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Novel insights into biosynthesis and uptake of rhamnolipids and their precursors

The human pathogenic bacterium Pseudomonas aeruginosa produces rhamnolipids, glycolipids with functions for bacterial motility, biofilm formation, and uptake of hydrophobic substrates. Rhamnolipids represent a chemically heterogeneous group of secondary metabolites composed of one or two rhamnose mo...

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Autores principales: Wittgens, Andreas, Kovacic, Filip, Müller, Markus Michael, Gerlitzki, Melanie, Santiago-Schübel, Beatrix, Hofmann, Diana, Tiso, Till, Blank, Lars Mathias, Henkel, Marius, Hausmann, Rudolf, Syldatk, Christoph, Wilhelm, Susanne, Rosenau, Frank
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5352749/
https://www.ncbi.nlm.nih.gov/pubmed/27988798
http://dx.doi.org/10.1007/s00253-016-8041-3
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author Wittgens, Andreas
Kovacic, Filip
Müller, Markus Michael
Gerlitzki, Melanie
Santiago-Schübel, Beatrix
Hofmann, Diana
Tiso, Till
Blank, Lars Mathias
Henkel, Marius
Hausmann, Rudolf
Syldatk, Christoph
Wilhelm, Susanne
Rosenau, Frank
author_facet Wittgens, Andreas
Kovacic, Filip
Müller, Markus Michael
Gerlitzki, Melanie
Santiago-Schübel, Beatrix
Hofmann, Diana
Tiso, Till
Blank, Lars Mathias
Henkel, Marius
Hausmann, Rudolf
Syldatk, Christoph
Wilhelm, Susanne
Rosenau, Frank
author_sort Wittgens, Andreas
collection PubMed
description The human pathogenic bacterium Pseudomonas aeruginosa produces rhamnolipids, glycolipids with functions for bacterial motility, biofilm formation, and uptake of hydrophobic substrates. Rhamnolipids represent a chemically heterogeneous group of secondary metabolites composed of one or two rhamnose molecules linked to one or mostly two 3-hydroxyfatty acids of various chain lengths. The biosynthetic pathway involves rhamnosyltransferase I encoded by the rhlAB operon, which synthesizes 3-(3-hydroxyalkanoyloxy)alkanoic acids (HAAs) followed by their coupling to one rhamnose moiety. The resulting mono-rhamnolipids are converted to di-rhamnolipids in a third reaction catalyzed by the rhamnosyltransferase II RhlC. However, the mechanism behind the biosynthesis of rhamnolipids containing only a single fatty acid is still unknown. To understand the role of proteins involved in rhamnolipid biosynthesis the heterologous expression of rhl-genes in non-pathogenic Pseudomonas putida KT2440 strains was used in this study to circumvent the complex quorum sensing regulation in P. aeruginosa. Our results reveal that RhlA and RhlB are independently involved in rhamnolipid biosynthesis and not in the form of a RhlAB heterodimer complex as it has been previously postulated. Furthermore, we demonstrate that mono-rhamnolipids provided extracellularly as well as HAAs as their precursors are generally taken up into the cell and are subsequently converted to di-rhamnolipids by P. putida and the native host P. aeruginosa. Finally, our results throw light on the biosynthesis of rhamnolipids containing one fatty acid, which occurs by hydrolyzation of typical rhamnolipids containing two fatty acids, valuable for the production of designer rhamnolipids with desired physicochemical properties.
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spelling pubmed-53527492017-03-27 Novel insights into biosynthesis and uptake of rhamnolipids and their precursors Wittgens, Andreas Kovacic, Filip Müller, Markus Michael Gerlitzki, Melanie Santiago-Schübel, Beatrix Hofmann, Diana Tiso, Till Blank, Lars Mathias Henkel, Marius Hausmann, Rudolf Syldatk, Christoph Wilhelm, Susanne Rosenau, Frank Appl Microbiol Biotechnol Biotechnologically Relevant Enzymes and Proteins The human pathogenic bacterium Pseudomonas aeruginosa produces rhamnolipids, glycolipids with functions for bacterial motility, biofilm formation, and uptake of hydrophobic substrates. Rhamnolipids represent a chemically heterogeneous group of secondary metabolites composed of one or two rhamnose molecules linked to one or mostly two 3-hydroxyfatty acids of various chain lengths. The biosynthetic pathway involves rhamnosyltransferase I encoded by the rhlAB operon, which synthesizes 3-(3-hydroxyalkanoyloxy)alkanoic acids (HAAs) followed by their coupling to one rhamnose moiety. The resulting mono-rhamnolipids are converted to di-rhamnolipids in a third reaction catalyzed by the rhamnosyltransferase II RhlC. However, the mechanism behind the biosynthesis of rhamnolipids containing only a single fatty acid is still unknown. To understand the role of proteins involved in rhamnolipid biosynthesis the heterologous expression of rhl-genes in non-pathogenic Pseudomonas putida KT2440 strains was used in this study to circumvent the complex quorum sensing regulation in P. aeruginosa. Our results reveal that RhlA and RhlB are independently involved in rhamnolipid biosynthesis and not in the form of a RhlAB heterodimer complex as it has been previously postulated. Furthermore, we demonstrate that mono-rhamnolipids provided extracellularly as well as HAAs as their precursors are generally taken up into the cell and are subsequently converted to di-rhamnolipids by P. putida and the native host P. aeruginosa. Finally, our results throw light on the biosynthesis of rhamnolipids containing one fatty acid, which occurs by hydrolyzation of typical rhamnolipids containing two fatty acids, valuable for the production of designer rhamnolipids with desired physicochemical properties. Springer Berlin Heidelberg 2016-12-17 2017 /pmc/articles/PMC5352749/ /pubmed/27988798 http://dx.doi.org/10.1007/s00253-016-8041-3 Text en © The Author(s) 2016 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Biotechnologically Relevant Enzymes and Proteins
Wittgens, Andreas
Kovacic, Filip
Müller, Markus Michael
Gerlitzki, Melanie
Santiago-Schübel, Beatrix
Hofmann, Diana
Tiso, Till
Blank, Lars Mathias
Henkel, Marius
Hausmann, Rudolf
Syldatk, Christoph
Wilhelm, Susanne
Rosenau, Frank
Novel insights into biosynthesis and uptake of rhamnolipids and their precursors
title Novel insights into biosynthesis and uptake of rhamnolipids and their precursors
title_full Novel insights into biosynthesis and uptake of rhamnolipids and their precursors
title_fullStr Novel insights into biosynthesis and uptake of rhamnolipids and their precursors
title_full_unstemmed Novel insights into biosynthesis and uptake of rhamnolipids and their precursors
title_short Novel insights into biosynthesis and uptake of rhamnolipids and their precursors
title_sort novel insights into biosynthesis and uptake of rhamnolipids and their precursors
topic Biotechnologically Relevant Enzymes and Proteins
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5352749/
https://www.ncbi.nlm.nih.gov/pubmed/27988798
http://dx.doi.org/10.1007/s00253-016-8041-3
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