Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases

Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases

Bacterial two-component systems are composed of a sensor histidine kinase (HK) and an effector response regulator and upon signal detection, the HK autophosphorylates a conserved His residue. Here the authors structurally and functionally characterise two HKs, HK853–RR468 and EnvZ–OmpR, and find tha...

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Main Authors: Cristina Mideros-Mora, Laura Miguel-Romero, Alonso Felipe-Ruiz, Patricia Casino, Alberto Marina
Format: Article
Language:English
Published: Nature Publishing Group 2020-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-14540-5
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spelling doaj-a680d0f7de9a49d3bb3359801876a0f32021-05-11T08:48:00ZengNature Publishing GroupNature Communications2041-17232020-02-0111111310.1038/s41467-020-14540-5Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinasesCristina Mideros-Mora0Laura Miguel-Romero1Alonso Felipe-Ruiz2Patricia Casino3Alberto Marina4Instituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas (IBV-CSIC)Instituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas (IBV-CSIC)Instituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas (IBV-CSIC)Departament de Bioquímica i Biología molecular, Universitat de ValènciaInstituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas (IBV-CSIC)Bacterial two-component systems are composed of a sensor histidine kinase (HK) and an effector response regulator and upon signal detection, the HK autophosphorylates a conserved His residue. Here the authors structurally and functionally characterise two HKs, HK853–RR468 and EnvZ–OmpR, and find that the rotamer of the phosphorylatable catalytic His is not influenced by the environmental pH, ruling out an earlier proposed pH-gated model.https://doi.org/10.1038/s41467-020-14540-5
collection DOAJ
language English
format Article
sources DOAJ
author Cristina Mideros-Mora
Laura Miguel-Romero
Alonso Felipe-Ruiz
Patricia Casino
Alberto Marina
spellingShingle Cristina Mideros-Mora
Laura Miguel-Romero
Alonso Felipe-Ruiz
Patricia Casino
Alberto Marina
Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
Nature Communications
author_facet Cristina Mideros-Mora
Laura Miguel-Romero
Alonso Felipe-Ruiz
Patricia Casino
Alberto Marina
author_sort Cristina Mideros-Mora
title Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
title_short Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
title_full Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
title_fullStr Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
title_full_unstemmed Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
title_sort revisiting the ph-gated conformational switch on the activities of hiska-family histidine kinases
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2020-02-01
description Bacterial two-component systems are composed of a sensor histidine kinase (HK) and an effector response regulator and upon signal detection, the HK autophosphorylates a conserved His residue. Here the authors structurally and functionally characterise two HKs, HK853–RR468 and EnvZ–OmpR, and find that the rotamer of the phosphorylatable catalytic His is not influenced by the environmental pH, ruling out an earlier proposed pH-gated model.
url https://doi.org/10.1038/s41467-020-14540-5
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AT patriciacasino revisitingthephgatedconformationalswitchontheactivitiesofhiskafamilyhistidinekinases
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