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Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate
One-third of the lipid A found in the Escherichia coli outer membrane contains an unsubstituted diphosphate unit at position 1 (lipid A 1-diphosphate). We now report an inner membrane enzyme, LpxT (YeiU), which specifically transfers a phosphate group to lipid A, forming the 1-diphosphate species. (...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Blackwell Publishing Ltd
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2229476/ https://www.ncbi.nlm.nih.gov/pubmed/18047581 http://dx.doi.org/10.1111/j.1365-2958.2007.06044.x |
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author | Touzé, Thierry Tran, An X Hankins, Jessica V Mengin-Lecreulx, Dominique Trent, M Stephen |
author_facet | Touzé, Thierry Tran, An X Hankins, Jessica V Mengin-Lecreulx, Dominique Trent, M Stephen |
author_sort | Touzé, Thierry |
collection | PubMed |
description | One-third of the lipid A found in the Escherichia coli outer membrane contains an unsubstituted diphosphate unit at position 1 (lipid A 1-diphosphate). We now report an inner membrane enzyme, LpxT (YeiU), which specifically transfers a phosphate group to lipid A, forming the 1-diphosphate species. (32)P-labelled lipid A obtained from lpxT mutants do not produce lipid A 1-diphosphate. In vitro assays with Kdo(2)-[4′-(32)P]lipid A as the acceptor shows that LpxT uses undecaprenyl pyrophosphate as the substrate donor. Inhibition of lipid A 1-diphosphate formation in wild-type bacteria was demonstrated by sequestering undecaprenyl pyrophosphate with the cyclic polypeptide antibiotic bacitracin, providing evidence that undecaprenyl pyrophosphate serves as the donor substrate within whole bacteria. LpxT-catalysed phosphorylation is dependent upon transport of lipid A across the inner membrane by MsbA, a lipid A flippase, indicating a periplasmic active site. In conclusion, we demonstrate a novel pathway in the periplasmic modification of lipid A that is directly linked to the synthesis of undecaprenyl phosphate, an essential carrier lipid required for the synthesis of various bacterial polymers, such as peptidoglycan. |
format | Text |
id | pubmed-2229476 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Blackwell Publishing Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-22294762008-02-12 Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate Touzé, Thierry Tran, An X Hankins, Jessica V Mengin-Lecreulx, Dominique Trent, M Stephen Mol Microbiol Research Articles One-third of the lipid A found in the Escherichia coli outer membrane contains an unsubstituted diphosphate unit at position 1 (lipid A 1-diphosphate). We now report an inner membrane enzyme, LpxT (YeiU), which specifically transfers a phosphate group to lipid A, forming the 1-diphosphate species. (32)P-labelled lipid A obtained from lpxT mutants do not produce lipid A 1-diphosphate. In vitro assays with Kdo(2)-[4′-(32)P]lipid A as the acceptor shows that LpxT uses undecaprenyl pyrophosphate as the substrate donor. Inhibition of lipid A 1-diphosphate formation in wild-type bacteria was demonstrated by sequestering undecaprenyl pyrophosphate with the cyclic polypeptide antibiotic bacitracin, providing evidence that undecaprenyl pyrophosphate serves as the donor substrate within whole bacteria. LpxT-catalysed phosphorylation is dependent upon transport of lipid A across the inner membrane by MsbA, a lipid A flippase, indicating a periplasmic active site. In conclusion, we demonstrate a novel pathway in the periplasmic modification of lipid A that is directly linked to the synthesis of undecaprenyl phosphate, an essential carrier lipid required for the synthesis of various bacterial polymers, such as peptidoglycan. Blackwell Publishing Ltd 2008-01 2007-11-02 /pmc/articles/PMC2229476/ /pubmed/18047581 http://dx.doi.org/10.1111/j.1365-2958.2007.06044.x Text en © 2007 The Authors Journal compilation © 2007 Blackwell Publishing Ltd https://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation. |
spellingShingle | Research Articles Touzé, Thierry Tran, An X Hankins, Jessica V Mengin-Lecreulx, Dominique Trent, M Stephen Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate |
title | Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate |
title_full | Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate |
title_fullStr | Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate |
title_full_unstemmed | Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate |
title_short | Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate |
title_sort | periplasmic phosphorylation of lipid a is linked to the synthesis of undecaprenyl phosphate |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2229476/ https://www.ncbi.nlm.nih.gov/pubmed/18047581 http://dx.doi.org/10.1111/j.1365-2958.2007.06044.x |
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