Journal article

Phosphorelay of non-orthodox two component systems functions through a bi-molecular mechanism in vivo: the case of ArcB

Goran Jovanovic, Xia Sheng, Angelique Ale, Elisenda Feliu, Heather A Harrington, Paul Kirk, Carsten Wiuf, Martin Buck, Michael PH Stumpf



Two-component systems play a central part in bacterial signal transduction. Phosphorelay mechanisms have been linked to more robust and ultra-sensitive signalling dynamics. The molecular machinery that facilitates such a signalling is, however, only understood in outline. In particular the functional relevance of the dimerization of a non-orthodox or hybrid histidine kinase along which the phosphorelay takes place has been a subject of debate. We use a combination of molecular and genetic approaches, coupled to mathematical and statistical modelling, to demonstrate that the different possible intra- and inter-molecular mechanisms of phosphotransfer are formally non-identifiable in Escherichi..

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University of Melbourne Researchers


Awarded by Biotechnology and Biological Sciences Research Council

Awarded by Engineering and Physical Sciences Research Council

Awarded by Lundbeck Foundation

Awarded by Medical Research Council

Funding Acknowledgements

We thank P. Mehta for technical help, C. Georgelis for ArcB antibodies, J. Beckwith for plasmids, M. Bekker for strains, and D. Ladant for providing strains and plasmids. We gratefully acknowlegde financial support from the BBSRC, MRC, the Kwok Foundation, the Wellcome Trust and the Leverhulme Trust. Finally, we thank two anonymous referees for their comments which have helped in improving the manuscript.