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Three bacterial DedA subfamilies with distinct functions and phylogenetic distribution

Recent studies in bacteria suggested that the broadly conserved but enigmatic DedA proteins function as undecaprenyl-phosphate (UndP) flippases, recycling this essential lipid carrier. To determine whether all DedA proteins have UndP flippase activity, we performed a phylogenetic analysis and correl...

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Detalles Bibliográficos
Autores principales: Todor, Horia, Herrera, Nadia, Gross, Carol
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9881974/
https://www.ncbi.nlm.nih.gov/pubmed/36712119
http://dx.doi.org/10.1101/2023.01.04.522824
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author Todor, Horia
Herrera, Nadia
Gross, Carol
author_facet Todor, Horia
Herrera, Nadia
Gross, Carol
author_sort Todor, Horia
collection PubMed
description Recent studies in bacteria suggested that the broadly conserved but enigmatic DedA proteins function as undecaprenyl-phosphate (UndP) flippases, recycling this essential lipid carrier. To determine whether all DedA proteins have UndP flippase activity, we performed a phylogenetic analysis and correlated it to previously published experimental results and predicted structures. We uncovered three major DedA subfamilies: one contains UndP flippases, the second contains putative phospholipid flippases and is associated with aerobic metabolism, and the third is found only in specific Gram-negative phyla.
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spelling pubmed-98819742023-01-28 Three bacterial DedA subfamilies with distinct functions and phylogenetic distribution Todor, Horia Herrera, Nadia Gross, Carol bioRxiv Article Recent studies in bacteria suggested that the broadly conserved but enigmatic DedA proteins function as undecaprenyl-phosphate (UndP) flippases, recycling this essential lipid carrier. To determine whether all DedA proteins have UndP flippase activity, we performed a phylogenetic analysis and correlated it to previously published experimental results and predicted structures. We uncovered three major DedA subfamilies: one contains UndP flippases, the second contains putative phospholipid flippases and is associated with aerobic metabolism, and the third is found only in specific Gram-negative phyla. Cold Spring Harbor Laboratory 2023-01-05 /pmc/articles/PMC9881974/ /pubmed/36712119 http://dx.doi.org/10.1101/2023.01.04.522824 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator.
spellingShingle Article
Todor, Horia
Herrera, Nadia
Gross, Carol
Three bacterial DedA subfamilies with distinct functions and phylogenetic distribution
title Three bacterial DedA subfamilies with distinct functions and phylogenetic distribution
title_full Three bacterial DedA subfamilies with distinct functions and phylogenetic distribution
title_fullStr Three bacterial DedA subfamilies with distinct functions and phylogenetic distribution
title_full_unstemmed Three bacterial DedA subfamilies with distinct functions and phylogenetic distribution
title_short Three bacterial DedA subfamilies with distinct functions and phylogenetic distribution
title_sort three bacterial deda subfamilies with distinct functions and phylogenetic distribution
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9881974/
https://www.ncbi.nlm.nih.gov/pubmed/36712119
http://dx.doi.org/10.1101/2023.01.04.522824
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