© 2007 The Author(s).
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RESEARCH PAPER |
Dual targeting of the tRNA nucleotidyltransferase in plants: not just the signal
1LMU München, VW-Research group, Department of Biology I, Menzinger Str. 67, D-80638 München, Germany
2Department of Biology and Centre for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke St W., Montréal, Québec, Canada H4B 1R6
3Department of Chemistry and Biochemistry, Concordia University, 7141 Sherbrooke St W., Montréal, Québec Canada H4B 1R6
* To whom correspondence should be addressed. E-mail: joycep{at}alcor.concordia.ca
Enzymes involved in tRNA maturation are essential for cytosolic, mitochondrial, and plastid protein synthesis and are therefore localized to these different compartments of the cell. Interestingly, only one isoform of tRNA nucleotidyltransferase (responsible for adding the 3'-terminal cytidine–cytidine–adenosine to tRNAs) has been identified in plants. The present study therefore explored how signals contained on this enzyme allow it to be distributed among the different cell compartments. It is demonstrated that the N-terminal portion of the protein acts as an organellar targeting signal and that differential use of multiple in-frame start codons alters the localization of the protein. Moreover, it is shown that the mature domain has a major impact on the distribution of the protein within the cell. These data indicate that regulation of dual localization involves not only specific N-terminal signals, but also additional factors within the protein or the cell.
Key words: Dual targeting, plant protein distribution, targeting signal, tRNA nucleotidyltransferase
Received 14 August 2007; Revised 26 September 2007 Accepted 27 September 2007
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