Elongation factor-P at the crossroads of the host-endosymbiont interface
Elongation factor P (EF-P) is an ancient bacterial translational factor that aids the ribosome in polymerizing oligo-prolines. EF-P structurally resembles tRNA and binds in-between the exit and peptidyl sites of the ribosome to accelerate the intrinsically slow rea...
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2015-09-01
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doaj-abfa713107df47399a2e12dcabe293ca2020-11-24T23:03:33ZengShared Science Publishers OGMicrobial Cell2311-26382015-09-0121036036210.15698/mic2015.10.232123455678Elongation factor-P at the crossroads of the host-endosymbiont interfaceAndrei Rajkovic0Anne Witzky1William Navarre2Andrew J. Darwin3Michael Ibba4Molecular, Cellular and Developmental Biology Program, Ohio State University, Columbus, Ohio, USA.Department of Molecular Genetics, Ohio State University, Columbus, Ohio, USA.Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.Department of Microbiology, New York University School of Medicine, New York, New York, USA.Department of Microbiology and Center for RNA Biology, Ohio State University, Columbus, Ohio, USA.Elongation factor P (EF-P) is an ancient bacterial translational factor that aids the ribosome in polymerizing oligo-prolines. EF-P structurally resembles tRNA and binds in-between the exit and peptidyl sites of the ribosome to accelerate the intrinsically slow reaction of peptidyl-prolyl bond formation. Recent studies have identified in separate organisms, two evolutionarily convergent EF-P posttranslational modification systems (EPMS), split predominantly between gammaproteobacteria, and betaproteobacteria. In both cases EF-P receives a post-translational modification, critical for its function, on a highly conserved residue that protrudes into the peptidyl-transfer center of the ribosome. EPMSs are comprised of a gene(s) that synthesizes the precursor molecule used in modifying EF-P, and a gene(s) encoding an enzyme that reacts with the precursor molecule to catalyze covalent attachment to EF-P. However, not all organisms genetically encode a complete EPMS. For instance, some symbiotic bacteria harbor efp and the corresponding gene that enzymatically attaches the modification, but lack the ability to synthesize the substrate used in the modification reaction. Here we highlight the recent discoveries made regarding EPMSs, with a focus on how these incomplete modification pathways shape or have been shaped by the endosymbiont-host relationship.http://microbialcell.com/researcharticles/elongation-factor-p-at-the-crossroads-of-the-host-endosymbiont-interface/elongation factor-Prhamnosylationmodificationtranslation |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Andrei Rajkovic Anne Witzky William Navarre Andrew J. Darwin Michael Ibba |
spellingShingle |
Andrei Rajkovic Anne Witzky William Navarre Andrew J. Darwin Michael Ibba Elongation factor-P at the crossroads of the host-endosymbiont interface Microbial Cell elongation factor-P rhamnosylation modification translation |
author_facet |
Andrei Rajkovic Anne Witzky William Navarre Andrew J. Darwin Michael Ibba |
author_sort |
Andrei Rajkovic |
title |
Elongation factor-P at the crossroads of the host-endosymbiont interface |
title_short |
Elongation factor-P at the crossroads of the host-endosymbiont interface |
title_full |
Elongation factor-P at the crossroads of the host-endosymbiont interface |
title_fullStr |
Elongation factor-P at the crossroads of the host-endosymbiont interface |
title_full_unstemmed |
Elongation factor-P at the crossroads of the host-endosymbiont interface |
title_sort |
elongation factor-p at the crossroads of the host-endosymbiont interface |
publisher |
Shared Science Publishers OG |
series |
Microbial Cell |
issn |
2311-2638 |
publishDate |
2015-09-01 |
description |
Elongation factor P (EF-P) is an ancient bacterial translational factor that aids the ribosome in polymerizing oligo-prolines. EF-P structurally resembles tRNA and binds in-between the exit and peptidyl sites of the ribosome to accelerate the intrinsically slow reaction of peptidyl-prolyl bond formation. Recent studies have identified in separate organisms, two evolutionarily convergent EF-P posttranslational modification systems (EPMS), split predominantly between gammaproteobacteria, and betaproteobacteria. In both cases EF-P receives a post-translational modification, critical for its function, on a highly conserved residue that protrudes into the peptidyl-transfer center of the ribosome. EPMSs are comprised of a gene(s) that synthesizes the precursor molecule used in modifying EF-P, and a gene(s) encoding an enzyme that reacts with the precursor molecule to catalyze covalent attachment to EF-P. However, not all organisms genetically encode a complete EPMS. For instance, some symbiotic bacteria harbor efp and the corresponding gene that enzymatically attaches the modification, but lack the ability to synthesize the substrate used in the modification reaction. Here we highlight the recent discoveries made regarding EPMSs, with a focus on how these incomplete modification pathways shape or have been shaped by the endosymbiont-host relationship. |
topic |
elongation factor-P rhamnosylation modification translation |
url |
http://microbialcell.com/researcharticles/elongation-factor-p-at-the-crossroads-of-the-host-endosymbiont-interface/ |
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