Abstract
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.
Keywords: Chimera, histidine kinase, phosphotransfer, protein engineering, response regulator, signal transduction, two-component system
Protein & Peptide Letters
Title: Protein Engineering of Bacterial Histidine Kinase Receptor Systems
Volume: 17 Issue: 7
Author(s): Wei Xie, Katherine Y. Blain, Mario Meng-Chiang Kuo and Senyon Choe
Affiliation:
Keywords: Chimera, histidine kinase, phosphotransfer, protein engineering, response regulator, signal transduction, two-component system
Abstract: 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.
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Cite this article as:
Xie Wei, Y. Blain Katherine, Meng-Chiang Kuo Mario and Choe Senyon, Protein Engineering of Bacterial Histidine Kinase Receptor Systems, Protein & Peptide Letters 2010; 17 (7) . https://dx.doi.org/10.2174/092986610791306706
DOI https://dx.doi.org/10.2174/092986610791306706 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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