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From Cell Death to Metabolism: Holin-Antiholin Homologues with New Functions

Programmed cell death in bacteria is generally triggered by membrane proteins with functions analogous to those of bacteriophage holins: they disrupt the membrane potential, whereas antiholins antagonize this process. The holin-like class of proteins is present in all three domains of life, but thei...

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Detalles Bibliográficos
Autores principales: van den Esker, Marielle H., Kovács, Ákos T., Kuipers, Oscar P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Microbiology 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5717393/
https://www.ncbi.nlm.nih.gov/pubmed/29208748
http://dx.doi.org/10.1128/mBio.01963-17
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author van den Esker, Marielle H.
Kovács, Ákos T.
Kuipers, Oscar P.
author_facet van den Esker, Marielle H.
Kovács, Ákos T.
Kuipers, Oscar P.
author_sort van den Esker, Marielle H.
collection PubMed
description Programmed cell death in bacteria is generally triggered by membrane proteins with functions analogous to those of bacteriophage holins: they disrupt the membrane potential, whereas antiholins antagonize this process. The holin-like class of proteins is present in all three domains of life, but their functions can be different, depending on the species. Using a series of biochemical and genetic approaches, in a recent article in mBio, Charbonnier et al. (mBio 8:e00976-17, 2017, https://doi.org/10.1128/mBio.00976-17) demonstrate that the antiholin homologue in Bacillus subtilis transports pyruvate and is regulated in an unconventional way by its substrate molecule. Here, we discuss the connection between cell death and metabolism in various bacteria carrying genes encoding these holin-antiholin analogues and place the recent study by Charbonnier et al. in an evolutionary context.
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spelling pubmed-57173932017-12-14 From Cell Death to Metabolism: Holin-Antiholin Homologues with New Functions van den Esker, Marielle H. Kovács, Ákos T. Kuipers, Oscar P. mBio Commentary Programmed cell death in bacteria is generally triggered by membrane proteins with functions analogous to those of bacteriophage holins: they disrupt the membrane potential, whereas antiholins antagonize this process. The holin-like class of proteins is present in all three domains of life, but their functions can be different, depending on the species. Using a series of biochemical and genetic approaches, in a recent article in mBio, Charbonnier et al. (mBio 8:e00976-17, 2017, https://doi.org/10.1128/mBio.00976-17) demonstrate that the antiholin homologue in Bacillus subtilis transports pyruvate and is regulated in an unconventional way by its substrate molecule. Here, we discuss the connection between cell death and metabolism in various bacteria carrying genes encoding these holin-antiholin analogues and place the recent study by Charbonnier et al. in an evolutionary context. American Society for Microbiology 2017-12-05 /pmc/articles/PMC5717393/ /pubmed/29208748 http://dx.doi.org/10.1128/mBio.01963-17 Text en Copyright © 2017 van den Esker et al. https://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Commentary
van den Esker, Marielle H.
Kovács, Ákos T.
Kuipers, Oscar P.
From Cell Death to Metabolism: Holin-Antiholin Homologues with New Functions
title From Cell Death to Metabolism: Holin-Antiholin Homologues with New Functions
title_full From Cell Death to Metabolism: Holin-Antiholin Homologues with New Functions
title_fullStr From Cell Death to Metabolism: Holin-Antiholin Homologues with New Functions
title_full_unstemmed From Cell Death to Metabolism: Holin-Antiholin Homologues with New Functions
title_short From Cell Death to Metabolism: Holin-Antiholin Homologues with New Functions
title_sort from cell death to metabolism: holin-antiholin homologues with new functions
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5717393/
https://www.ncbi.nlm.nih.gov/pubmed/29208748
http://dx.doi.org/10.1128/mBio.01963-17
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