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Published online 8 January 2001. doi:10.1083/jcb.152.1.157
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© The Rockefeller University Press, 0021-9525/2001/1/157/ $5.00
The Journal of Cell Biology, Volume 152, Number 1, January 8, 2001 157-164

Original Article

The Telomerase/Vault-associated Protein TEP1 Is Required for Vault RNA Stability and Its Association with the Vault Particle

Valerie A. Kickhoefera, Yie Liuc, Lawrence B. Kongb, Bryan E. Snowc, Phoebe L. Stewartb, Lea Harringtonc, and Leonard H. Romea
a Department of Biological Chemistry and Jonsson Comprehensive Cancer Center, Crump Institute for Molecular Imaging, University of California at Los Angeles, School of Medicine, Los Angeles, California 90095
b Department of Molecular and Medical Pharmacology, Crump Institute for Molecular Imaging, University of California at Los Angeles, School of Medicine, Los Angeles, California 90095
c Ontario Cancer Institute/Amgen Institute, Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2C1, Canada

Correspondence to: Valerie A. Kickhoefer, Department of Biological Chemistry, UCLA School of Medicine and Jonsson Comprehensive Cancer Center, Los Angeles, CA 90095-1737. Tel:(310) 794-4873 Fax:(310) 206-5272 E-mail:vkick{at}mednet.ucla.edu.

Vaults and telomerase are ribonucleoprotein (RNP) particles that share a common protein subunit, TEP1. Although its role in either complex has not yet been defined, TEP1 has been shown to interact with the mouse telomerase RNA and with several of the human vault RNAs in a yeast three-hybrid assay. An mTep1-/- mouse was previously generated which resulted in no apparent change in telomere length or telomerase activity in six generations of mTep1-deficient mice. Here we show that the levels of the telomerase RNA and its association with the telomerase RNP are also unaffected in mTep1-/- mice. Although vaults purified from the livers of mTep1-/- mice appear structurally intact by both negative stain and cryoelectron microscopy, three-dimensional reconstruction of the mTep1-/- vault revealed less density in the cap than previously observed for the intact rat vault. Furthermore, the absence of TEP1 completely disrupted the stable association of the vault RNA with the purified vault particle and also resulted in a decrease in the levels and stability of the vault RNA. Therefore, we have uncovered a novel role for TEP1 in vivo as an integral vault protein important for the stabilization and recruitment of the vault RNA to the vault particle.

Key Words: TEP1, vaults, mouse embryonic stem cells, RNA stability, cryo-EM


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