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

16 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 Jan 1
Externally publishedYes

Fingerprint

Peptide Elongation Factor G
Spirochaetales
Borrelia burgdorferi
Ribosomes
Recycling
Prokaryotic Initiation Factor-3
Bacteria
Transfer RNA
Guanosine Triphosphate
Mitochondria
Hydrolysis

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

A bacterial elongation factor G homologue exclusively functions in ribosome recycling in the spirochaete Borrelia burgdorferi. / Suematsu, Takuma; Yokobori, Shin Ichi; Morita, Hiroyuki; Yoshinari, Shigeo; Ueda, Takuya; Kita, Kiyoshi; Takeuchi, Nono; Watanabe, Yoh Ichi.

In: Molecular Microbiology, Vol. 75, No. 6, 01.01.2010, p. 1445-1454.

Research output: Contribution to journalArticle

Suematsu, T, Yokobori, SI, Morita, H, Yoshinari, S, Ueda, T, Kita, K, Takeuchi, N & Watanabe, YI 2010, 'A bacterial elongation factor G homologue exclusively functions in ribosome recycling in the spirochaete Borrelia burgdorferi', Molecular Microbiology, vol. 75, no. 6, pp. 1445-1454. https://doi.org/10.1111/j.1365-2958.2010.07067.x
Suematsu, Takuma ; Yokobori, Shin Ichi ; Morita, Hiroyuki ; Yoshinari, Shigeo ; Ueda, Takuya ; Kita, Kiyoshi ; Takeuchi, Nono ; Watanabe, Yoh Ichi. / A bacterial elongation factor G homologue exclusively functions in ribosome recycling in the spirochaete Borrelia burgdorferi. In: Molecular Microbiology. 2010 ; Vol. 75, No. 6. pp. 1445-1454.
@article{37530c0269f344c2ba772de822d974ab,
title = "A bacterial elongation factor G homologue exclusively functions in ribosome recycling in the spirochaete Borrelia burgdorferi",
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.",
author = "Takuma Suematsu and Yokobori, {Shin Ichi} and Hiroyuki Morita and Shigeo Yoshinari and Takuya Ueda and Kiyoshi Kita and Nono Takeuchi and Watanabe, {Yoh Ichi}",
year = "2010",
month = "1",
day = "1",
doi = "10.1111/j.1365-2958.2010.07067.x",
language = "English",
volume = "75",
pages = "1445--1454",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley-Blackwell",
number = "6",

}

TY - JOUR

T1 - A bacterial elongation factor G homologue exclusively functions in ribosome recycling in the spirochaete Borrelia burgdorferi

AU - Suematsu, Takuma

AU - Yokobori, Shin Ichi

AU - Morita, Hiroyuki

AU - Yoshinari, Shigeo

AU - Ueda, Takuya

AU - Kita, Kiyoshi

AU - Takeuchi, Nono

AU - Watanabe, Yoh Ichi

PY - 2010/1/1

Y1 - 2010/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=77949404662&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77949404662&partnerID=8YFLogxK

U2 - 10.1111/j.1365-2958.2010.07067.x

DO - 10.1111/j.1365-2958.2010.07067.x

M3 - Article

C2 - 20132446

AN - SCOPUS:77949404662

VL - 75

SP - 1445

EP - 1454

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 6

ER -