Chaperone properties of mammalian mitochondrial translation elongation factor Tu

Hiroaki Suzuki, Takuya Ueda, Hideki Taguchi, Nono Takeuchi*


研究成果: Article査読

58 被引用数 (Scopus)


The main function of the prokaryotic translation elongation factor Tu (EF-Tu) and its eukaryotic counterpart eEF1A is to deliver aminoacyl-tRNA to the A-site on the ribosome. In addition to this primary function, it has been reported that EF-Tu from various sources has chaperone activity. At present, little information is available about the chaperone activity of mitochondrial EF-Tu. In the present study, we have examined the chaperone function of mammalian mitochondrial EF-Tu (EF-Tumt). We demonstrate that recombinant EF-Tumt prevents thermal aggregation of proteins and enhances protein refolding in vitro and that this EF-Tumt chaperone activity proceeds in a GTP-independent manner. We also demonstrate that, under heat stress, the newly synthesized peptides from the mitochondrial ribosome specifically co-immunoprecipitate with EF-Tumt and are destabilized in EF-Tumt-overexpressing cells. We show that most of the EF-Tumt localizes on the mitochondrial inner membrane where most mitochondrial ribosomes are found. We discuss the possible role of EF-Tumt chaperone activity in protein quality control in mitochondria, with regard to the recently reported in vivo chaperone function of eEF1A.

ジャーナルJournal of Biological Chemistry
出版ステータスPublished - 2007 1月 9

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 細胞生物学


「Chaperone properties of mammalian mitochondrial translation elongation factor Tu」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。