An evolutionary 'intermediate state' of mitochondrial translation systems found in Trichinella species of parasitic nematodes: co-evolution of tRNA and EF-Tu

Nucleic Acids Res. 2006;34(18):5291-9. doi: 10.1093/nar/gkl526. Epub 2006 Sep 29.

Abstract

EF-Tu delivers aminoacyl-tRNAs to ribosomes in the translation system. However, unusual truncations found in some animal mitochondrial tRNAs seem to prevent recognition by a canonical EF-Tu. We showed previously that the chromadorean nematode has two distinct EF-Tus, one of which (EF-Tu1) binds only to T-armless aminoacyl-tRNAs and the other (EF-Tu2) binds to D-armless Ser-tRNAs. Neither of the EF-Tus can bind to canonical cloverleaf tRNAs. In this study, by analyzing the translation system of enoplean nematode Trichinella species, we address how EF-Tus and tRNAs have evolved from the canonical structures toward those of the chromadorean translation system. Trichinella mitochondria possess three types of tRNAs: cloverleaf tRNAs, which do not exist in chromadorean nematode mitochondria; T-armless tRNAs; and D-armless tRNAs. We found two mitochondrial EF-Tu species, EF-Tu1 and EF-Tu2, in Trichinella britovi. T.britovi EF-Tu2 could bind to only D-armless Ser-tRNA, as Caenorhabditis elegans EF-Tu2 does. In contrast to the case of C.elegans EF-Tu1, however, T.britovi EF-Tu1 bound to all three types of tRNA present in Trichinella mitochondria. These results suggest that Trichinella mitochondrial translation system, and particularly the tRNA-binding specificity of EF-Tu1, could be an intermediate state between the canonical system and the chromadorean nematode mitochondrial system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Caenorhabditis elegans Proteins / chemistry
  • Evolution, Molecular*
  • Helminth Proteins / chemistry
  • Helminth Proteins / metabolism
  • Mitochondria / genetics*
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Peptide Elongation Factor Tu / chemistry*
  • Peptide Elongation Factor Tu / metabolism
  • Protein Biosynthesis*
  • RNA / chemistry
  • RNA / metabolism
  • RNA, Helminth / chemistry
  • RNA, Helminth / metabolism
  • RNA, Mitochondrial
  • RNA, Transfer / chemistry*
  • RNA, Transfer / metabolism
  • RNA, Transfer, Ala / chemistry
  • RNA, Transfer, Ala / metabolism
  • RNA, Transfer, Ser / chemistry
  • RNA, Transfer, Ser / metabolism
  • RNA, Transfer, Trp / chemistry
  • RNA, Transfer, Trp / metabolism
  • Sequence Alignment
  • Trichinella / genetics*

Substances

  • Caenorhabditis elegans Proteins
  • Helminth Proteins
  • RNA, Helminth
  • RNA, Mitochondrial
  • RNA, Transfer, Ala
  • RNA, Transfer, Ser
  • RNA, Transfer, Trp
  • RNA
  • RNA, Transfer
  • Peptide Elongation Factor Tu