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Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity

Under anaerobic conditions, bacteria may utilize nitrates and nitrites as electron acceptors. Sensitivity to nitrous compounds is achieved via several mechanisms, some of which rely on sensor histidine kinases (HKs). The best studied nitrate- and nitrite-sensing HKs (NSHKs) are NarQ and NarX from Es...

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Autores principales: Gushchin, Ivan, Aleksenko, Vladimir A., Orekhov, Philipp, Goncharov, Ivan M., Nazarenko, Vera V., Semenov, Oleg, Remeeva, Alina, Gordeliy, Valentin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8199190/
https://www.ncbi.nlm.nih.gov/pubmed/34072989
http://dx.doi.org/10.3390/ijms22115933
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author Gushchin, Ivan
Aleksenko, Vladimir A.
Orekhov, Philipp
Goncharov, Ivan M.
Nazarenko, Vera V.
Semenov, Oleg
Remeeva, Alina
Gordeliy, Valentin
author_facet Gushchin, Ivan
Aleksenko, Vladimir A.
Orekhov, Philipp
Goncharov, Ivan M.
Nazarenko, Vera V.
Semenov, Oleg
Remeeva, Alina
Gordeliy, Valentin
author_sort Gushchin, Ivan
collection PubMed
description Under anaerobic conditions, bacteria may utilize nitrates and nitrites as electron acceptors. Sensitivity to nitrous compounds is achieved via several mechanisms, some of which rely on sensor histidine kinases (HKs). The best studied nitrate- and nitrite-sensing HKs (NSHKs) are NarQ and NarX from Escherichia coli. Here, we review the function of NSHKs, analyze their natural diversity, and describe the available structural information. In particular, we show that around 6000 different NSHK sequences forming several distinct clusters may now be found in genomic databases, comprising mostly the genes from Beta- and Gammaproteobacteria as well as from Bacteroidetes and Chloroflexi, including those from anaerobic ammonia oxidation (annamox) communities. We show that the architecture of NSHKs is mostly conserved, although proteins from Bacteroidetes lack the HAMP and GAF-like domains yet sometimes have PAS. We reconcile the variation of NSHK sequences with atomistic models and pinpoint the structural elements important for signal transduction from the sensor domain to the catalytic module over the transmembrane and cytoplasmic regions spanning more than 200 Å.
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spelling pubmed-81991902021-06-14 Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity Gushchin, Ivan Aleksenko, Vladimir A. Orekhov, Philipp Goncharov, Ivan M. Nazarenko, Vera V. Semenov, Oleg Remeeva, Alina Gordeliy, Valentin Int J Mol Sci Review Under anaerobic conditions, bacteria may utilize nitrates and nitrites as electron acceptors. Sensitivity to nitrous compounds is achieved via several mechanisms, some of which rely on sensor histidine kinases (HKs). The best studied nitrate- and nitrite-sensing HKs (NSHKs) are NarQ and NarX from Escherichia coli. Here, we review the function of NSHKs, analyze their natural diversity, and describe the available structural information. In particular, we show that around 6000 different NSHK sequences forming several distinct clusters may now be found in genomic databases, comprising mostly the genes from Beta- and Gammaproteobacteria as well as from Bacteroidetes and Chloroflexi, including those from anaerobic ammonia oxidation (annamox) communities. We show that the architecture of NSHKs is mostly conserved, although proteins from Bacteroidetes lack the HAMP and GAF-like domains yet sometimes have PAS. We reconcile the variation of NSHK sequences with atomistic models and pinpoint the structural elements important for signal transduction from the sensor domain to the catalytic module over the transmembrane and cytoplasmic regions spanning more than 200 Å. MDPI 2021-05-31 /pmc/articles/PMC8199190/ /pubmed/34072989 http://dx.doi.org/10.3390/ijms22115933 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Gushchin, Ivan
Aleksenko, Vladimir A.
Orekhov, Philipp
Goncharov, Ivan M.
Nazarenko, Vera V.
Semenov, Oleg
Remeeva, Alina
Gordeliy, Valentin
Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity
title Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity
title_full Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity
title_fullStr Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity
title_full_unstemmed Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity
title_short Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity
title_sort nitrate- and nitrite-sensing histidine kinases: function, structure, and natural diversity
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8199190/
https://www.ncbi.nlm.nih.gov/pubmed/34072989
http://dx.doi.org/10.3390/ijms22115933
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