Optimized assay for the quantification of histidine kinase autophosphorylation
| Autor: | Takahiro B. Ueno, Elizabeth M. Boon, Roger A. Johnson |
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| Rok vydání: | 2015 |
| Předmět: |
Binding Sites
Histidine Kinase biology Kinase Autophosphorylation Histidine kinase Biophysics Cell Biology biology.organism_classification Biochemistry Legionella pneumophila Enzyme Activation Response regulator Bacterial Proteins Protein Interaction Mapping Autoradiography Phosphorylation Biological Assay Shewanella oneidensis Protein Kinases Molecular Biology Histidine Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 465:331-337 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2015.07.121 |
| Popis: | Although two-component signaling systems, comprising a sensory histidine kinase and a response regulator, are a primary means by which bacteria detect and respond to environmental stimuli, they are poorly characterized. Here we report optimized conditions for detecting histidine phosphorylation using a facile medium-throughput filter paper-binding assay. Employing this assay we report the kinetic parameters of previously uncharacterized histidine kinases from Vibrio haveyi, Vibrio parahaemolytius, Shewanella oneidensis, and Legionella pneumophila. In characterizing these kinases, we effectively double the number of kinetically characterized histidine kinases that have been reported in the literature. |
| Databáze: | OpenAIRE |
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