Cargando…
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...
Autores principales: | , , , , , , , |
---|---|
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 |
_version_ | 1783707318244868096 |
---|---|
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. |
format | Online Article Text |
id | pubmed-8199190 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT gushchinivan nitrateandnitritesensinghistidinekinasesfunctionstructureandnaturaldiversity AT aleksenkovladimira nitrateandnitritesensinghistidinekinasesfunctionstructureandnaturaldiversity AT orekhovphilipp nitrateandnitritesensinghistidinekinasesfunctionstructureandnaturaldiversity AT goncharovivanm nitrateandnitritesensinghistidinekinasesfunctionstructureandnaturaldiversity AT nazarenkoverav nitrateandnitritesensinghistidinekinasesfunctionstructureandnaturaldiversity AT semenovoleg nitrateandnitritesensinghistidinekinasesfunctionstructureandnaturaldiversity AT remeevaalina nitrateandnitritesensinghistidinekinasesfunctionstructureandnaturaldiversity AT gordeliyvalentin nitrateandnitritesensinghistidinekinasesfunctionstructureandnaturaldiversity |