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Vol. 11, Issue 3, 999-1010, March 2000
and
*Department of Molecular Biology and Genetics, The Johns Hopkins
University School of Medicine, Baltimore, Maryland 21205; and
Telomerase plays a crucial role in telomere maintenance in vivo. To
understand telomerase regulation, we have been characterizing components of the enzyme. To date several components of the mammalian telomerase holoenzyme have been identified: the essential RNA component
(human telomerase RNA [hTR]), the catalytic subunit human
telomerase reverse transcriptase (hTERT), and telomerase-associated protein 1. Here we describe the identification of two new
proteins that interact with hTR: hStau and L22. Antisera against both
proteins immunoprecipitated hTR, hTERT, and telomerase activity from
cell extracts, suggesting that the proteins are associated with
telomerase. Both proteins localized to the nucleolus and cytoplasm.
Although these proteins are associated with telomerase, we found no
evidence of their association with each other or with
telomerase-associated protein 1. Both hStau and L22 are more abundant
than TERT. This, together with their localization, suggests that they
may be associated with other ribonucleoprotein complexes in
cells. We propose that these two hTR-associated proteins may play a
role in hTR processing, telomerase assembly, or localization in vivo.
Department of Biochemistry and Cell Biology, State
University of New York, Stony Brook, New York 11794
Corresponding author. E-mail address:
cgreider{at}jhmi.edu.
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