The ArcB Leucine Zipper Domain Is Required for Proper ArcB Signaling

The Arc two-component system modulates the expression of numerous genes in response to respiratory growth conditions. This system comprises ArcA as the response regulator and ArcB as the sensor kinase. ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-...

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Detalles Bibliográficos
Autores principales: Nuñez Oreza, Luis Alberto, Alvarez, Adrián F., Arias-Olguín, Imilla I., Torres Larios, Alfredo, Georgellis, Dimitris
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3364231/
https://www.ncbi.nlm.nih.gov/pubmed/22666479
http://dx.doi.org/10.1371/journal.pone.0038187
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author Nuñez Oreza, Luis Alberto
Alvarez, Adrián F.
Arias-Olguín, Imilla I.
Torres Larios, Alfredo
Georgellis, Dimitris
author_facet Nuñez Oreza, Luis Alberto
Alvarez, Adrián F.
Arias-Olguín, Imilla I.
Torres Larios, Alfredo
Georgellis, Dimitris
author_sort Nuñez Oreza, Luis Alberto
collection PubMed
description The Arc two-component system modulates the expression of numerous genes in response to respiratory growth conditions. This system comprises ArcA as the response regulator and ArcB as the sensor kinase. ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-located redox-active cysteine residues that participate in intermolecular disulfide bond formation. Here, we report that the ArcB protein segment covering residues 70–121, fulfills the molecular characteristics of a leucine zipper containing coiled coil structure. Also, mutational analyses of this segment reveal three different phenotypical effects to be distributed along the coiled coil structure of ArcB, demonstrating that this motif is essential for proper ArcB signaling.
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spelling pubmed-33642312012-06-04 The ArcB Leucine Zipper Domain Is Required for Proper ArcB Signaling Nuñez Oreza, Luis Alberto Alvarez, Adrián F. Arias-Olguín, Imilla I. Torres Larios, Alfredo Georgellis, Dimitris PLoS One Research Article The Arc two-component system modulates the expression of numerous genes in response to respiratory growth conditions. This system comprises ArcA as the response regulator and ArcB as the sensor kinase. ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-located redox-active cysteine residues that participate in intermolecular disulfide bond formation. Here, we report that the ArcB protein segment covering residues 70–121, fulfills the molecular characteristics of a leucine zipper containing coiled coil structure. Also, mutational analyses of this segment reveal three different phenotypical effects to be distributed along the coiled coil structure of ArcB, demonstrating that this motif is essential for proper ArcB signaling. Public Library of Science 2012-05-30 /pmc/articles/PMC3364231/ /pubmed/22666479 http://dx.doi.org/10.1371/journal.pone.0038187 Text en Nuñez Oreza et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Nuñez Oreza, Luis Alberto
Alvarez, Adrián F.
Arias-Olguín, Imilla I.
Torres Larios, Alfredo
Georgellis, Dimitris
The ArcB Leucine Zipper Domain Is Required for Proper ArcB Signaling
title The ArcB Leucine Zipper Domain Is Required for Proper ArcB Signaling
title_full The ArcB Leucine Zipper Domain Is Required for Proper ArcB Signaling
title_fullStr The ArcB Leucine Zipper Domain Is Required for Proper ArcB Signaling
title_full_unstemmed The ArcB Leucine Zipper Domain Is Required for Proper ArcB Signaling
title_short The ArcB Leucine Zipper Domain Is Required for Proper ArcB Signaling
title_sort arcb leucine zipper domain is required for proper arcb signaling
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3364231/
https://www.ncbi.nlm.nih.gov/pubmed/22666479
http://dx.doi.org/10.1371/journal.pone.0038187
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