Two RmlC homologs catalyze dTDP-4-keto-6-deoxy-d-glucose epimerization in Pseudomonas putida KT2440

Abstract l-Rhamnose is an important monosaccharide both as nutrient source and as building block in prokaryotic glycoproteins and glycolipids. Generation of those composite molecules requires activated precursors being provided e. g. in form of nucleotide sugars such as dTDP-β-l-rhamnose (dTDP-l-Rha...

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Autores principales:	Franziska Koller, Jürgen Lassak
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/549fcec0fc20478eb78026694a87e7b5
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spelling	oai:doaj.org-article:549fcec0fc20478eb78026694a87e7b52021-12-02T17:47:18ZTwo RmlC homologs catalyze dTDP-4-keto-6-deoxy-d-glucose epimerization in Pseudomonas putida KT244010.1038/s41598-021-91421-x2045-2322https://doaj.org/article/549fcec0fc20478eb78026694a87e7b52021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-91421-xhttps://doaj.org/toc/2045-2322Abstract l-Rhamnose is an important monosaccharide both as nutrient source and as building block in prokaryotic glycoproteins and glycolipids. Generation of those composite molecules requires activated precursors being provided e. g. in form of nucleotide sugars such as dTDP-β-l-rhamnose (dTDP-l-Rha). dTDP-l-Rha is synthesized in a conserved 4-step reaction which is canonically catalyzed by the enzymes RmlABCD. An intact pathway is especially important for the fitness of pseudomonads, as dTDP-l-Rha is essential for the activation of the polyproline specific translation elongation factor EF-P in these bacteria. Within the scope of this study, we investigated the dTDP-l-Rha-biosynthesis route of Pseudomonas putida KT2440 with a focus on the last two steps. Bioinformatic analysis in combination with a screening approach revealed that epimerization of dTDP-4-keto-6-deoxy-d-glucose to dTDP-4-keto-6-deoxy-l-mannose is catalyzed by the two paralogous proteins PP_1782 (RmlC1) and PP_0265 (RmlC2), whereas the reduction to the final product is solely mediated by PP_1784 (RmlD). Thus, we also exclude the distinct RmlD homolog PP_0500 and the genetically linked nucleoside diphosphate-sugar epimerase PP_0501 to be involved in dTDP-l-Rha formation, other than suggested by certain databases. Together our analysis contributes to the molecular understanding how this important nucleotide-sugar is synthesized in pseudomonads.Franziska KollerJürgen LassakNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Franziska Koller Jürgen Lassak Two RmlC homologs catalyze dTDP-4-keto-6-deoxy-d-glucose epimerization in Pseudomonas putida KT2440
description	Abstract l-Rhamnose is an important monosaccharide both as nutrient source and as building block in prokaryotic glycoproteins and glycolipids. Generation of those composite molecules requires activated precursors being provided e. g. in form of nucleotide sugars such as dTDP-β-l-rhamnose (dTDP-l-Rha). dTDP-l-Rha is synthesized in a conserved 4-step reaction which is canonically catalyzed by the enzymes RmlABCD. An intact pathway is especially important for the fitness of pseudomonads, as dTDP-l-Rha is essential for the activation of the polyproline specific translation elongation factor EF-P in these bacteria. Within the scope of this study, we investigated the dTDP-l-Rha-biosynthesis route of Pseudomonas putida KT2440 with a focus on the last two steps. Bioinformatic analysis in combination with a screening approach revealed that epimerization of dTDP-4-keto-6-deoxy-d-glucose to dTDP-4-keto-6-deoxy-l-mannose is catalyzed by the two paralogous proteins PP_1782 (RmlC1) and PP_0265 (RmlC2), whereas the reduction to the final product is solely mediated by PP_1784 (RmlD). Thus, we also exclude the distinct RmlD homolog PP_0500 and the genetically linked nucleoside diphosphate-sugar epimerase PP_0501 to be involved in dTDP-l-Rha formation, other than suggested by certain databases. Together our analysis contributes to the molecular understanding how this important nucleotide-sugar is synthesized in pseudomonads.
format	article
author	Franziska Koller Jürgen Lassak
author_facet	Franziska Koller Jürgen Lassak
author_sort	Franziska Koller
title	Two RmlC homologs catalyze dTDP-4-keto-6-deoxy-d-glucose epimerization in Pseudomonas putida KT2440
title_short	Two RmlC homologs catalyze dTDP-4-keto-6-deoxy-d-glucose epimerization in Pseudomonas putida KT2440
title_full	Two RmlC homologs catalyze dTDP-4-keto-6-deoxy-d-glucose epimerization in Pseudomonas putida KT2440
title_fullStr	Two RmlC homologs catalyze dTDP-4-keto-6-deoxy-d-glucose epimerization in Pseudomonas putida KT2440
title_full_unstemmed	Two RmlC homologs catalyze dTDP-4-keto-6-deoxy-d-glucose epimerization in Pseudomonas putida KT2440
title_sort	two rmlc homologs catalyze dtdp-4-keto-6-deoxy-d-glucose epimerization in pseudomonas putida kt2440
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/549fcec0fc20478eb78026694a87e7b5
work_keys_str_mv	AT franziskakoller twormlchomologscatalyzedtdp4keto6deoxydglucoseepimerizationinpseudomonasputidakt2440 AT jurgenlassak twormlchomologscatalyzedtdp4keto6deoxydglucoseepimerizationinpseudomonasputidakt2440
_version_	1718379466716086272

Two RmlC homologs catalyze dTDP-4-keto-6-deoxy-d-glucose epimerization in Pseudomonas putida KT2440

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