Cargando…
Interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in Azotobacter vinelandii
All diazotrophic bacteria and archaea isolated so far utilise a nitrogenase enzyme‐containing molybdenum in the active site co‐factor to fix atmospheric dinitrogen to ammonia. However, in addition to the Mo‐dependent nitrogenase, some nitrogen‐fixing prokaryotes also express genetically distinct alt...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9542535/ https://www.ncbi.nlm.nih.gov/pubmed/35718936 http://dx.doi.org/10.1111/mmi.14955 |
_version_ | 1784804171931713536 |
---|---|
author | Appia‐Ayme, Corinne Little, Richard Chandra, Govind de Oliveira Martins, Carlo Bueno Batista, Marcelo Dixon, Ray |
author_facet | Appia‐Ayme, Corinne Little, Richard Chandra, Govind de Oliveira Martins, Carlo Bueno Batista, Marcelo Dixon, Ray |
author_sort | Appia‐Ayme, Corinne |
collection | PubMed |
description | All diazotrophic bacteria and archaea isolated so far utilise a nitrogenase enzyme‐containing molybdenum in the active site co‐factor to fix atmospheric dinitrogen to ammonia. However, in addition to the Mo‐dependent nitrogenase, some nitrogen‐fixing prokaryotes also express genetically distinct alternative nitrogenase isoenzymes, namely the V‐dependent and Fe‐only nitrogenases, respectively. Nitrogenase isoenzymes are expressed hierarchically according to metal availability and catalytic efficiency. In proteobacteria, this hierarchy is maintained via stringent transcriptional regulation of gene clusters by dedicated bacterial enhancer‐binding proteins (bEBPs). The model diazotroph Azotobacter vinelandii contains two paralogs of the vanadium nitrogenase activator VnfA (henceforth, VnfA1), designated VnfA2 and VnfA3, with unknown functions. Here we demonstrate that the VnfA1 and VnfA3 bEBPs bind to the same target promoters in the Azotobacter vinelandii genome and co‐activate a subset of genes in the absence of V, including the structural genes for the Fe‐only nitrogenase. Co‐activation is inhibited by the presence of V and is dependent on an accessory protein VnfZ that is co‐expressed with VnfA3. Our studies uncover a plethora of interactions between bEBPs required for nitrogen fixation, revealing the unprecedented potential for fine‐tuning the expression of alternative nitrogenases in response to metal availability. |
format | Online Article Text |
id | pubmed-9542535 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-95425352022-10-14 Interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in Azotobacter vinelandii Appia‐Ayme, Corinne Little, Richard Chandra, Govind de Oliveira Martins, Carlo Bueno Batista, Marcelo Dixon, Ray Mol Microbiol Research Articles All diazotrophic bacteria and archaea isolated so far utilise a nitrogenase enzyme‐containing molybdenum in the active site co‐factor to fix atmospheric dinitrogen to ammonia. However, in addition to the Mo‐dependent nitrogenase, some nitrogen‐fixing prokaryotes also express genetically distinct alternative nitrogenase isoenzymes, namely the V‐dependent and Fe‐only nitrogenases, respectively. Nitrogenase isoenzymes are expressed hierarchically according to metal availability and catalytic efficiency. In proteobacteria, this hierarchy is maintained via stringent transcriptional regulation of gene clusters by dedicated bacterial enhancer‐binding proteins (bEBPs). The model diazotroph Azotobacter vinelandii contains two paralogs of the vanadium nitrogenase activator VnfA (henceforth, VnfA1), designated VnfA2 and VnfA3, with unknown functions. Here we demonstrate that the VnfA1 and VnfA3 bEBPs bind to the same target promoters in the Azotobacter vinelandii genome and co‐activate a subset of genes in the absence of V, including the structural genes for the Fe‐only nitrogenase. Co‐activation is inhibited by the presence of V and is dependent on an accessory protein VnfZ that is co‐expressed with VnfA3. Our studies uncover a plethora of interactions between bEBPs required for nitrogen fixation, revealing the unprecedented potential for fine‐tuning the expression of alternative nitrogenases in response to metal availability. John Wiley and Sons Inc. 2022-06-29 2022 /pmc/articles/PMC9542535/ /pubmed/35718936 http://dx.doi.org/10.1111/mmi.14955 Text en © 2022 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Appia‐Ayme, Corinne Little, Richard Chandra, Govind de Oliveira Martins, Carlo Bueno Batista, Marcelo Dixon, Ray Interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in Azotobacter vinelandii |
title | Interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in Azotobacter vinelandii
|
title_full | Interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in Azotobacter vinelandii
|
title_fullStr | Interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in Azotobacter vinelandii
|
title_full_unstemmed | Interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in Azotobacter vinelandii
|
title_short | Interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in Azotobacter vinelandii
|
title_sort | interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in azotobacter vinelandii |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9542535/ https://www.ncbi.nlm.nih.gov/pubmed/35718936 http://dx.doi.org/10.1111/mmi.14955 |
work_keys_str_mv | AT appiaaymecorinne interactionsbetweenparalogousbacterialenhancerbindingproteinsenablemetaldependentregulationofalternativenitrogenasesinazotobactervinelandii AT littlerichard interactionsbetweenparalogousbacterialenhancerbindingproteinsenablemetaldependentregulationofalternativenitrogenasesinazotobactervinelandii AT chandragovind interactionsbetweenparalogousbacterialenhancerbindingproteinsenablemetaldependentregulationofalternativenitrogenasesinazotobactervinelandii AT deoliveiramartinscarlo interactionsbetweenparalogousbacterialenhancerbindingproteinsenablemetaldependentregulationofalternativenitrogenasesinazotobactervinelandii AT buenobatistamarcelo interactionsbetweenparalogousbacterialenhancerbindingproteinsenablemetaldependentregulationofalternativenitrogenasesinazotobactervinelandii AT dixonray interactionsbetweenparalogousbacterialenhancerbindingproteinsenablemetaldependentregulationofalternativenitrogenasesinazotobactervinelandii |