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Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
Published on: January 11, 2017
Histidine kinases from bacteria to humans
1School of Chemistry and Biochemistry, University of Western Australia, Crawley, WA 6009, Australia. paul.attwood@uwa.edu.au
Biochemical Society Transactions
|July 19, 2013
Summary
Protein histidine phosphorylation, though discovered decades ago, is gaining recognition. Recent findings suggest operational two-component histidine kinase systems likely exist in higher eukaryotes, including mammals.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Signaling
Background:
- Protein histidine phosphorylation was first identified in 1962.
- Histidine kinases are less understood compared to serine/threonine and tyrosine kinases.
- Two-component signaling systems are well-characterized in bacteria, fungi, and plants.
Purpose of the Study:
- To investigate the presence and role of histidine kinases in higher eukaryotes.
- To explore the mechanisms and functions of protein histidine phosphorylation in mammals.
- To identify novel histidine kinases and their substrates in eukaryotic organisms.
Main Methods:
- Comparative genomics of eukaryotic genomes.
- Analysis of protein sequences for histidine kinase domains.
- Biochemical assays to detect and characterize protein histidine phosphorylation.
- Proteomic studies to identify mammalian histidine kinases and their targets.
Main Results:
- Evidence suggests that two-component histidine kinase systems are present in higher eukaryotes.
- Direct evidence confirms protein histidine phosphorylation occurs in mammals.
- Nucleoside diphosphate kinases are implicated, but other histidine kinases are yet to be identified.
Conclusions:
- Operational two-component histidine kinase systems are likely functional in higher eukaryotes.
- Protein histidine phosphorylation may play significant roles in mammalian cellular processes.
- Further research is needed to identify all mammalian histidine kinases and elucidate their functions.
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