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Evidence for Escherichia coli DcuD carrier dependent F(O)F(1)-ATPase activity during fermentation of glycerol
During fermentation Escherichia coli excrete succinate mainly via Dcu family carriers. Current work reveals the total and N,N’-dicyclohexylcarbodiimide (DCCD) inhibited ATPase activity at pH 7.5 and 5.5 in E. coli wild type and dcu mutants upon glycerol fermentation. The overall ATPase activity was...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6414658/ https://www.ncbi.nlm.nih.gov/pubmed/30862913 http://dx.doi.org/10.1038/s41598-019-41044-0 |
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author | Karapetyan, L. Valle, A. Bolivar, J. Trchounian, A. Trchounian, K. |
author_facet | Karapetyan, L. Valle, A. Bolivar, J. Trchounian, A. Trchounian, K. |
author_sort | Karapetyan, L. |
collection | PubMed |
description | During fermentation Escherichia coli excrete succinate mainly via Dcu family carriers. Current work reveals the total and N,N’-dicyclohexylcarbodiimide (DCCD) inhibited ATPase activity at pH 7.5 and 5.5 in E. coli wild type and dcu mutants upon glycerol fermentation. The overall ATPase activity was highest at pH 7.5 in dcuABCD mutant. In wild type cells 50% of the activity came from the F(O)F(1)-ATPase but in dcuD mutant it reached ~80%. K(+) (100 mM) stimulate total but not DCCD inhibited ATPase activity 40% and 20% in wild type and dcuD mutant, respectively. 90% of overall ATPase activity was inhibited by DCCD at pH 5.5 only in dcuABC mutant. At pH 7.5 the H(+) fluxes in E. coli wild type, dcuD and dcuABCD mutants was similar but in dcuABC triple mutant the H(+) flux decreased 1.4 fold reaching 1.15 mM/min when glycerol was supplemented. In succinate assays the H(+) flux was higher in the strains where DcuD is absent. No significant differences were determined in wild type and mutants specific growth rate except dcuD strain. Taken together it is suggested that during glycerol fermentation DcuD has impact on H(+) fluxes, F(O)F(1)-ATPase activity and depends on potassium ions. |
format | Online Article Text |
id | pubmed-6414658 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-64146582019-03-14 Evidence for Escherichia coli DcuD carrier dependent F(O)F(1)-ATPase activity during fermentation of glycerol Karapetyan, L. Valle, A. Bolivar, J. Trchounian, A. Trchounian, K. Sci Rep Article During fermentation Escherichia coli excrete succinate mainly via Dcu family carriers. Current work reveals the total and N,N’-dicyclohexylcarbodiimide (DCCD) inhibited ATPase activity at pH 7.5 and 5.5 in E. coli wild type and dcu mutants upon glycerol fermentation. The overall ATPase activity was highest at pH 7.5 in dcuABCD mutant. In wild type cells 50% of the activity came from the F(O)F(1)-ATPase but in dcuD mutant it reached ~80%. K(+) (100 mM) stimulate total but not DCCD inhibited ATPase activity 40% and 20% in wild type and dcuD mutant, respectively. 90% of overall ATPase activity was inhibited by DCCD at pH 5.5 only in dcuABC mutant. At pH 7.5 the H(+) fluxes in E. coli wild type, dcuD and dcuABCD mutants was similar but in dcuABC triple mutant the H(+) flux decreased 1.4 fold reaching 1.15 mM/min when glycerol was supplemented. In succinate assays the H(+) flux was higher in the strains where DcuD is absent. No significant differences were determined in wild type and mutants specific growth rate except dcuD strain. Taken together it is suggested that during glycerol fermentation DcuD has impact on H(+) fluxes, F(O)F(1)-ATPase activity and depends on potassium ions. Nature Publishing Group UK 2019-03-12 /pmc/articles/PMC6414658/ /pubmed/30862913 http://dx.doi.org/10.1038/s41598-019-41044-0 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Karapetyan, L. Valle, A. Bolivar, J. Trchounian, A. Trchounian, K. Evidence for Escherichia coli DcuD carrier dependent F(O)F(1)-ATPase activity during fermentation of glycerol |
title | Evidence for Escherichia coli DcuD carrier dependent F(O)F(1)-ATPase activity during fermentation of glycerol |
title_full | Evidence for Escherichia coli DcuD carrier dependent F(O)F(1)-ATPase activity during fermentation of glycerol |
title_fullStr | Evidence for Escherichia coli DcuD carrier dependent F(O)F(1)-ATPase activity during fermentation of glycerol |
title_full_unstemmed | Evidence for Escherichia coli DcuD carrier dependent F(O)F(1)-ATPase activity during fermentation of glycerol |
title_short | Evidence for Escherichia coli DcuD carrier dependent F(O)F(1)-ATPase activity during fermentation of glycerol |
title_sort | evidence for escherichia coli dcud carrier dependent f(o)f(1)-atpase activity during fermentation of glycerol |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6414658/ https://www.ncbi.nlm.nih.gov/pubmed/30862913 http://dx.doi.org/10.1038/s41598-019-41044-0 |
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