title: A unique serine-specific elongation factor Tu found in nematode mitochondria.
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.
authors.affiliation: Department of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Chiba, Japan.
authors.forename: Takashi
authors.initials: T
authors.lastname: Ohtsuki
authors.forename: Aya
authors.initials: A
authors.lastname: Sato
authors.forename: Yoh-ichi
authors.initials: Y
authors.lastname: Watanabe
authors.forename: Kimitsuna
authors.initials: K
authors.lastname: Watanabe
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017173:Caenorhabditis elegans / Q000378:metabolism*; D018076:DNA, Complementary; D008928:Mitochondria / Q000378:metabolism*; D008969:Molecular Sequence Data; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012694:Serine / Q000378:metabolism*
chemical_list: D018076:DNA, Complementary; D012346:RNA, Transfer, Amino Acyl; D012694:Serine; D010444:Peptide Elongation Factor Tu