Masutomi, Luvsanjav Delgermaa, Kuniaki Arai, Naoki Oishi, Hideki Mizuno, Naoyuki Hayashi, William C. Hahn, Seishi Murakami

Research output: Contribution to journalArticlepeer-review

94 Scopus citations


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 compartiments 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 carbosyl-terminal RGG domain, and this binding also involves the telomerase RNA subwait 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.

Original languageEnglish (US)
Pages (from-to)51508-51515
Number of pages8
JournalJournal of Biological Chemistry
Issue number49
StatePublished - Dec 3 2004
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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