All three endogenous quinone species of Escherichia coli are involved in controlling the activity of the aerobic/anaerobic response regulator ArcA
The enteron Escherichia coli is equipped with a branched electron transfer chain that mediates chemiosmotic electron transfer, that drives ATP synthesis. The components of this electron transfer chain couple the oxidation of available electron donors from cellular metabolism (e.g. NADH, succinate, l...
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Format: | Article |
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Frontiers Media S.A.
2016-09-01
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Series: | Frontiers in Microbiology |
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Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01339/full |
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author | Johan Willem Albertus Van Beilen Klaas Jan Hellingwerf |
author_facet | Johan Willem Albertus Van Beilen Klaas Jan Hellingwerf |
author_sort | Johan Willem Albertus Van Beilen |
collection | DOAJ |
description | The enteron Escherichia coli is equipped with a branched electron transfer chain that mediates chemiosmotic electron transfer, that drives ATP synthesis. The components of this electron transfer chain couple the oxidation of available electron donors from cellular metabolism (e.g. NADH, succinate, lactate, formate, etc.) to the reduction of electron acceptors like oxygen, nitrate, fumarate, di-methyl-sulfoxide, etc. Three different quinones, i.e. ubiquinone, demethyl-menaquinone and menaquinone, couple the transfer of electrons between the dehydrogenases and reductases/oxidases that constitute this electron transfer chain, whereas the two-component regulation system ArcB/A regulates gene expression, to allow the organism to adapt itself to the ambient conditions of available electron donors and acceptors. Here we report that E. coli can grow and adjust well to transitions in the availability of oxygen, with any of the three quinones as its single quinone. In all three ‘single-quinone’ E. coli strains transitions in the activity of ArcB are observed, as evidenced by changes in the level of phosphorylation of the response regulator ArcA, upon depletion/readmission of oxygen. These results lead us to conclude that all quinol species of E. coli can reduce (i.e. activate) the sensor ArcB and all three quinones oxidize (i.e. de-activate) it. These results also confirm our earlier conclusion that demethyl-menaquinone can function in aerobic respiration. |
first_indexed | 2024-12-22T22:03:34Z |
format | Article |
id | doaj.art-49f6238ba04846d6bf92465c8865195b |
institution | Directory Open Access Journal |
issn | 1664-302X |
language | English |
last_indexed | 2024-12-22T22:03:34Z |
publishDate | 2016-09-01 |
publisher | Frontiers Media S.A. |
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series | Frontiers in Microbiology |
spelling | doaj.art-49f6238ba04846d6bf92465c8865195b2022-12-21T18:11:03ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2016-09-01710.3389/fmicb.2016.01339208925All three endogenous quinone species of Escherichia coli are involved in controlling the activity of the aerobic/anaerobic response regulator ArcAJohan Willem Albertus Van Beilen0Klaas Jan Hellingwerf1University of AmsterdamUniversity of AmsterdamThe enteron Escherichia coli is equipped with a branched electron transfer chain that mediates chemiosmotic electron transfer, that drives ATP synthesis. The components of this electron transfer chain couple the oxidation of available electron donors from cellular metabolism (e.g. NADH, succinate, lactate, formate, etc.) to the reduction of electron acceptors like oxygen, nitrate, fumarate, di-methyl-sulfoxide, etc. Three different quinones, i.e. ubiquinone, demethyl-menaquinone and menaquinone, couple the transfer of electrons between the dehydrogenases and reductases/oxidases that constitute this electron transfer chain, whereas the two-component regulation system ArcB/A regulates gene expression, to allow the organism to adapt itself to the ambient conditions of available electron donors and acceptors. Here we report that E. coli can grow and adjust well to transitions in the availability of oxygen, with any of the three quinones as its single quinone. In all three ‘single-quinone’ E. coli strains transitions in the activity of ArcB are observed, as evidenced by changes in the level of phosphorylation of the response regulator ArcA, upon depletion/readmission of oxygen. These results lead us to conclude that all quinol species of E. coli can reduce (i.e. activate) the sensor ArcB and all three quinones oxidize (i.e. de-activate) it. These results also confirm our earlier conclusion that demethyl-menaquinone can function in aerobic respiration.http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01339/fullUbiquinoneArcAArcBA two-component systemmenaquinonephos-tag electrophoresissingle-quinone producing mutants |
spellingShingle | Johan Willem Albertus Van Beilen Klaas Jan Hellingwerf All three endogenous quinone species of Escherichia coli are involved in controlling the activity of the aerobic/anaerobic response regulator ArcA Frontiers in Microbiology Ubiquinone ArcA ArcBA two-component system menaquinone phos-tag electrophoresis single-quinone producing mutants |
title | All three endogenous quinone species of Escherichia coli are involved in controlling the activity of the aerobic/anaerobic response regulator ArcA |
title_full | All three endogenous quinone species of Escherichia coli are involved in controlling the activity of the aerobic/anaerobic response regulator ArcA |
title_fullStr | All three endogenous quinone species of Escherichia coli are involved in controlling the activity of the aerobic/anaerobic response regulator ArcA |
title_full_unstemmed | All three endogenous quinone species of Escherichia coli are involved in controlling the activity of the aerobic/anaerobic response regulator ArcA |
title_short | All three endogenous quinone species of Escherichia coli are involved in controlling the activity of the aerobic/anaerobic response regulator ArcA |
title_sort | all three endogenous quinone species of escherichia coli are involved in controlling the activity of the aerobic anaerobic response regulator arca |
topic | Ubiquinone ArcA ArcBA two-component system menaquinone phos-tag electrophoresis single-quinone producing mutants |
url | http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01339/full |
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