Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 23, Issue 9, Pages 3237-3246Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.23.9.3237-3246.2003
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Funding
- NCI NIH HHS [CA82481, R01 CA082481] Funding Source: Medline
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Telomerase, the enzyme that elongates telomeres, is essential to maintain telomere length and to immortalize most cancer cells. However, little is known about the regulation of this enzyme in higher eukaryotes. We previously described a domain in the hTERT telomerase catalytic subunit that is essential for telomere elongation and cell immortalization in vivo but dispensable for catalytic activity in vitro. Here, we show that fusions of hTERT containing different mutations in this domain to the telomere binding protein hTRF2 redirected the mutated hTERT to telomeres and rescued its in vivo functions. We suggest that this domain posttranscriptionally regulates telomerase function by targeting the enzyme, to telomeres.
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