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Nucleic Acids Research 2004 32(18):5464-5470; doi:10.1093/nar/gkh886
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Published online 11 October 2004

Nucleic Acids Research, Vol. 32 No. 18 © Oxford University Press 2004; all rights reserved

Interaction of mitochondrial initiation factor 2 with mitochondrial fMet-tRNA

Angela C. Spencer and Linda L. Spremulli*

Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3290, USA

* To whom correspondence should be addressed. Tel: +1 919 966 1567; Fax: +1 919 966 3675; Email: Linda_Spremulli{at}unc.edu

Received July 22, 2004; Revised and Accepted September 23, 2004

The mammalian mitochondrial genome contains a single tRNAMet gene that gives rise to the initiator and elongator tRNAMet. It is generally believed that mitochondrial protein synthesis begins with formylmethionyl-tRNA, which indicates that the formylation of mitochondrial Met-tRNA specifies its participation in initiation through its interaction with initiation factor 2 (IF-2). However, recent studies in yeast mitochondria, suggest that formylation is not required for protein synthesis. In addition, bovine IF-2mt could replace yeast IF-2mt in strains that lack fMet-tRNA which suggests that this paradigm may extend to mammalian mitochondria. Here, the importance of the formylation of mitochondrial Met-tRNA for the interaction with IF-2mt was investigated by measuring the ability of bovine IF-2mt to bind mitochondrial fMet-tRNA. In direct binding experiments, bovine IF-2mt has a 25-fold greater affinity for mitochondrial fMet-tRNA than Met-tRNA, using either the native mitochondrial tRNAMet or an in vitro transcript of bovine mitochondrial tRNAMet. In addition, IF-2mt will not effectively stimulate mitochondrial Met-tRNA binding to mitochondrial ribosomes, exhibiting a 50-fold preference for fMet-tRNA over Met-tRNA in this assay. Finally, the region of IF-2mt responsible for the interaction with fMet-tRNA was mapped to the C2 sub-domain of domain VI of this factor.


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