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

Molecular Microbiology
Takuma SuematsuYoh-ichi Watanabe

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.

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Citations

Nov 26, 2010·Molecular Biology and Evolution·Gemma C Atkinson, Sandra L Baldauf
Nov 22, 2013·PloS One·Stephanie O PalmerJames M Bullard
Nov 12, 2013·Molecular and Biochemical Parasitology·Ankit GuptaSaman Habib
Nov 26, 2013·Journal of Biochemistry·Takuma SuematsuYoh-ichi Watanabe
Mar 6, 2012·The EMBO Journal·Takeshi YokoyamaRajendra K Agrawal
Aug 5, 2015·BMC Genomics·Libia Catalina Salinas CastellanosJorge Hernández-Torres
Aug 17, 2016·Trends in Parasitology·Saman HabibKirti Gupta
Dec 2, 2010·Biochemical Society Transactions·Ricarda RichterZofia M A Chrzanowska-Lightowlers
Jun 16, 2021·Nature Communications·Ravi Kiran KoripellaRajendra K Agrawal

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