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Nucleic Acids Research Advance Access published online on November 28, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn925
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Rex1p deficiency leads to accumulation of precursor initiator tRNAMet and polyadenylation of substrate RNAs in Saccharomyces Cerevisiae

Sarah G. Ozanick1, Xuying Wang1, Michael Costanzo2, Renee L. Brost2, Charles Boone2 and James T. Anderson1,*

1Department of Biological Sciences, Marquette University, Milwaukee, WI, USA and 2Banting and Best Department of Medical Research and the Department of Molecular Genetics, Donnelly CCBR, University of Toronto, Toronto, Canada

*To whom correspondence should be addressed. Tel: +1 414 288 1481; Fax: +1 414 288 7357; Email: james.anderson{at}mu.edu

Received August 5, 2008. Revised October 1, 2008. Accepted November 3, 2008.

A synthetic genetic array was used to identify lethal and slow-growth phenotypes produced when a mutation in TRM6, which encodes a tRNA modification enzyme subunit, was combined with the deletion of any non-essential gene in Saccharomyces cerevisiae. We found that deletion of the REX1 gene resulted in a slow-growth phenotype in the trm6-504 strain. Previously, REX1 was shown to be involved in processing the 3' ends of 5S rRNA and the dimeric tRNAArg-tRNAAsp. In this study, we have discovered a requirement for Rex1p in processing the 3' end of tRNAiMet precursors and show that precursor tRNAiMet accumulates in a trm6-504 rex1{Delta} strain. Loss of Rex1p results in polyadenylation of its substrates, including tRNAiMet, suggesting that defects in 3' end processing can activate the nuclear surveillance pathway. Finally, purified Rex1p displays Mg2+-dependent ribonuclease activity in vitro, and the enzyme is inactivated by mutation of two highly conserved amino acids.


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