ArticlePLoS computational biology2013
Split histidine kinases enable ultrasensitivity and bistability in two-component signaling networks.
Article in PLoS computational biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 21 citations in OpenAlex.
- A General Approach for the Modelling of Negative Feedback Physiological Control Systems.Bioengineering (Basel, Switzerland) · 2023Article
- Exploring the mono-/bistability range of positively autoregulated signaling systems in the presence of competing transcription factor binding sites.PLoS computational biology · 2022Article
- Multiple communication mechanisms between sensor kinases are crucial for virulence in Pseudomonas aeruginosa.Nature communications · 2018Article
- Molecular and cellular factors control signal transduction via switchable allosteric modulator proteins (SAMPs).BMC systems biology · 2016Article
- Ultrasensitive Negative Feedback Control: A Natural Approach for the Design of Synthetic Controllers.PloS one · 2016Article
- Logical-continuous modelling of post-translationally regulated bistability of curli fiber expression in Escherichia coli.BMC systems biology · 2015Article
- Unlimited multistability and Boolean logic in microbial signalling.Journal of the Royal Society, Interface · 2015Article
- A minimal model for metabolism-dependent chemotaxis in Rhodobacter sphaeroides (†).Interface focus · 2014Article
- Phosphate sink containing two-component signaling systems as tunable threshold devices.PLoS computational biology · 2014Article
- A novel signal transduction pathway that modulates rhl quorum sensing and bacterial virulence in Pseudomonas aeruginosa.PLoS pathogens · 2014Article
- Reciprocal regulation as a source of ultrasensitivity in two-component systems with a bifunctional sensor kinase.PLoS computational biology · 2014Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria sense and respond to their environment through signaling cascades generally referred to as two-component signaling networks. These networks comprise histidine kinases and their cognate response regulators. Histidine kinases have a number of biochemical activities: ATP binding, autophosphorylation, the ability to act as a phosphodonor for their response regulators, and in many cases the ability to catalyze the hydrolytic dephosphorylation of their response regulator. Here, we explore the functional role of "split kinases" where the ATP binding and phosphotransfer activities of a conventional histidine kinase are split onto two distinct proteins that form a complex. We find that this unusual configuration can enable ultrasensitivity and bistability in the signal-response relationship of the resulting system. These dynamics are displayed under a wide parameter range but only when specific biochemical requirements are met. We experimentally show that one of these requirements, namely segregation of the phosphatase activity predominantly onto the free form of one of the proteins making up the split kinase, is met in Rhodobacter sphaeroides. These findings indicate split kinases as a bacterial alternative for enabling ultrasensitivity and bistability in signaling networks. Genomic analyses reveal that up 1.7% of all identified histidine kinases have the potential to be split and bifunctional.
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