In: PLOS ONE
9(2), e89671
[PDF, 2MB]
Abstract
KdpD and KdpE form a histidine kinase/response regulator system that senses K+ limitation and induces the kdpFABC operon, which encodes a high-affinity K+ uptake complex. To define the primary stimulus perceived by KdpD we focused in this study on the dynamics of the Kdp response. Escherichia coli cells were subjected to severe K+ limitation, and all relevant parameters of the Kdp response, i.e.,levels of kdpFABC transcripts and KdpFABC proteins, as well as extra-and intracellular K+ concentrations, were quantitatively analysed over time (0 to 180 min). Unexpectedly, induction of kdpFABC was found to follow a non-monotonic time-course. To interpret this unusual behaviour, a mathematical model that adequately captures the dynamics of the Kdp system was established and used for simulations. We found a strong correlation between KdpD/KdpE activation and the intracellular K+ concentration, which is influenced by the uptake of K+ via the KdpFABC complex. Based on these results a model is proposed in which KdpD/KdpE phosphorylation is inversely correlated with the intracellular K+ concentration. To corroborate this hypothesis an isogenic mutant that produces a defective KdpFABC complex, and the trans-complemented mutant that expresses the KtrAB high-affinity K+ uptake system of Vibrio alginolyticus were quantitatively analysed. Experimental data and simulations for the mutants consistently support the tight correlation between KdpD/KdpE activation and the intracellular K+ concentration. This study presents a striking example of the non-intuitive dynamics of a functional unit comprising signalling proteins and a transporter with K+ as mediator.
Dokumententyp: | Zeitschriftenartikel |
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Fakultät: | Biologie > Department Biologie I |
Themengebiete: | 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften; Biologie |
URN: | urn:nbn:de:bvb:19-epub-33735-1 |
ISSN: | 1932-6203 |
Sprache: | Englisch |
Dokumenten ID: | 33735 |
Datum der Veröffentlichung auf Open Access LMU: | 15. Feb. 2017, 14:45 |
Letzte Änderungen: | 04. Nov. 2020, 13:11 |