Duplication of Drosophila melanogaster mitochondrial EF-Tu

Pre-adaptation to T-arm truncation and exclusion of bulky aminoacyl residues

Aya Sato, Takuma Suematsu, Koh Ki Aihara, Kiyoshi Kita, Tsutomu Suzuki, Kimitsuna Watanabe, Takashi Ohtsuki, Yoh Ichi Watanabe

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Translation elongation factor Tu (EF-Tu) delivers aminoacyl-tRNA (aa-tRNA) to ribosomes in protein synthesis. EF-Tu generally recognizes aminoacyl moieties and acceptor- and T-stems of aa-tRNAs. However, nematode mitochondrial (mt) tRNAs frequently lack all or part of the T-arm that is recognized by canonical EF-Tu. We previously reported that two distinct EF-Tu species, EF-Tu1 and EF-Tu2, respectively, recognize mt tRNAs lacking T-arms and D-arms in the mitochondria of the chromadorean nematode Caenorhabditis elegans. C. elegans EF-Tu2 specifically recognizes the seryl moiety of serylated D-armless tRNAs. Mitochondria of the enoplean nematode Trichinella possess three structural types of tRNAs: T-armless tRNAs, D-armless tRNAs, and cloverleaf tRNAs with a short T-arm. Trichinella mt EF-Tu1 binds to all three types and EF-Tu2 binds only to D-armless Ser-tRNAs, showing an evolutionary intermediate state from canonical EF-Tu to chromadorean nematode (e.g. C. elegans) EF-Tu species. We report here that two EF-Tu species also participate in Drosophila melanogaster mitochondria. Both D. melanogaster EF-Tu1 and EF-Tu2 bound to cloverleaf and D-armless tRNAs. D. melanogaster EF-Tu1 has the ability to recognize T-armless tRNAs that do not evidently exist in D. melanogaster mitochondria, but do exist in related arthropod species. In addition, D. melanogaster EF-Tu2 preferentially bound to aatRNAs carrying small amino acids, but not to aa-tRNAs carrying bulky amino acids. These results suggest that the Drosophila mt translation system could be another intermediate state between the canonical and nematode mitochondria-type translation systems.

Original languageEnglish
Pages (from-to)957-969
Number of pages13
JournalBiochemical Journal
Volume474
Issue number6
DOIs
Publication statusPublished - Mar 15 2017

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Peptide Elongation Factor Tu
Transfer RNA
Drosophila melanogaster
Mitochondria
Caenorhabditis elegans
Trichinella
RNA, Transfer, Ser
Amino Acids
Arthropods
Ribosomes
Drosophila

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Duplication of Drosophila melanogaster mitochondrial EF-Tu : Pre-adaptation to T-arm truncation and exclusion of bulky aminoacyl residues. / Sato, Aya; Suematsu, Takuma; Aihara, Koh Ki; Kita, Kiyoshi; Suzuki, Tsutomu; Watanabe, Kimitsuna; Ohtsuki, Takashi; Watanabe, Yoh Ichi.

In: Biochemical Journal, Vol. 474, No. 6, 15.03.2017, p. 957-969.

Research output: Contribution to journalArticle

Sato, Aya ; Suematsu, Takuma ; Aihara, Koh Ki ; Kita, Kiyoshi ; Suzuki, Tsutomu ; Watanabe, Kimitsuna ; Ohtsuki, Takashi ; Watanabe, Yoh Ichi. / Duplication of Drosophila melanogaster mitochondrial EF-Tu : Pre-adaptation to T-arm truncation and exclusion of bulky aminoacyl residues. In: Biochemical Journal. 2017 ; Vol. 474, No. 6. pp. 957-969.
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