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Open Access Research article

The TROVE module: A common element in Telomerase, Ro and Vault ribonucleoproteins

Alex Bateman1* and Valerie Kickhoefer2

Author Affiliations

1 The Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SA, UK

2 Department of Biological Chemistry and the Jonsson Comprehensive Cancer Center, The David Geffen School of Medicine, University of California, Los Angeles, California 90095-1737, USA

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BMC Bioinformatics 2003, 4:49  doi:10.1186/1471-2105-4-49

Published: 16 October 2003



Ribonucleoproteins carry out a variety of important tasks in the cell. In this study we show that a number of these contain a novel module, that we speculate mediates RNA-binding.


The TROVE module – Telomerase, Ro and Vault module – is found in TEP1 and Ro60 the protein components of three ribonucleoprotein particles. This novel module, consisting of one or more domains, may be involved in binding the RNA components of the three RNPs, which are telomerase RNA, Y RNA and vault RNA. A second conserved region in these proteins is shown to be a member of the vWA domain family. The vWA domain in TEP1 is closely related to the previously recognised vWA domain in VPARP a second component of the vault particle. This vWA domain may mediate interactions between these vault components or bind as yet unidentified components of the RNPs.


This work suggests that a number of ribonucleoprotein components use a common RNA-binding module. The TROVE module is also found in bacterial ribonucleoproteins suggesting an ancient origin for these ribonucleoproteins.

Y RNA; vRNA; telomerase RNA; VPARP; TEP1; Ro60