Allen, J;
Ibrahim, IM;
Wang, L;
Puthiyaveetil, S;
Krauß, N;
Nield, J;
(2017)
Oligomeric states in sodium ion-dependent regulation of cyanobacterial histidine kinase-2.
Protoplasma
10.1007/s00709-017-1196-7.
(In press).
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Abstract
Two-component signal transduction systems (TCSs) consist of sensor histidine kinases and response regulators. TCSs mediate adaptation to environmental changes in bacteria, plants, fungi and protists. Histidine kinase 2 (Hik2) is a sensor histidine kinase found in all known cyanobacteria and as chloroplast sensor kinase in eukaryotic algae and plants. Sodium ions have been shown to inhibit the autophosphorylation activity of Hik2 with precedes phosphoryl transfer to response regulators, but the mechanism of inhibition has not been determined. We report on the mechanism of Hik2 activation and inactivation probed by chemical cross-linking and size exclusion chromatography together with direct visualisation of the kinase using negative-stain transmission electron microscopy of single particles. We show that the functional form of Hik2 is a higher-order oligomer such as a hexamer or octamer. Increased NaCl concentration converts the active hexamer into an inactive tetramer. The action of NaCl appears to be confined to the Hik2 kinase domain.
| Type: | Article |
|---|---|
| Title: | Oligomeric states in sodium ion-dependent regulation of cyanobacterial histidine kinase-2 |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1007/s00709-017-1196-7 |
| Publisher version: | http://doi.org/10.1007/s00709-017-1196-7 |
| Language: | English |
| Additional information: | Copyright information © The Author(s) 2017 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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. |
| Keywords: | Two-component regulatory system, Sensor histidine kinase, Oligomerisation, Size-exclusion chromatography, Single-particle electron microscopy, Transcriptional regulation, Protein phosphorylation |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Genetics, Evolution and Environment |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10040886 |
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