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

Takashi Ohtsuki, Aya Sato, Yoh ichi Watanabe, Kimitsuna Watanabe

Research output: Contribution to journalArticle

38 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)669-673
Number of pages5
JournalNature Structural Biology
Volume9
Issue number9
DOIs
Publication statusPublished - Sep 2002
Externally publishedYes

Fingerprint

Peptide Elongation Factor Tu
Mitochondria
Transfer RNA
Serine
Animals
Ribosomes
Amino Acids

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

A unique serine-specific elongation factor Tu found in nematode mitochondria. / Ohtsuki, Takashi; Sato, Aya; Watanabe, Yoh ichi; Watanabe, Kimitsuna.

In: Nature Structural Biology, Vol. 9, No. 9, 09.2002, p. 669-673.

Research output: Contribution to journalArticle

Ohtsuki, Takashi ; Sato, Aya ; Watanabe, Yoh ichi ; Watanabe, Kimitsuna. / A unique serine-specific elongation factor Tu found in nematode mitochondria. In: Nature Structural Biology. 2002 ; Vol. 9, No. 9. pp. 669-673.
@article{803bea795717421394f06b7270d6e473,
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.",
author = "Takashi Ohtsuki and Aya Sato and Watanabe, {Yoh ichi} and Kimitsuna Watanabe",
year = "2002",
month = "9",
doi = "10.1038/nsb826",
language = "English",
volume = "9",
pages = "669--673",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "Nature Publishing Group",
number = "9",

}

TY - JOUR

T1 - A unique serine-specific elongation factor Tu found in nematode mitochondria

AU - Ohtsuki, Takashi

AU - Sato, Aya

AU - Watanabe, Yoh ichi

AU - Watanabe, Kimitsuna

PY - 2002/9

Y1 - 2002/9

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0036725278&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036725278&partnerID=8YFLogxK

U2 - 10.1038/nsb826

DO - 10.1038/nsb826

M3 - Article

VL - 9

SP - 669

EP - 673

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 9

ER -