1. Human telomerase contains evolutionarily conserved catalytic and structural subunits
- Author
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Timothy McPhail, Wen Zhou, Murray O. Robinson, Michael Bass, David Yeung, Rena Oulton, Vernon Mar, and Lea Harrington
- Subjects
Telomerase ,Protein subunit ,Saccharomyces cerevisiae ,Molecular Sequence Data ,DNA-binding protein ,Catalysis ,Conserved sequence ,Evolution, Molecular ,Telomerase RNA component ,Research Communication ,Genetics ,Tumor Cells, Cultured ,Humans ,Amino Acid Sequence ,Peptide sequence ,Conserved Sequence ,Cell Nucleus ,Binding Sites ,biology ,Sequence Homology, Amino Acid ,Proteins ,RNA-Binding Proteins ,RNA-Directed DNA Polymerase ,biology.organism_classification ,Molecular biology ,Reverse transcriptase ,Cell biology ,DNA-Binding Proteins ,RNA ,Carrier Proteins ,Developmental Biology ,HeLa Cells - Abstract
We have cloned and characterized a human gene encoding TP2 (telomerase-associated protein2), a protein with similarity to reverse transcriptases and the catalytic telomerase subunits from Saccharomyces cerevisiae and Euplotes aediculatus. Indirect immunofluorescence revealed that TP2 was localized to the nucleus. Using antibodies to endogenous and epitope-tagged TP2, we found that TP2 was associated specifically with human telomerase activity and the recently identified telomerase-associated protein TP1. Mutation of conserved residues within the reverse transcriptase domain of TP2 severely reduced associated telomerase activity. These results suggest that telomerase is an evolutionarily conserved multisubunit complex composed of both structural and catalytic subunits.
- Published
- 1997