TY - JOUR
T1 - Nucleolin interacts with telomerase
AU - Khurts, Shilagardi
AU - Masutomi, Kenkichi
AU - Delgermaa, Luvsanjav
AU - Arai, Kuniaki
AU - Oishi, Naoki
AU - Mizuno, Hideki
AU - Hayashi, Naoyuki
AU - Hahn, William C.
AU - Murakami, Seishi
PY - 2004/12/3
Y1 - 2004/12/3
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M407643200
DO - 10.1074/jbc.M407643200
M3 - Article
C2 - 15371412
AN - SCOPUS:10944266466
SN - 0021-9258
VL - 279
SP - 51508
EP - 51515
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 49
ER -