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Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances

tRNA-dependent addition of amino acids to lipids on the outer surface of the bacterial membrane results in decreased effectiveness of antimicrobials such as cationic antimicrobial peptides (CAMPs) that target the membrane, and increased virulence of several pathogenic species. After a brief introduc...

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Detalles Bibliográficos
Autores principales: Fields, Rachel N., Roy, Hervé
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6103681/
https://www.ncbi.nlm.nih.gov/pubmed/28816600
http://dx.doi.org/10.1080/15476286.2017.1356980
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author Fields, Rachel N.
Roy, Hervé
author_facet Fields, Rachel N.
Roy, Hervé
author_sort Fields, Rachel N.
collection PubMed
description tRNA-dependent addition of amino acids to lipids on the outer surface of the bacterial membrane results in decreased effectiveness of antimicrobials such as cationic antimicrobial peptides (CAMPs) that target the membrane, and increased virulence of several pathogenic species. After a brief introduction to CAMPs and the various bacterial resistance mechanisms used to counteract these compounds, this review focuses on recent advances in tRNA-dependent pathways for lipid modification in bacteria. Phenotypes associated with amino acid lipid modifications and regulation of their expression will also be discussed.
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spelling pubmed-61036812018-08-24 Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances Fields, Rachel N. Roy, Hervé RNA Biol Review - Solicited tRNA-dependent addition of amino acids to lipids on the outer surface of the bacterial membrane results in decreased effectiveness of antimicrobials such as cationic antimicrobial peptides (CAMPs) that target the membrane, and increased virulence of several pathogenic species. After a brief introduction to CAMPs and the various bacterial resistance mechanisms used to counteract these compounds, this review focuses on recent advances in tRNA-dependent pathways for lipid modification in bacteria. Phenotypes associated with amino acid lipid modifications and regulation of their expression will also be discussed. Taylor & Francis 2017-11-03 /pmc/articles/PMC6103681/ /pubmed/28816600 http://dx.doi.org/10.1080/15476286.2017.1356980 Text en © 2018 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.
spellingShingle Review - Solicited
Fields, Rachel N.
Roy, Hervé
Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances
title Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances
title_full Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances
title_fullStr Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances
title_full_unstemmed Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances
title_short Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances
title_sort deciphering the trna-dependent lipid aminoacylation systems in bacteria: novel components and structural advances
topic Review - Solicited
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6103681/
https://www.ncbi.nlm.nih.gov/pubmed/28816600
http://dx.doi.org/10.1080/15476286.2017.1356980
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