A bacterial elongation factor G homologue exclusively functions in ribosome recycling in the spirochaete Borrelia burgdorferi

Takuma Suematsu, Shin Ichi Yokobori, Hiroyuki Morita, Shigeo Yoshinari, Takuya Ueda, Kiyoshi Kita, Nono Takeuchi, Yoh Ichi Watanabe

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Translation elongation factor G (EF-G) in bacteria plays two distinct roles in different phases of the translation system. EF-G catalyses the translocation of tRNAs on the ribosome in the elongation step, as well as the dissociation of the post-termination state ribosome into two subunits in the recycling step. In contrast to this conventional view, it has very recently been demonstrated that the dual functions of bacterial EF-G are distributed over two different EF-G paralogues in human mitochondria. In the present study, we show that the same division of roles of EF-G is also found in bacteria. Two EF-G paralogues are found in the spirochaete Borrelia burgdorferi, EF-G1 and EF-G2. We demonstrate that EF-G1 is a translocase, while EF-G2 is an exclusive recycling factor. We further demonstrate that B. burgdorferi EF-G2 does not require GTP hydrolysis for ribosome disassembly, provided that translation initiation factor 3 (IF-3) is present in the reaction. These results indicate that two B. burgdorferi EF-G paralogues are close relatives to mitochondrial EF-G paralogues rather than the conventional bacterial EF-G, in both their phylogenetic and biochemical features.

Original languageEnglish
Pages (from-to)1445-1454
Number of pages10
JournalMolecular Microbiology
Volume75
Issue number6
DOIs
Publication statusPublished - 2010 Mar

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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