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LurR is a regulator of the central lactate oxidation pathway in sulfate-reducing Desulfovibrio species
The central carbon/lactate utilization pathway in the model sulfate-reducing bacterium, Desulfovibrio vulgaris Hildenborough, is encoded by the highly conserved operon DVU3025-3033. Our earlier in vitro genome-wide study had suggested a network of four two-component system regulators that target thi...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6456213/ https://www.ncbi.nlm.nih.gov/pubmed/30964892 http://dx.doi.org/10.1371/journal.pone.0214960 |
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author | Rajeev, Lara Luning, Eric G. Zane, Grant M. Juba, Thomas R. Kazakov, Alexey E. Novichkov, Pavel S. Wall, Judy D. Mukhopadhyay, Aindrila |
author_facet | Rajeev, Lara Luning, Eric G. Zane, Grant M. Juba, Thomas R. Kazakov, Alexey E. Novichkov, Pavel S. Wall, Judy D. Mukhopadhyay, Aindrila |
author_sort | Rajeev, Lara |
collection | PubMed |
description | The central carbon/lactate utilization pathway in the model sulfate-reducing bacterium, Desulfovibrio vulgaris Hildenborough, is encoded by the highly conserved operon DVU3025-3033. Our earlier in vitro genome-wide study had suggested a network of four two-component system regulators that target this large operon; however, how these four regulators control this operon was not known. Here, we probe the regulation of the lactate utilization operon with mutant strains and DNA-protein binding assays. We show that the LurR response regulator is required for optimal growth and complete lactate utilization, and that it activates the DVU3025-3033 lactate oxidation operon as well as DVU2451, a lactate permease gene, in the presence of lactate. We show by electrophoretic mobility shift assays that LurR binds to three sites in the upstream region of DVU3025, the first gene of the operon. NrfR, a response regulator that is activated under nitrite stress, and LurR share similar binding site motifs and bind the same sites upstream of DVU3025. The DVU3025 promoter also has a binding site motif (Pho box) that is bound by PhoB, a two-component response regulator activated under phosphate limitation. The lactate utilization operon, the regulator LurR, and LurR binding sites are conserved across the order Desulfovibrionales whereas possible modulation of the lactate utilization genes by additional regulators such as NrfR and PhoB appears to be limited to D. vulgaris. |
format | Online Article Text |
id | pubmed-6456213 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-64562132019-05-03 LurR is a regulator of the central lactate oxidation pathway in sulfate-reducing Desulfovibrio species Rajeev, Lara Luning, Eric G. Zane, Grant M. Juba, Thomas R. Kazakov, Alexey E. Novichkov, Pavel S. Wall, Judy D. Mukhopadhyay, Aindrila PLoS One Research Article The central carbon/lactate utilization pathway in the model sulfate-reducing bacterium, Desulfovibrio vulgaris Hildenborough, is encoded by the highly conserved operon DVU3025-3033. Our earlier in vitro genome-wide study had suggested a network of four two-component system regulators that target this large operon; however, how these four regulators control this operon was not known. Here, we probe the regulation of the lactate utilization operon with mutant strains and DNA-protein binding assays. We show that the LurR response regulator is required for optimal growth and complete lactate utilization, and that it activates the DVU3025-3033 lactate oxidation operon as well as DVU2451, a lactate permease gene, in the presence of lactate. We show by electrophoretic mobility shift assays that LurR binds to three sites in the upstream region of DVU3025, the first gene of the operon. NrfR, a response regulator that is activated under nitrite stress, and LurR share similar binding site motifs and bind the same sites upstream of DVU3025. The DVU3025 promoter also has a binding site motif (Pho box) that is bound by PhoB, a two-component response regulator activated under phosphate limitation. The lactate utilization operon, the regulator LurR, and LurR binding sites are conserved across the order Desulfovibrionales whereas possible modulation of the lactate utilization genes by additional regulators such as NrfR and PhoB appears to be limited to D. vulgaris. Public Library of Science 2019-04-09 /pmc/articles/PMC6456213/ /pubmed/30964892 http://dx.doi.org/10.1371/journal.pone.0214960 Text en © 2019 Rajeev 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 (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Rajeev, Lara Luning, Eric G. Zane, Grant M. Juba, Thomas R. Kazakov, Alexey E. Novichkov, Pavel S. Wall, Judy D. Mukhopadhyay, Aindrila LurR is a regulator of the central lactate oxidation pathway in sulfate-reducing Desulfovibrio species |
title | LurR is a regulator of the central lactate oxidation pathway in sulfate-reducing Desulfovibrio species |
title_full | LurR is a regulator of the central lactate oxidation pathway in sulfate-reducing Desulfovibrio species |
title_fullStr | LurR is a regulator of the central lactate oxidation pathway in sulfate-reducing Desulfovibrio species |
title_full_unstemmed | LurR is a regulator of the central lactate oxidation pathway in sulfate-reducing Desulfovibrio species |
title_short | LurR is a regulator of the central lactate oxidation pathway in sulfate-reducing Desulfovibrio species |
title_sort | lurr is a regulator of the central lactate oxidation pathway in sulfate-reducing desulfovibrio species |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6456213/ https://www.ncbi.nlm.nih.gov/pubmed/30964892 http://dx.doi.org/10.1371/journal.pone.0214960 |
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