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J Biol Chem, Vol. 274, Issue 46, 32712-32717, November 12, 1999
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From the Vaults are large cytoplasmic ribonucleoprotein
complexes of undetermined function. Mammalian vaults have two high
molecular mass proteins of 193 and 240 kDa. We have identified a
partial cDNA encoding the 240-kDa vault protein and determined it
is identical to the mammalian telomerase-associated component, TEP1.
TEP1 is the mammalian homolog of the Tetrahymena p80
telomerase protein and has been shown to interact specifically with
mammalian telomerase RNA and the catalytic protein subunit hTERT. We
show that while TEP1 is a component of the vault particle, vaults have
no detectable telomerase activity. Using a yeast three-hybrid assay we
demonstrate that several of the human vRNAs interact in a
sequence-specific manner with TEP1. The presence of 16 WD40 repeats in
the carboxyl terminus of the TEP1 protein is a convenient number for
this protein to serve a structural or organizing role in the vault, a
particle with eight-fold symmetry. The sharing of the TEP1 protein
between vaults and telomerase suggests that TEP1 may play a common role in some aspect of ribonucleoprotein structure, function, or assembly.
Department of Biological Chemistry, UCLA
School of Medicine and Jonsson Comprehensive Cancer Center, Los
Angeles, California 90095, the ¶ Ontario Cancer Institute-Amgen
Institute, Department of Medical Biophysics, University of Toronto,
Toronto, Ontario M5G 2C1, Canada, and Amgen, Inc.,
Thousand Oaks, California 91320
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