Light-regulated tetracycline binding to the Tet repressor = 빛을 이용한 DNA 결합 조절 기술

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Title
Light-regulated tetracycline binding to the Tet repressor = 빛을 이용한 DNA 결합 조절 기술
Author(s)
J Moon; Jongsik Gam; Seung Goo Lee; Y G Suh; J Lee
Bibliographic Citation
Chemistry-A European Journal, vol. 20, no. 9, pp. 2508-2514
Publication Year
2014
Abstract
Elucidation of the signal-transmission pathways between distant sites within proteins is of great importance in medical and bioengineering sciences. The use of optical methods to redesign protein functions is emerging as a general approach for the control of biological systems with high spatiotemporal precision. Here we report the detailed thermodynamic and kinetic characterization of novel chimeric light-regulated Tet repressor (TetR) switches in which light modulates the TetR function. Light absorbed by flavin mononucleotide (FMN) generates a signal that is transmitted to As-LOV and YtvA-LOV fused TetR proteins (LOV=light-oxygen-voltage), in which it alters the binding to tetracycline, the TetR ligand. The engineering of light-sensing protein modules with TetR is a valuable tool that deepens our understanding of the mechanism of signal transmission within proteins. In addition, the light-regulated changes of drug binding that we describe here suggest that engineered light-sensitive proteins may be used for the development of novel therapeutic strategies. Tet-a-tet: Light absorbed by flavin mononucleotide (FMN) generates a signal that is transmitted to the light-oxygen-voltage (LOV) domain fused Tet repressor proteins (see figure), in which it alters the binding to tetracycline, thereby controlling the tetO DNA binding affinity.
Keyword
antibioticsDNALOV domainnucleotidesproteinstetracyclinethermodynamics
ISSN
0947-6539
Publisher
Wiley
DOI
http://dx.doi.org/10.1002/chem.201304027
Type
Article
Appears in Collections:
Synthetic Biology and Bioengineering Research Institute > 1. Journal Articles
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