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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2017
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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. |
format | Online Article Text |
id | pubmed-6103681 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
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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