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A unique serine-specific elongation factor Tu found in nematode mitochondria

A Corrigendum to this article was published on 01 August 2003

Abstract

The translation elongation factor Tu (EF-Tu) delivers aminoacyl-tRNAs to ribosomes by recognizing the tRNA acceptor and T stems. However, the unusual truncation observed in some animal mitochondrial tRNAs seems to prevent recognition by a canonical EF-Tu. For instance, nematode mitochondria contain tRNAs lacking a T or D arm. We recently found an atypical EF-Tu (EF-Tu1) specific for nematode mitochondrial tRNAs that lack the T arm. We have now discovered a second factor, EF-Tu2, which binds only to tRNAs that lack a D arm. EF-Tu2 seems unique in its amino acid specificity because it recognizes the aminoacyl moiety of seryl-tRNAs and the tRNA structure itself. Such EF-Tu evolution might explain tRNA structural divergence in animal mitochondria.

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Figure 1: Unique features of C. elegans EF-Tu amino acid sequences.
Figure 2: tRNA binding specificity of EF-Tu1, EF-Tu2 and the canonical EF-Tu species.
Figure 3: Serine specificity of EF-Tu2.
Figure 4: Schematic depiction of the co-evolution of nematode mt tRNA and EF-Tu from entities possessing the canonical structure.

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Acknowledgements

We thank A. Coulson (Sanger Centre, UK) for the cDNA clone, K. Kita (University of Tokyo) for A. suum and T. Hanada for E. coli AlaRS. Supported by Grants-in-Aid from the Ministry of Education, Science, Sports and Culture, Japan (to K.W.) and Grant-in-Aid for Encouragement of Young Scientists (to T.O.).

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Correspondence to Kimitsuna Watanabe.

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Ohtsuki, T., Sato, A., Watanabe, Yi. et al. A unique serine-specific elongation factor Tu found in nematode mitochondria. Nat Struct Mol Biol 9, 669–673 (2002). https://doi.org/10.1038/nsb826

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