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A more recent version of this article appeared on September 1, 2002
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Submitted on April 18, 2002
Revised on June 10, 2002
Accepted on June 20, 2002
1 Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis-Jewish General Hospital, Montréal, Québec, H3T 1E2, Canada; and Department of Anatomy and Cell Biology, McGill University, Montréal, Québec, H3A 2B2
2 Bloomfield Centre for Research in Aging, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis-Jewish General Hospital, Montréal, Québec, H3T 1E2, Canada; and Terry Fox Molecular Oncology Group and Departments of Oncology, Medecine, and Microbiology and Immunology, McGill University, Montréal, Québec, Canada
* Corresponding author. E-mail address: chantal.autexier{at}mcgill.ca.
Telomerase is a ribonucleoprotein (RNP) complex that is minimally composed of a protein catalytic subunit, the telomerase reverse transcriptase (TERT), and an RNA component, the telomerase RNA (TR). The survival of motor neuron (SMN) gene codes for a protein involved in the biogenesis of certain RNPs. Here we report that SMN is a telomerase-associated protein. Using in vitro binding assays and immunoprecipitation experiments, we demonstrate an association between SMN and the telomerase RNP in vitro and in human cells. The specific immunopurification of SMN from human 293 cells copurified telomerase activity, suggesting that SMN associates with a subset of the functional telomerase holoenzyme. Our results also indicate that the human TR and the human TERT are not associated with Sm proteins, in contrast to Saccharomyces cerevisiae telomerase. Immunofluorescence analysis showed that hTERT does not specifically colocalize with wild-type SMN in gems or Cajal bodies. However, a dominant-negative mutant of SMN (SMN
N27) previously characterized to elicit the cellular reorganization of small nuclear RNPs caused the accumulation of hTERT in specific SMNN27-induced cellular bodies. Furthermore, coexpression of SMNN27 and hTERT in rabbit reticulocyte lysates decreased the efficiency of human telomerase reconstitution in vitro. Our results establish SMN as a novel telomerase-associated protein that is likely to function in human telomerase biogenesis.
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