Telomerase plays a crucial role in telomere maintenance in vivo. To underst
and telomerase regulation,we have been characterizing components of the enz
yme. 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 e
xtracts, 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 w
ith each other or with telomerase-associated protein 1. Both hStau and L22
are more abundant than TERT. This, together with their localization, sugges
ts that they may be associated with other ribonucleoprotein complexes in ce
lls. We propose that these two hTR-associated proteins may play a role in h
TR processing, telomerase assembly, or localization in vivo.