Protein engineering of bacterial histidine kinase receptor systems
| Autor: | Katherine Y. Blain, Mario Meng-Chiang Kuo, Wei Xie, Senyon Choe |
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| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular Histidine Kinase Recombinant Fusion Proteins Receptors Cell Surface Biology Protein Engineering Biochemistry Signal perception Bacterial Proteins Structural Biology Multienzyme Complexes Two-Hybrid System Techniques Protein phosphorylation Receptor Kinase Escherichia coli Proteins fungi Histidine kinase Membrane Proteins General Medicine Protein engineering Chemoreceptor Cells Cell biology Response regulator Trans-Activators Signal transduction Protein Kinases Bacterial Outer Membrane Proteins Signal Transduction |
| Zdroj: | Protein and peptide letters. 17(7) |
| ISSN: | 1875-5305 |
| Popis: | Two-component systems (TCS) involving the His-Asp phosphotransfer are commonly utilized for signal transduction in prokaryotes in which the two essential components are a sensor histidine kinase (HK) receptor and a response regulator (RR). Despite great efforts in structural and functional characterization of signal perception mechanisms, the exact signaling mechanisms remain elusive for many TCSs. Mimicking the natural TCS signaling pathways, chimeric receptor kinases and response regulators have been constructed through the process of swapping modular domains of related TCSs. To design chimeras with new signaling pathways, domains from different proteins that have little relationship at the primary structural level but carrying desirable functional properties can be conjoined to engineer novel TCSs. These chimeras maintain the ability to respond to environmental stimulants by regulating protein phosphorylation to produce downstream output signals. Depending on the nature of external signals, chimeric TCSs can serve as a novel tool not only to examine the natural signaling mechanisms in TCSs, but also for industrial and clinical applications. |
| Databáze: | OpenAIRE |
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