ArticleJournal of bacteriology2009
The atypical hybrid histidine protein kinase RodK in Myxococcus xanthus: spatial proximity supersedes kinetic preference in phosphotransfer reactions.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- Archaeal Signalling Networks-New Insights Into the Structure and Function of Histidine Kinases and Response Regulators of the Methanogenic Archaeon Methanosarcina acetivorans.Environmental microbiology · 2025Article
- Article
- Azorhizobium caulinodans Chemotaxis Is Controlled by an Unusual Phosphorelay Network.Journal of bacteriology · 2022Article
- A Radical Reimagining of Fungal Two-Component Regulatory Systems.Trends in microbiology · 2021Review
- Evolutionary history expands the range of signaling interactions in hybrid multikinase networks.Scientific reports · 2021Article
- Orphan Hybrid Histidine Protein Kinase SinK Acts as a Signal Integrator To Fine-Tune Multicellular Behavior inJournal of bacteriology · 2019Article
- Cross Talk Inhibition Nullified by a Receiver Domain Missense Substitution.Journal of bacteriology · 2015Article
- Phosphate flow between hybrid histidine kinases CheA₃ and CheS₃ controls Rhodospirillum centenum cyst formation.PLoS genetics · 2013Article
- Intra- and interprotein phosphorylation between two-hybrid histidine kinases controls Myxococcus xanthus developmental progression.The Journal of biological chemistry · 2012Article
- The orphan histidine protein kinase SgmT is a c-di-GMP receptor and regulates composition of the extracellular matrix together with the orphan DNA binding response regulator DigR in Myxococcus xanthus.Molecular microbiology · 2012Article
- The genetic organisation of prokaryotic two-component system signalling pathways.BMC genomics · 2010Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many proteins of two-component signal transduction systems (TCS) have domain structures that do not comply with a phosphate flow as observed in linear TCS, phosphorelays, or simple branched pathways. An example is RodK, which is essential for fruiting body formation in Myxococcus xanthus and, in addition to a sensor domain, consists of a kinase domain and three receiver domains (RodK-R1, -R2, and -R3), all of which are functionally important. We identified the RokA response regulator as part of the RodK pathway. In vitro the isolated RodK kinase domain engages in phosphotransfer to RodK-R3 and RokA, with a kinetic preference for RokA. However, in the context of the full-length protein, the RodK kinase domain has a preference for phosphotransfer to RodK-R3 over RokA. We suggest that in full-length RodK, the spatial proximity of the RodK kinase domain and RodK-R3 compensate for the kinetic preference of the isolated kinase domain for RokA. Thus, the kinetic preference observed using an isolated kinase domain of a hybrid kinase does not necessarily reflect the phosphotransfer preference of the full-length protein. We speculate that the phosphorylation status of RodK-R1 and RodK-R2 determines whether RodK engages in phosphotransfer to RodK-R3 or RokA in vivo.
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