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J. Biol. Chem., Vol. 277, Issue 27, 24764-24770, July 5, 2002
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From the Telomerase is the enzyme essential to complete
the replication of the terminal DNA of most eukaryotic chromosomes. In
humans, this enzyme is composed of the telomerase reverse transcriptase (hTERT) and telomerase RNA (hTR) subunits. 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 here that hTERT does
indeed localize to the nucleolus, and we 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, wild type hTERT
was detected in the nucleolus of cells that failed 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 targeting of both the hTR and hTERT
subunits to the nucleolus supports the premise that the assembly of
telomerase occurs in the nucleolus.
Departments of Pharmacology and
Cancer Biology and Radiation Oncology, Duke University Medical Center,
Durham, North Carolina 27710 and the § Department of
Biochemistry and Molecular Biology, University of Georgia,
Athens, Georgia 30602
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