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Nucleic Acids Research, 2001, Vol. 29, No. 11 2268-2275
© 2001 Oxford University Press

hnRNP A1 may interact simultaneously with telomeric DNA and the human telomerase RNA in vitro

Stéphan Fiset and Benoit Chabot*

Département de Microbiologie et d’Infectiologie, Faculté de Médecine, Université de Sherbrooke, Sherbrooke, Québec J1H 5N4, Canada

The hnRNP A1 protein and a shortened derivative (UP1) promote telomere elongation in mammalian cells. In support of a direct role for A1 in telomere biogenesis, we have shown that the recombinant UP1 protein binds to telomeric DNA sequences in vitro, and pulls down telomerase activity from a cell extract. Here we show that A1/UP1 can interact directly with the RNA component of human telomerase (hTR). A portion of A1/UP1 that contains RNA recognition motif 2 (RRM2) is sufficient for an interaction with the first 208 nt of hTR. Given that the portion of A1/UP1 that contains RRM1 is sufficient for binding to a telomeric DNA oligonucleotide, we have tested whether A1/UP1 can interact simultaneously with both nucleic acids. Using a chromatography assay, we find that A1/UP1 bound to hTR can interact with telomeric DNA. Notably, these interactions are sufficiently robust to withstand incubation in a cell extract. Our results suggest that hnRNP A1 may help recruit telomerase to the ends of chromosomes.

* To whom correspondence should be addressed. Tel: +1 819 564 5295; Fax: +1 819 564 5392; Email: b.chabot{at}courrier.usherb.ca Present address:Stéphan Fiset, Medicago Inc., 2480 rue Hochelaga, Sainte-Foy, Québec G1K 7P4, Canada


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