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First published online 3 June 2008
doi: 10.1242/jcs.024091

Journal of Cell Science 121, 2169-2176 (2008)
Published by The Company of Biologists 2008
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Research Article

Nucleolar localization of TERT is unrelated to telomerase function in human cells

Jian Lin*, Rui Jin*, Bin Zhang*, Hao Chen*, Yun Xiu Bai, Ping Xun Yang, Su Wen Han, Yao Hua Xie, Pei Tang Huang, Cuifen Huang and Jun Jian Huang{ddagger}

Laboratory of Tumor and Molecular Biology, Beijing Institute of Biotechnology, 27 Taiping Road, Beijing, People's Republic of China

{ddagger} Author for correspondence (e-mail: huangjun_j{at}yahoo.com)

Accepted 18 February 2008

Telomerase maintains telomere length and has been implicated in both aging and carcinogenesis of human cells. This enzyme is a specialized ribonucleoprotein (RNP) complex, minimally consisting of two essential components: the protein catalytic subunit TERT (telomerase reverse transcriptase) and the integral RNA moiety TR (telomerase RNA, TERC). Both TERT and TR have been found to localize to nucleoli within the nucleus, leading to the suggestion of nucleoli as the site for telomerase RNP biogenesis in human cells. However, whether this statement is true or not has not yet been convincingly demonstrated. Here, we identify that residues 965-981 of the human TERT polypeptide constitute an active nucleolar-targeting signal (NTS) essential for mediating human TERT nucleolar localization. Mutational inactivation of this NTS completely disrupted TERT nucleolar translocation in both normal and malignant human cells. Most interestingly, such a TERT mutant still retained the capacity to activate telomerase activity, maintain telomere length and extend the life-span of cellular proliferation, as does wild-type TERT, in BJ cells (normal fibroblasts). Therefore, our data suggest that TERT nucleolar localization is unrelated to telomerase function in human cells.

Key words: Nucleolus, TERT, NTS, Localization, Telomerase


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