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M201227200v1
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Papers In Press, published online ahead of print April 15, 2002
J. Biol. Chem, 10.1074/jbc.M201227200
Submitted on February 6, 2002
Revised on April 15, 2002
Accepted on April 15, 2002

The nucleolar localization domain of the catalytic subunit of human telomerase

Katherine T. Etheridge, Soma S.R. Banik, Blaine N. Armbruster, Yusheng Zhu, Rebecca M. Terns, Michael P. Terns, and Christopher M. Counter

Department of Pharmacology and Cancer Biology, DUMC, Durham, NC 27710

Corresponding Author: count004{at}mc.duke.edu

Telomerase is the enzyme essential to complete the replication of the terminal DNA of most eukaryotic chromosomes. In humans, this enzyme is composed of a reverse transcriptase (hTERT) and a telomerase RNA (hTR) subunit. The hTR has been found in the nucleolus, a site of assembly of ribosomes as well as other ribonucleoproteins (RNPs). We therefore tested whether the hTERT component is also found in the nucleolus, where it could complex with the hTR RNA to form a functional enzyme. We report that hTERT does indeed localize to the nucleolus, and mapped the domain responsible for this localization to the hTR-binding region of the protein by deletion analysis. Substitution mutations in two of the three conserved hTR-binding domains in this nucleolar localization domain (NoLD) abolished nucleolar localization. However, another mutation that impeded hTR binding did not alter this subcellular localization. Additionally, wildtype hTERT was detected in the nucleolus of cells that fail to express hTR. Taken together, we propose that the nucleolar localization of hTERT involves more than just the association with the hTR subunit. Furthermore, the coincidental targetting of both the hTR and hTERT subunits to the nucleolus supports the premise that the assembly of telomerase occurs in the nucleolus.


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