The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates

Abstract Microbial colonization of different environments is enabled to a great extent by the plasticity of their sensory mechanisms, among them, the two-component signal transduction systems (TCS). Here, an example of TCS plasticity is presented: the regulation of L-malate catabolism via malic enzy...

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Autores principales:	L. Miguel-Romero, P. Casino, J. M. Landete, V. Monedero, M. Zúñiga, A. Marina
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8eb96945d93644eb938ca552ac96f2a3
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spelling	oai:doaj.org-article:8eb96945d93644eb938ca552ac96f2a32021-12-02T16:06:10ZThe malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates10.1038/s41598-017-02900-z2045-2322https://doaj.org/article/8eb96945d93644eb938ca552ac96f2a32017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02900-zhttps://doaj.org/toc/2045-2322Abstract Microbial colonization of different environments is enabled to a great extent by the plasticity of their sensory mechanisms, among them, the two-component signal transduction systems (TCS). Here, an example of TCS plasticity is presented: the regulation of L-malate catabolism via malic enzyme by MaeRK in Lactobacillales. MaeKR belongs to the citrate family of TCS as the Escherichia coli DcuSR system. We show that the Lactobacillus casei histidine-kinase MaeK is defective in autophosphorylation activity as it lacks a functional catalytic and ATP binding domain. The cognate response regulator MaeR was poorly phosphorylated at its phosphoacceptor Asp in vitro. This phosphorylation, however, enhanced MaeR binding in vitro to its target sites and it was required for induction of regulated genes in vivo. Elucidation of the MaeR structure revealed that response regulator dimerization is accomplished by the swapping of α4-β5-α5 elements between two monomers, generating a phosphoacceptor competent conformation. Sequence and phylogenetic analyses showed that the MaeKR peculiarities are not exclusive to L. casei as they are shared by the rest of orthologous systems of Lactobacillales. Our results reveal MaeKR as a non-canonical TCS displaying distinctive features: a swapped response regulator and a sensor histidine kinase lacking ATP-dependent kinase activity.L. Miguel-RomeroP. CasinoJ. M. LandeteV. MonederoM. ZúñigaA. MarinaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-16 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q L. Miguel-Romero P. Casino J. M. Landete V. Monedero M. Zúñiga A. Marina The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates
description	Abstract Microbial colonization of different environments is enabled to a great extent by the plasticity of their sensory mechanisms, among them, the two-component signal transduction systems (TCS). Here, an example of TCS plasticity is presented: the regulation of L-malate catabolism via malic enzyme by MaeRK in Lactobacillales. MaeKR belongs to the citrate family of TCS as the Escherichia coli DcuSR system. We show that the Lactobacillus casei histidine-kinase MaeK is defective in autophosphorylation activity as it lacks a functional catalytic and ATP binding domain. The cognate response regulator MaeR was poorly phosphorylated at its phosphoacceptor Asp in vitro. This phosphorylation, however, enhanced MaeR binding in vitro to its target sites and it was required for induction of regulated genes in vivo. Elucidation of the MaeR structure revealed that response regulator dimerization is accomplished by the swapping of α4-β5-α5 elements between two monomers, generating a phosphoacceptor competent conformation. Sequence and phylogenetic analyses showed that the MaeKR peculiarities are not exclusive to L. casei as they are shared by the rest of orthologous systems of Lactobacillales. Our results reveal MaeKR as a non-canonical TCS displaying distinctive features: a swapped response regulator and a sensor histidine kinase lacking ATP-dependent kinase activity.
format	article
author	L. Miguel-Romero P. Casino J. M. Landete V. Monedero M. Zúñiga A. Marina
author_facet	L. Miguel-Romero P. Casino J. M. Landete V. Monedero M. Zúñiga A. Marina
author_sort	L. Miguel-Romero
title	The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates
title_short	The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates
title_full	The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates
title_fullStr	The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates
title_full_unstemmed	The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates
title_sort	malate sensing two-component system maekr is a non-canonical class of sensory complex for c4-dicarboxylates
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/8eb96945d93644eb938ca552ac96f2a3
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The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates

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